HEADER HYDROLASE 26-JUN-08 3DL7

TITLE AGED FORM OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY TABUN-

TITLE 2 UPDATE

COMPND MOL_ID: 1;

COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;

COMPND 3 CHAIN: A, B;

COMPND 4 FRAGMENT: UNP RESIDUES 32-576;

COMPND 5 SYNONYM: ACHE;

COMPND 6 EC: 3.1.1.7 <http://www.expasy.org/cgi-bin/nicezyme.pl?3.1.1.7>;

COMPND 7 ENGINEERED: YES

SOURCE MOL_ID: 1;

SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;

SOURCE 3 ORGANISM_COMMON: MOUSE;

SOURCE 4 ORGANISM_TAXID: 10090;

SOURCE 5 GENE: ACHE;

SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;

SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;

SOURCE 8 EXPRESSION_SYSTEM_STRAIN: HEK293F;

SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;

SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PCDNA3.1

KEYWDS HYDROLASE, TABUN, ORGANOPHOSPHATE, AGING, ALTERNATIVE

KEYWDS 2 SPLICING, CELL JUNCTION, GLYCOPROTEIN, GPI-ANCHOR,

KEYWDS 3 LIPOPROTEIN, MEMBRANE, NEUROTRANSMITTER DEGRADATION,

KEYWDS 4 SECRETED, SERINE ESTERASE, SYNAPSE

EXPDTA X-RAY DIFFRACTION

AUTHOR E.CARLETTI,H.LI,B.LI,F.EKSTROM,Y.NICOLET,M.LOIODICE,

AUTHOR 2 E.GILLON,M.T.FROMENT,O.LOCKRIDGE,L.M.SCHOPFER,P.MASSON,

AUTHOR 3 F.NACHON

REVDAT 1 02-DEC-08 3DL7 0

JRNL AUTH E.CARLETTI,H.LI,B.LI,F.EKSTROM,Y.NICOLET,

JRNL AUTH 2 M.LOIODICE,E.GILLON,M.T.FROMENT,O.LOCKRIDGE,

JRNL AUTH 3 L.M.SCHOPFER,P.MASSON,F.NACHON

JRNL TITL AGING OF CHOLINESTERASES PHOSPHYLATED BY TABUN

JRNL TITL 2 PROCEEDS THROUGH O-DEALKYLATION.

JRNL REF J.AM.CHEM.SOC. V. 130 16011 2008

JRNL REFN ISSN 0002-7863

JRNL PMID 18975951

JRNL DOI 10.1021/JA804941Z

REMARK 1

REMARK 2

REMARK 2 RESOLUTION. 2.50 ANGSTROMS.

REMARK 3

REMARK 3 REFINEMENT.

REMARK 3 PROGRAM : REFMAC 5.2.0019

REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON

REMARK 3

REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD

REMARK 3

REMARK 3 DATA USED IN REFINEMENT.

REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50

REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.82

REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000

REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2

REMARK 3 NUMBER OF REFLECTIONS : 69037

REMARK 3

REMARK 3 FIT TO DATA USED IN REFINEMENT.

REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT

REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM

REMARK 3 R VALUE (WORKING + TEST SET) : 0.188

REMARK 3 R VALUE (WORKING SET) : 0.187

REMARK 3 FREE R VALUE : 0.227

REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.000

REMARK 3 FREE R VALUE TEST SET COUNT : 1381

REMARK 3

REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.

REMARK 3 TOTAL NUMBER OF BINS USED : 20

REMARK 3 BIN RESOLUTION RANGE HIGH : 2.50

REMARK 3 BIN RESOLUTION RANGE LOW : 2.56

REMARK 3 REFLECTION IN BIN (WORKING SET) : 4887

REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.79

REMARK 3 BIN R VALUE (WORKING SET) : 0.2910

REMARK 3 BIN FREE R VALUE SET COUNT : 104

REMARK 3 BIN FREE R VALUE : 0.3540

REMARK 3

REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.

REMARK 3 ALL ATOMS : 8926

REMARK 3

REMARK 3 B VALUES.

REMARK 3 FROM WILSON PLOT (A**2) : NULL

REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.69

REMARK 3 OVERALL ANISOTROPIC B VALUE.

REMARK 3 B11 (A**2) : NULL

REMARK 3 B22 (A**2) : NULL

REMARK 3 B33 (A**2) : NULL

REMARK 3 B12 (A**2) : NULL

REMARK 3 B13 (A**2) : NULL

REMARK 3 B23 (A**2) : NULL

REMARK 3

REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.

REMARK 3 ESU BASED ON R VALUE (A): 0.249

REMARK 3 ESU BASED ON FREE R VALUE (A): 0.208

REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.150

REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.892

REMARK 3

REMARK 3 CORRELATION COEFFICIENTS.

REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954

REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.932

REMARK 3

REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT

REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8735 ; 0.013 ; 0.022

REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL

REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11943 ; 1.461 ; 1.963

REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL

REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1078 ; 6.473 ; 5.000

REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 402 ;33.485 ;22.761

REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1268 ;17.585 ;15.000

REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 75 ;20.097 ;15.000

REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1281 ; 0.097 ; 0.200

REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6867 ; 0.005 ; 0.020

REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL

REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4609 ; 0.218 ; 0.200

REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL

REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 6024 ; 0.315 ; 0.200

REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL

REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 591 ; 0.147 ; 0.200

REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL

REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL

REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL

REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 40 ; 0.203 ; 0.200

REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL

REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 11 ; 0.204 ; 0.200

REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL

REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL

REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL

REMARK 3

REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT

REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 5461 ; 0.776 ; 1.500

REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL

REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8661 ; 1.355 ; 2.000

REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3713 ; 1.792 ; 3.000

REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3277 ; 2.901 ; 4.500

REMARK 3

REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT

REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL

REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL

REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL

REMARK 3

REMARK 3 NCS RESTRAINTS STATISTICS

REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL

REMARK 3

REMARK 3 TLS DETAILS

REMARK 3 NUMBER OF TLS GROUPS : NULL

REMARK 3

REMARK 3 BULK SOLVENT MODELLING.

REMARK 3 METHOD USED : BABINET MODEL WITH MASK

REMARK 3 PARAMETERS FOR MASK CALCULATION

REMARK 3 VDW PROBE RADIUS : 1.20

REMARK 3 ION PROBE RADIUS : 0.80

REMARK 3 SHRINKAGE RADIUS : 0.80

REMARK 3

REMARK 3 OTHER REFINEMENT REMARKS: NULL

REMARK 4

REMARK 4 3DL7 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08

REMARK 100

REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUN-08.

REMARK 100 THE RCSB ID CODE IS RCSB048176.

REMARK 200

REMARK 200 EXPERIMENTAL DETAILS

REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION

REMARK 200 DATE OF DATA COLLECTION : 08-MAR-05

REMARK 200 TEMPERATURE (KELVIN) : 100

REMARK 200 PH : 7.0

REMARK 200 NUMBER OF CRYSTALS USED : 1

REMARK 200

REMARK 200 SYNCHROTRON (Y/N) : Y

REMARK 200 RADIATION SOURCE : MAX II

REMARK 200 BEAMLINE : I711

REMARK 200 X-RAY GENERATOR MODEL : NULL

REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M

REMARK 200 WAVELENGTH OR RANGE (A) : 0.9694

REMARK 200 MONOCHROMATOR : NULL

REMARK 200 OPTICS : NULL

REMARK 200

REMARK 200 DETECTOR TYPE : CCD

REMARK 200 DETECTOR MANUFACTURER : MAR CCD

REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS

REMARK 200 DATA SCALING SOFTWARE : SCALA

REMARK 200

REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 69074

REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500

REMARK 200 RESOLUTION RANGE LOW (A) : 29.000

REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000

REMARK 200

REMARK 200 OVERALL.

REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3

REMARK 200 DATA REDUNDANCY : 7.400

REMARK 200 R MERGE (I) : 0.07000

REMARK 200 R SYM (I) : NULL

REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.6000

REMARK 200

REMARK 200 IN THE HIGHEST RESOLUTION SHELL.

REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50

REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64

REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0

REMARK 200 DATA REDUNDANCY IN SHELL : 7.50

REMARK 200 R MERGE FOR SHELL (I) : 0.51000

REMARK 200 R SYM FOR SHELL (I) : NULL

REMARK 200 <I/SIGMA(I)> FOR SHELL : 7.500

REMARK 200

REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH

REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT

REMARK 200 SOFTWARE USED: MOLREP

REMARK 200 STARTING MODEL: NULL

REMARK 200

REMARK 200 REMARK: NULL

REMARK 280

REMARK 280 CRYSTAL

REMARK 280 SOLVENT CONTENT, VS (%): 70.06

REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.11

REMARK 280

REMARK 280 CRYSTALLIZATION CONDITIONS: 27-31 % (V/V) PEG750MME, 0.1M

REMARK 280 HEPES, 100 MM HEPES, PH 7.0, VAPOR DIFFUSION, HANGING DROP,

REMARK 280 TEMPERATURE 277K

REMARK 290

REMARK 290 CRYSTALLOGRAPHIC SYMMETRY

REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21

REMARK 290

REMARK 290 SYMOP SYMMETRY

REMARK 290 NNNMMM OPERATOR

REMARK 290 1555 X,Y,Z

REMARK 290 2555 -X+1/2,-Y,Z+1/2

REMARK 290 3555 -X,Y+1/2,-Z+1/2

REMARK 290 4555 X+1/2,-Y+1/2,-Z

REMARK 290

REMARK 290 WHERE NNN -> OPERATOR NUMBER

REMARK 290 MMM -> TRANSLATION VECTOR

REMARK 290

REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS

REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM

REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY

REMARK 290 RELATED MOLECULES.

REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000

REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000

REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000

REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 39.51000

REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000

REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 113.19000

REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000

REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.44000

REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 113.19000

REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.51000

REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.44000

REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000

REMARK 290

REMARK 290 REMARK: NULL

REMARK 300

REMARK 300 BIOMOLECULE: 1

REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM

REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN

REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON

REMARK 300 BURIED SURFACE AREA.

REMARK 350

REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN

REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE

REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS

REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND

REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.

REMARK 350

REMARK 350 BIOMOLECULE: 1

REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC

REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B

REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000

REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000

REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000

REMARK 465

REMARK 465 MISSING RESIDUES

REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE

REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN

REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)

REMARK 465

REMARK 465 M RES C SSSEQI

REMARK 465 PRO A 259

REMARK 465 GLY A 260

REMARK 465 GLY A 261

REMARK 465 ALA A 262

REMARK 465 GLY A 263

REMARK 465 GLY A 264

REMARK 465 ALA A 544

REMARK 465 THR A 545

REMARK 465 GLU A 546

REMARK 465 ALA A 547

REMARK 465 PRO A 548

REMARK 465 GLU B 1

REMARK 465 GLY B 2

REMARK 465 ARG B 3

REMARK 465 PRO B 258

REMARK 465 PRO B 259

REMARK 465 GLY B 260

REMARK 465 GLY B 261

REMARK 465 ALA B 262

REMARK 465 GLY B 263

REMARK 465 GLY B 264

REMARK 465 LYS B 496

REMARK 465 THR B 545

REMARK 465 GLU B 546

REMARK 465 ALA B 547

REMARK 465 PRO B 548

REMARK 470

REMARK 470 MISSING ATOM

REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;

REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;

REMARK 470 I=INSERTION CODE):

REMARK 470 M RES CSSEQI ATOMS

REMARK 470 LYS A 496 CG CD CE NZ

REMARK 470 SER B 497 OG

REMARK 470 ALA B 544 CA C O CB

REMARK 500

REMARK 500 GEOMETRY AND STEREOCHEMISTRY

REMARK 500 SUBTOPIC: COVALENT BOND ANGLES

REMARK 500

REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES

REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE

REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN

REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).

REMARK 500

REMARK 500 STANDARD TABLE:

REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)

REMARK 500

REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999

REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996

REMARK 500

REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3

REMARK 500 LEU A 161 CA - CB - CG ANGL. DEV. = -15.3 DEGREES

REMARK 500

REMARK 500 REMARK: NULL

REMARK 500

REMARK 500 GEOMETRY AND STEREOCHEMISTRY

REMARK 500 SUBTOPIC: TORSION ANGLES

REMARK 500

REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:

REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;

REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).

REMARK 500

REMARK 500 STANDARD TABLE:

REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)

REMARK 500

REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-

REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400

REMARK 500

REMARK 500 M RES CSSEQI PSI PHI

REMARK 500 PHE A 47 -9.01 75.37

REMARK 500 PRO A 104 163.07 -49.27

REMARK 500 ALA A 127 140.37 -172.51

REMARK 500 PHE A 158 -5.05 -140.89

REMARK 500 ASN A 170 17.62 55.83

REMARK 500 ASP A 306 -88.94 -130.91

REMARK 500 SER A 371 -174.77 -60.83

REMARK 500 VAL A 407 -65.73 -129.74

REMARK 500 ASN A 464 10.98 82.23

REMARK 500 ASP A 494 120.54 169.69

REMARK 500 SER A 541 -86.14 -60.80

REMARK 500 ALA A 542 51.58 -69.10

REMARK 500 PHE B 47 -2.59 71.19

REMARK 500 ALA B 62 58.34 -115.87

REMARK 500 PRO B 111 117.56 -37.81

REMARK 500 ALA B 167 68.45 -150.51

REMARK 500 ASP B 306 -78.60 -123.24

REMARK 500 ASP B 323 53.54 -103.45

REMARK 500 TYR B 341 34.29 -95.21

REMARK 500 ASN B 350 -129.38 -104.35

REMARK 500 LEU B 353 92.62 -67.19

REMARK 500 VAL B 407 -62.46 -123.02

REMARK 500 GLN B 421 32.17 -99.97

REMARK 500 PRO B 492 57.61 -114.71

REMARK 500 ASP B 494 -155.95 -78.27

REMARK 500 ASN B 514 -169.11 -161.52

REMARK 500 SER B 541 24.07 -69.10

REMARK 500 THR B 543 86.45 35.04

REMARK 500

REMARK 500 REMARK: NULL

REMARK 525

REMARK 525 SOLVENT

REMARK 525

REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT

REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST

REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT

REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE

REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;

REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE

REMARK 525 NUMBER; I=INSERTION CODE):

REMARK 525

REMARK 525 M RES CSSEQI

REMARK 525 HOH B 704 DISTANCE = 5.62 ANGSTROMS

REMARK 800

REMARK 800 SITE

REMARK 800 SITE_IDENTIFIER: AC1

REMARK 800 EVIDENCE_CODE: SOFTWARE

REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 549

REMARK 800 SITE_IDENTIFIER: AC2

REMARK 800 EVIDENCE_CODE: SOFTWARE

REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 550

REMARK 800 SITE_IDENTIFIER: AC3

REMARK 800 EVIDENCE_CODE: SOFTWARE

REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P6G A 551

REMARK 800 SITE_IDENTIFIER: AC4

REMARK 800 EVIDENCE_CODE: SOFTWARE

REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B 549

REMARK 900

REMARK 900 RELATED ENTRIES

REMARK 900 RELATED ID: 2C0P RELATED DB: PDB

REMARK 900 AGED FORM OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY TABUN

REMARK 900 - SAME DATASET WITH OLDER REFINEMENT.

REMARK 900 RELATED ID: 2C0Q RELATED DB: PDB

REMARK 900 NON-AGED FORM OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY

REMARK 900 TABUN - OLDER REFINEMENT

REMARK 900 RELATED ID: 3DKK RELATED DB: PDB

REMARK 900 AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY TABUN.

REMARK 900 RELATED ID: 3DJY RELATED DB: PDB

REMARK 900 NON-AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY

REMARK 900 TABUN.

REMARK 900 RELATED ID: 3DL4 RELATED DB: PDB

REMARK 900 NON-AGED FORM OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY

REMARK 900 TABUN.

REMARK 999

REMARK 999 SEQUENCE

REMARK 999 THE C-TERMINAL PART WAS ENGINEERED TO GET MONOMERIC ENZYME.

DBREF 3DL7 A 1 543 UNP P21836 ACES_MOUSE <http://www.expasy.org/cgi-bin/niceprot.pl?ACES_MOUSE > 32 574

DBREF 3DL7 B 1 543 UNP P21836 ACES_MOUSE <http://www.expasy.org/cgi-bin/niceprot.pl?ACES_MOUSE > 32 574

SEQADV 3DL7 SEN A 203 UNP P21836 SER 234 MICROHETEROGENEITY

SEQADV 3DL7 SUN A 203 UNP P21836 SER 234 MICROHETEROGENEITY

SEQADV 3DL7 ALA A 544 UNP P21836 SEE REMARK 999

SEQADV 3DL7 THR A 545 UNP P21836 SEE REMARK 999

SEQADV 3DL7 GLU A 546 UNP P21836 SEE REMARK 999

SEQADV 3DL7 ALA A 547 UNP P21836 SEE REMARK 999

SEQADV 3DL7 PRO A 548 UNP P21836 SEE REMARK 999

SEQADV 3DL7 SEN B 203 UNP P21836 SER 234 MICROHETEROGENEITY

SEQADV 3DL7 SUN B 203 UNP P21836 SER 234 MICROHETEROGENEITY

SEQADV 3DL7 ALA B 544 UNP P21836 SEE REMARK 999

SEQADV 3DL7 THR B 545 UNP P21836 SEE REMARK 999

SEQADV 3DL7 GLU B 546 UNP P21836 SEE REMARK 999

SEQADV 3DL7 ALA B 547 UNP P21836 SEE REMARK 999

SEQADV 3DL7 PRO B 548 UNP P21836 SEE REMARK 999

SEQRES 1 A 548 GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG

SEQRES 2 A 548 GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY

SEQRES 3 A 548 GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU

SEQRES 4 A 548 PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO

SEQRES 5 A 548 LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE

SEQRES 6 A 548 GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO

SEQRES 7 A 548 GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU

SEQRES 8 A 548 LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO

SEQRES 9 A 548 TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP

SEQRES 10 A 548 ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU

SEQRES 11 A 548 ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY

SEQRES 12 A 548 ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE

SEQRES 13 A 548 GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY

SEQRES 14 A 548 ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP

SEQRES 15 A 548 VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET

SEQRES 16 A 548 SER VAL THR LEU PHE GLY GLU SEN ALA GLY ALA ALA SER

SEQRES 17 A 548 VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU

SEQRES 18 A 548 PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY

SEQRES 19 A 548 PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG

SEQRES 20 A 548 ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY

SEQRES 21 A 548 GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU

SEQRES 22 A 548 ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP

SEQRES 23 A 548 HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE

SEQRES 24 A 548 VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO

SEQRES 25 A 548 GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN

SEQRES 26 A 548 VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE

SEQRES 27 A 548 LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU

SEQRES 28 A 548 SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG

SEQRES 29 A 548 ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA

SEQRES 30 A 548 VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP

SEQRES 31 A 548 PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY

SEQRES 32 A 548 ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY

SEQRES 33 A 548 ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE

SEQRES 34 A 548 PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP

SEQRES 35 A 548 MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE

SEQRES 36 A 548 GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU

SEQRES 37 A 548 GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR

SEQRES 38 A 548 ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP

SEQRES 39 A 548 SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA

SEQRES 40 A 548 GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL

SEQRES 41 A 548 ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN

SEQRES 42 A 548 ARG PHE LEU PRO LYS LEU LEU SER ALA THR ALA THR GLU

SEQRES 43 A 548 ALA PRO

SEQRES 1 B 548 GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG

SEQRES 2 B 548 GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY

SEQRES 3 B 548 GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU

SEQRES 4 B 548 PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO

SEQRES 5 B 548 LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE

SEQRES 6 B 548 GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO

SEQRES 7 B 548 GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU

SEQRES 8 B 548 LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO

SEQRES 9 B 548 TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP

SEQRES 10 B 548 ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU

SEQRES 11 B 548 ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY

SEQRES 12 B 548 ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE

SEQRES 13 B 548 GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY

SEQRES 14 B 548 ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP

SEQRES 15 B 548 VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET

SEQRES 16 B 548 SER VAL THR LEU PHE GLY GLU SEN ALA GLY ALA ALA SER

SEQRES 17 B 548 VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU

SEQRES 18 B 548 PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY

SEQRES 19 B 548 PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG

SEQRES 20 B 548 ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY

SEQRES 21 B 548 GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU

SEQRES 22 B 548 ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP

SEQRES 23 B 548 HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE

SEQRES 24 B 548 VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO

SEQRES 25 B 548 GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN

SEQRES 26 B 548 VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE

SEQRES 27 B 548 LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU

SEQRES 28 B 548 SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG

SEQRES 29 B 548 ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA

SEQRES 30 B 548 VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP

SEQRES 31 B 548 PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY

SEQRES 32 B 548 ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY

SEQRES 33 B 548 ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE

SEQRES 34 B 548 PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP

SEQRES 35 B 548 MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE

SEQRES 36 B 548 GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU

SEQRES 37 B 548 GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR

SEQRES 38 B 548 ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP

SEQRES 39 B 548 SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA

SEQRES 40 B 548 GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL

SEQRES 41 B 548 ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN

SEQRES 42 B 548 ARG PHE LEU PRO LYS LEU LEU SER ALA THR ALA THR GLU

SEQRES 43 B 548 ALA PRO

MODRES 3DL7 ASN A 464 ASN GLYCOSYLATION SITE

MODRES 3DL7 SEN A 203 SER

MODRES 3DL7 SUN A 203 SER

MODRES 3DL7 SEN B 203 SER

MODRES 3DL7 SUN B 203 SER

HET SEN <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-het?SEN> A 203 12

HET SUN <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-het?SUN> A 203 14

HET SEN <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-het?SEN> B 203 12

HET SUN <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-het?SUN> B 203 14

HET NAG <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-het?NAG> A 549 14

HET CL <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-het?CL> A 550 1

HET P6G <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-het?P6G> A 551 19

HET PG4 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-het?PG4> B 549 13

HETNAM SEN O-[N,N-DIMETHYLPHOSPHORAMIDATE]-L-SERINE

HETNAM SUN O-[(R)-(DIMETHYLAMINO)(ETHOXY)PHOSPHORYL]-L-SERINE

HETNAM NAG N-ACETYL-D-GLUCOSAMINE

HETNAM CL CHLORIDE ION

HETNAM P6G HEXAETHYLENE GLYCOL

HETNAM PG4 TETRAETHYLENE GLYCOL

HETSYN SUN TABUN CONJUGATED SERINE

HETSYN NAG NAG

HETSYN P6G POLYETHYLENE GLYCOL PEG400

FORMUL 1 SEN 2(C5 H13 N2 O5 P)

FORMUL 1 SUN 2(C7 H17 N2 O5 P)

FORMUL 3 NAG C8 H15 N O6

FORMUL 4 CL CL 1-

FORMUL 5 P6G C12 H26 O7

FORMUL 6 PG4 C8 H18 O5

FORMUL 7 HOH *439(H2 O)

HELIX 1 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=ASP:A:+++5:GLN:A:+++7> 1 ASP A 5 GLN A 7 5 3

HELIX 2 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=VAL:A:++42:ARG:A:++46> 2 VAL A 42 ARG A 46 5 5

HELIX 3 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=PHE:A:++80:MET:A:++85> 3 PHE A 80 MET A 85 1 6

HELIX 4 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=LEU:A:+130:ASP:A:+134> 4 LEU A 130 ASP A 134 5 5

HELIX 5 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=GLY:A:+135:GLY:A:+143> 5 GLY A 135 GLY A 143 1 9

HELIX 6 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=VAL:A:+153:LEU:A:+159> 6 VAL A 153 LEU A 159 1 7

HELIX 7 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=ASN:A:+170:ILE:A:+187> 7 ASN A 170 ILE A 187 1 18

HELIX 8 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=ALA:A:+188:PHE:A:+190> 8 ALA A 188 PHE A 190 5 3

HELIX 9 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=SEN:A:+203:LEU:A:+214> 9 SEN A 203 LEU A 214 1 12

HELIX 10 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=SER:A:+215:SER:A:+220> 10 SER A 215 SER A 220 1 6

HELIX 11 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=ALA:A:+241:VAL:A:+255> 11 ALA A 241 VAL A 255 1 15

HELIX 12 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=ASN:A:+265:THR:A:+275> 12 ASN A 265 THR A 275 1 11

HELIX 13 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=PRO:A:+277:TRP:A:+286> 13 PRO A 277 TRP A 286 1 10

HELIX 14 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=HIS:A:+287:LEU:A:+289> 14 HIS A 287 LEU A 289 5 3

HELIX 15 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=THR:A:+311:GLY:A:+319> 15 THR A 311 GLY A 319 1 9

HELIX 16 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=GLY:A:+335:VAL:A:+343> 16 GLY A 335 VAL A 343 1 9

HELIX 17 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=SER:A:+355:VAL:A:+367> 17 SER A 355 VAL A 367 1 13

HELIX 18 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=SER:A:+371:THR:A:+383> 18 SER A 371 THR A 383 1 13

HELIX 19 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=ASP:A:+390:VAL:A:+407> 19 ASP A 390 VAL A 407 1 18

HELIX 20 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=VAL:A:+407:GLN:A:+421> 20 VAL A 407 GLN A 421 1 15

HELIX 21 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=PRO:A:+440:GLY:A:+444> 21 PRO A 440 GLY A 444 5 5

HELIX 22 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=GLU:A:+450:PHE:A:+455> 22 GLU A 450 PHE A 455 1 6

HELIX 23 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=GLY:A:+456:ASN:A:+464> 23 GLY A 456 ASN A 464 5 9

HELIX 24 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=THR:A:+466:GLY:A:+487> 24 THR A 466 GLY A 487 1 22

HELIX 25 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=ARG:A:+525:ARG:A:+534> 25 ARG A 525 ARG A 534 1 10

HELIX 26 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=ARG:A:+534:ALA:A:+542> 26 ARG A 534 ALA A 542 1 9

HELIX 27 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=VAL:B:++42:ARG:B:++46> 27 VAL B 42 ARG B 46 5 5

HELIX 28 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=PHE:B:++80:MET:B:++85> 28 PHE B 80 MET B 85 1 6

HELIX 29 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=LEU:B:+130:ASP:B:+134> 29 LEU B 130 ASP B 134 5 5

HELIX 30 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=GLY:B:+135:GLY:B:+143> 30 GLY B 135 GLY B 143 1 9

HELIX 31 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=VAL:B:+153:LEU:B:+159> 31 VAL B 153 LEU B 159 1 7

HELIX 32 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=ASN:B:+170:ILE:B:+187> 32 ASN B 170 ILE B 187 1 18

HELIX 33 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=ALA:B:+188:PHE:B:+190> 33 ALA B 188 PHE B 190 5 3

HELIX 34 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=SEN:B:+203:LEU:B:+214> 34 SEN B 203 LEU B 214 1 12

HELIX 35 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=SER:B:+215:SER:B:+220> 35 SER B 215 SER B 220 1 6

HELIX 36 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=ALA:B:+241:VAL:B:+255> 36 ALA B 241 VAL B 255 1 15

HELIX 37 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=ASN:B:+265:THR:B:+275> 37 ASN B 265 THR B 275 1 11

HELIX 38 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=PRO:B:+277:GLU:B:+285> 38 PRO B 277 GLU B 285 1 9

HELIX 39 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=TRP:B:+286:VAL:B:+288> 39 TRP B 286 VAL B 288 5 3

HELIX 40 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=THR:B:+311:GLY:B:+319> 40 THR B 311 GLY B 319 1 9

HELIX 41 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=GLY:B:+335:VAL:B:+340> 41 GLY B 335 VAL B 340 1 6

HELIX 42 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=SER:B:+355:VAL:B:+367> 42 SER B 355 VAL B 367 1 13

HELIX 43 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=SER:B:+371:THR:B:+383> 43 SER B 371 THR B 383 1 13

HELIX 44 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=ASP:B:+390:VAL:B:+407> 44 ASP B 390 VAL B 407 1 18

HELIX 45 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=VAL:B:+407:GLN:B:+421> 45 VAL B 407 GLN B 421 1 15

HELIX 46 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=PRO:B:+440:GLY:B:+444> 46 PRO B 440 GLY B 444 5 5

HELIX 47 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=GLU:B:+450:GLY:B:+456> 47 GLU B 450 GLY B 456 1 7

HELIX 48 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=LEU:B:+457:ASN:B:+464> 48 LEU B 457 ASN B 464 5 8

HELIX 49 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=THR:B:+466:GLY:B:+487> 49 THR B 466 GLY B 487 1 22

HELIX 50 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=ARG:B:+525:ARG:B:+534> 50 ARG B 525 ARG B 534 1 10

HELIX 51 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=ARG:B:+534:SER:B:+541> 51 ARG B 534 SER B 541 1 8

SHEET 1 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=LEU:A:+++9:VAL:A:++12> A 3 LEU A 9 VAL A 12 0

SHEET 2 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=GLY:A:++15:ARG:A:++18> A 3 GLY A 15 ARG A 18 -1 O LEU A 17 N VAL A 10

SHEET 3 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=VAL:A:++59:ASP:A:++61> A 3 VAL A 59 ASP A 61 1 O LEU A 60 N GLN A 16

SHEET 1 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=ILE:A:++20:ALA:A:++24> B11 ILE A 20 ALA A 24 0

SHEET 2 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=GLY:A:++27:PRO:A:++36> B11 GLY A 27 PRO A 36 -1 O VAL A 29 N LEU A 22

SHEET 3 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=TYR:A:++98:PRO:A:+104> B11 TYR A 98 PRO A 104 -1 O VAL A 101 N PHE A 32

SHEET 4 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=VAL:A:+145:MET:A:+149> B11 VAL A 145 MET A 149 -1 O SER A 148 N ASN A 100

SHEET 5 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=THR:A:+112:ILE:A:+118> B11 THR A 112 ILE A 118 1 N LEU A 115 O VAL A 145

SHEET 6 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=GLY:A:+192:GLU:A:+202> B11 GLY A 192 GLU A 202 1 O SER A 196 N VAL A 114

SHEET 7 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=ARG:A:+224:GLN:A:+228> B11 ARG A 224 GLN A 228 1 O VAL A 226 N LEU A 199

SHEET 8 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=GLN:A:+325:VAL:A:+331> B11 GLN A 325 VAL A 331 1 O LEU A 327 N LEU A 227

SHEET 9 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=ARG:A:+424:PHE:A:+430> B11 ARG A 424 PHE A 430 1 O PHE A 430 N VAL A 330

SHEET 10 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=GLN:A:+509:LEU:A:+513> B11 GLN A 509 LEU A 513 1 O LEU A 513 N ILE A 429

SHEET 11 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=GLU:A:+519:ARG:A:+522> B11 GLU A 519 ARG A 522 -1 O ARG A 521 N TYR A 510

SHEET 1 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=VAL:A:++68:CYS:A:++69> C 2 VAL A 68 CYS A 69 0

SHEET 2 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=LEU:A:++92:SER:A:++93> C 2 LEU A 92 SER A 93 1 O SER A 93 N VAL A 68

SHEET 1 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=VAL:A:+239:SER:A:+240> D 2 VAL A 239 SER A 240 0

SHEET 2 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=VAL:A:+302:VAL:A:+303> D 2 VAL A 302 VAL A 303 1 O VAL A 303 N VAL A 239

SHEET 1 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=LEU:B:+++9:VAL:B:++12> E 3 LEU B 9 VAL B 12 0

SHEET 2 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=GLY:B:++15:ARG:B:++18> E 3 GLY B 15 ARG B 18 -1 O LEU B 17 N VAL B 10

SHEET 3 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=VAL:B:++59:ASP:B:++61> E 3 VAL B 59 ASP B 61 1 O LEU B 60 N GLN B 16

SHEET 1 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=ILE:B:++20:ALA:B:++24> F11 ILE B 20 ALA B 24 0

SHEET 2 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=GLY:B:++27:PRO:B:++36> F11 GLY B 27 PRO B 36 -1 O VAL B 29 N LEU B 22

SHEET 3 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=TYR:B:++98:PRO:B:+104> F11 TYR B 98 PRO B 104 -1 O VAL B 101 N PHE B 32

SHEET 4 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=VAL:B:+145:MET:B:+149> F11 VAL B 145 MET B 149 -1 O SER B 148 N ASN B 100

SHEET 5 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=THR:B:+112:ILE:B:+118> F11 THR B 112 ILE B 118 1 N LEU B 115 O VAL B 147

SHEET 6 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=GLY:B:+192:GLU:B:+202> F11 GLY B 192 GLU B 202 1 O SER B 196 N VAL B 114

SHEET 7 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=ARG:B:+224:GLN:B:+228> F11 ARG B 224 GLN B 228 1 O ARG B 224 N LEU B 199

SHEET 8 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=GLN:B:+325:VAL:B:+331> F11 GLN B 325 VAL B 331 1 O LEU B 327 N LEU B 227

SHEET 9 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=ARG:B:+424:PHE:B:+430> F11 ARG B 424 PHE B 430 1 O TYR B 426 N VAL B 328

SHEET 10 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=GLN:B:+509:LEU:B:+513> F11 GLN B 509 LEU B 513 1 O LEU B 513 N ILE B 429

SHEET 11 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=GLU:B:+519:ARG:B:+522> F11 GLU B 519 ARG B 522 -1 O ARG B 521 N TYR B 510

SHEET 1 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=VAL:B:++68:CYS:B:++69> G 2 VAL B 68 CYS B 69 0

SHEET 2 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=LEU:B:++92:SER:B:++93> G 2 LEU B 92 SER B 93 1 O SER B 93 N VAL B 68

SHEET 1 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=VAL:B:+239:SER:B:+240> H 2 VAL B 239 SER B 240 0

SHEET 2 <http://www.ebi.ac.uk/msd-srv/oca/oca-bin/send-secstr?id=3DL7&t=VAL:B:+302:VAL:B:+303> H 2 VAL B 302 VAL B 303 1 O VAL B 303 N VAL B 239

SSBOND 1 CYS A 69 CYS A 96 1555 1555 2.05

SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.12

SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.07

SSBOND 4 CYS B 69 CYS B 96 1555 1555 2.07

SSBOND 5 CYS B 257 CYS B 272 1555 1555 2.11

SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.11

LINK C GLU A 202 N ASEN A 203 1555 1555 1.33

LINK C GLU A 202 N BSUN A 203 1555 1555 1.33

LINK C ASEN A 203 N ALA A 204 1555 1555 1.34

LINK C BSUN A 203 N ALA A 204 1555 1555 1.34

LINK C GLU B 202 N ASEN B 203 1555 1555 1.34

LINK C GLU B 202 N BSUN B 203 1555 1555 1.34

LINK C ASEN B 203 N ALA B 204 1555 1555 1.34

LINK C BSUN B 203 N ALA B 204 1555 1555 1.34

LINK ND2 ASN A 464 C1 NAG A 549 1555 1555 1.46

LINK C GLU A 202 N BSEN A 203 1555 1555 1.33

LINK C BSEN A 203 N ALA A 204 1555 1555 1.34

LINK C GLU B 202 N BSEN B 203 1555 1555 1.34

LINK C BSEN B 203 N ALA B 204 1555 1555 1.34

CISPEP 1 TYR A 105 PRO A 106 0 -0.85

CISPEP 2 TYR B 105 PRO B 106 0 3.97

CISPEP 3 PRO B 492 ARG B 493 0 26.78

CISPEP 4 ARG B 493 ASP B 494 0 18.61

SITE 1 AC1 2 SER A 462 ASN A 464

SITE 1 AC2 2 ILE A 429 ARG A 525

SITE 1 AC3 8 LEU A 380 HIS A 381 GLN A 527 PHE A 535

SITE 2 AC3 8 LEU B 380 HIS B 381 GLN B 527 PHE B 535

SITE 1 AC4 3 HIS B 381 TYR B 382 HIS B 393

CRYST1 79.020 110.880 226.380 90.00 90.00 90.00 P 21 21 21 8

ORIGX1 1.000000 0.000000 0.000000 0.00000

ORIGX2 0.000000 1.000000 0.000000 0.00000

ORIGX3 0.000000 0.000000 1.000000 0.00000

SCALE1 0.012655 0.000000 0.000000 0.00000

SCALE2 0.000000 0.009019 0.000000 0.00000

SCALE3 0.000000 0.000000 0.004417 0.00000

ATOM 1 N GLU A 1 31.770 15.368 55.050 1.00 72.97 N

ATOM 2 CA GLU A 1 30.473 14.672 55.290 1.00 72.74 C

ATOM 3 C GLU A 1 29.905 15.176 56.616 1.00 72.34 C

ATOM 4 O GLU A 1 30.655 15.643 57.477 1.00 72.82 O

ATOM 5 CB GLU A 1 30.676 13.146 55.290 1.00 72.83 C

ATOM 6 CG GLU A 1 29.395 12.321 55.042 1.00 72.68 C

ATOM 7 CD GLU A 1 29.647 11.003 54.314 1.00 72.68 C

ATOM 8 OE1 GLU A 1 28.754 10.124 54.358 1.00 72.85 O

ATOM 9 OE2 GLU A 1 30.728 10.844 53.694 1.00 73.05 O

ATOM 10 N GLY A 2 28.587 15.113 56.775 1.00 71.39 N

ATOM 11 CA GLY A 2 27.979 15.543 58.021 1.00 69.74 C

ATOM 12 C GLY A 2 26.748 16.345 57.743 1.00 68.93 C

ATOM 13 O GLY A 2 25.637 15.911 58.052 1.00 68.20 O

ATOM 14 N ARG A 3 26.955 17.506 57.122 1.00 68.71 N

ATOM 15 CA ARG A 3 25.872 18.482 56.898 1.00 68.26 C

ATOM 16 C ARG A 3 25.233 18.473 55.493 1.00 67.19 C

ATOM 17 O ARG A 3 24.202 19.113 55.287 1.00 67.34 O

ATOM 18 CB ARG A 3 26.313 19.903 57.317 1.00 68.81 C

ATOM 19 CG ARG A 3 25.663 20.440 58.637 1.00 69.99 C

ATOM 20 CD ARG A 3 26.277 19.835 59.927 1.00 71.94 C

ATOM 21 NE ARG A 3 25.636 20.252 61.193 1.00 72.05 N

ATOM 22 CZ ARG A 3 24.429 19.852 61.639 1.00 73.37 C

ATOM 23 NH1 ARG A 3 23.644 19.036 60.929 1.00 72.40 N

ATOM 24 NH2 ARG A 3 23.986 20.288 62.814 1.00 72.07 N

ATOM 25 N GLU A 4 25.813 17.727 54.552 1.00 65.60 N

ATOM 26 CA GLU A 4 25.370 17.761 53.154 1.00 63.98 C

ATOM 27 C GLU A 4 24.317 16.721 52.785 1.00 62.52 C

ATOM 28 O GLU A 4 23.971 15.863 53.596 1.00 62.36 O

ATOM 29 CB GLU A 4 26.564 17.679 52.204 1.00 64.31 C

ATOM 30 CG GLU A 4 27.462 16.480 52.415 1.00 65.66 C

ATOM 31 CD GLU A 4 28.867 16.722 51.872 1.00 68.09 C

ATOM 32 OE1 GLU A 4 29.832 16.467 52.614 1.00 68.42 O

ATOM 33 OE2 GLU A 4 29.013 17.177 50.714 1.00 69.05 O

ATOM 34 N ASP A 5 23.824 16.805 51.549 1.00 60.51 N

ATOM 35 CA ASP A 5 22.678 16.027 51.106 1.00 58.82 C

ATOM 36 C ASP A 5 23.026 14.547 50.955 1.00 58.42 C

ATOM 37 O ASP A 5 23.760 14.164 50.050 1.00 58.87 O

ATOM 38 CB ASP A 5 22.116 16.607 49.806 1.00 57.87 C

ATOM 39 CG ASP A 5 20.880 15.869 49.307 1.00 57.16 C

ATOM 40 OD1 ASP A 5 20.617 14.719 49.730 1.00 57.31 O

ATOM 41 OD2 ASP A 5 20.168 16.435 48.452 1.00 54.66 O

ATOM 42 N PRO A 6 22.472 13.693 51.830 1.00 57.80 N

ATOM 43 CA PRO A 6 22.779 12.259 51.784 1.00 56.77 C

ATOM 44 C PRO A 6 22.588 11.602 50.411 1.00 55.75 C

ATOM 45 O PRO A 6 23.163 10.543 50.174 1.00 55.44 O

ATOM 46 CB PRO A 6 21.778 11.661 52.780 1.00 57.05 C

ATOM 47 CG PRO A 6 20.734 12.744 52.991 1.00 56.96 C

ATOM 48 CD PRO A 6 21.497 14.000 52.894 1.00 57.61 C

ATOM 49 N GLN A 7 21.789 12.205 49.526 1.00 54.62 N

ATOM 50 CA GLN A 7 21.569 11.618 48.201 1.00 53.73 C

ATOM 51 C GLN A 7 22.652 11.895 47.177 1.00 52.22 C

ATOM 52 O GLN A 7 22.625 11.349 46.065 1.00 51.96 O

ATOM 53 CB GLN A 7 20.229 12.031 47.621 1.00 54.38 C

ATOM 54 CG GLN A 7 19.105 11.013 47.924 1.00 58.14 C

ATOM 55 CD GLN A 7 19.105 9.736 47.043 1.00 60.15 C

ATOM 56 OE1 GLN A 7 19.269 9.799 45.810 1.00 59.97 O

ATOM 57 NE2 GLN A 7 18.870 8.579 47.684 1.00 60.57 N

ATOM 58 N LEU A 8 23.606 12.740 47.542 1.00 50.12 N

ATOM 59 CA LEU A 8 24.548 13.257 46.563 1.00 48.19 C

ATOM 60 C LEU A 8 25.951 12.705 46.739 1.00 47.66 C

ATOM 61 O LEU A 8 26.863 13.091 46.007 1.00 47.72 O

ATOM 62 CB LEU A 8 24.557 14.787 46.591 1.00 46.99 C

ATOM 63 CG LEU A 8 23.226 15.414 46.203 1.00 44.87 C

ATOM 64 CD1 LEU A 8 23.286 16.920 46.376 1.00 41.17 C

ATOM 65 CD2 LEU A 8 22.805 15.024 44.781 1.00 41.86 C

ATOM 66 N LEU A 9 26.124 11.816 47.712 1.00 46.52 N

ATOM 67 CA LEU A 9 27.425 11.211 47.947 1.00 45.66 C

ATOM 68 C LEU A 9 27.354 9.774 47.453 1.00 45.24 C

ATOM 69 O LEU A 9 26.491 9.004 47.893 1.00 44.92 O

ATOM 70 CB LEU A 9 27.808 11.276 49.425 1.00 45.26 C

ATOM 71 CG LEU A 9 27.595 12.623 50.137 1.00 46.07 C

ATOM 72 CD1 LEU A 9 27.590 12.490 51.695 1.00 45.38 C

ATOM 73 CD2 LEU A 9 28.601 13.693 49.684 1.00 45.86 C

ATOM 74 N VAL A 10 28.252 9.438 46.524 1.00 44.22 N

ATOM 75 CA VAL A 10 28.305 8.131 45.876 1.00 43.44 C

ATOM 76 C VAL A 10 29.770 7.676 45.816 1.00 43.30 C

ATOM 77 O VAL A 10 30.681 8.512 45.699 1.00 43.37 O

ATOM 78 CB VAL A 10 27.729 8.249 44.455 1.00 43.03 C

ATOM 79 CG1 VAL A 10 28.180 7.139 43.555 1.00 43.98 C

ATOM 80 CG2 VAL A 10 26.249 8.254 44.514 1.00 43.97 C

ATOM 81 N ARG A 11 30.005 6.362 45.913 1.00 42.65 N

ATOM 82 CA ARG A 11 31.350 5.812 45.714 1.00 41.61 C

ATOM 83 C ARG A 11 31.432 5.105 44.378 1.00 41.12 C

ATOM 84 O ARG A 11 30.523 4.379 44.023 1.00 41.53 O

ATOM 85 CB ARG A 11 31.726 4.851 46.837 1.00 41.81 C

ATOM 86 CG ARG A 11 33.125 4.269 46.684 1.00 41.41 C

ATOM 87 CD ARG A 11 33.584 3.517 47.915 1.00 40.65 C

ATOM 88 NE ARG A 11 34.027 4.411 48.991 1.00 38.96 N

ATOM 89 CZ ARG A 11 35.273 4.840 49.142 1.00 37.28 C

ATOM 90 NH1 ARG A 11 35.578 5.651 50.145 1.00 37.56 N

ATOM 91 NH2 ARG A 11 36.210 4.471 48.281 1.00 37.13 N

ATOM 92 N VAL A 12 32.496 5.362 43.627 1.00 40.47 N

ATOM 93 CA VAL A 12 32.821 4.583 42.443 1.00 40.14 C

ATOM 94 C VAL A 12 34.225 3.972 42.631 1.00 40.55 C

ATOM 95 O VAL A 12 34.907 4.289 43.621 1.00 40.25 O

ATOM 96 CB VAL A 12 32.765 5.442 41.145 1.00 40.33 C

ATOM 97 CG1 VAL A 12 31.337 5.920 40.880 1.00 39.58 C

ATOM 98 CG2 VAL A 12 33.746 6.595 41.222 1.00 37.69 C

ATOM 99 N ARG A 13 34.664 3.134 41.682 1.00 40.41 N

ATOM 100 CA ARG A 13 35.920 2.369 41.830 1.00 41.32 C

ATOM 101 C ARG A 13 37.140 3.245 42.160 1.00 41.40 C

ATOM 102 O ARG A 13 38.012 2.847 42.910 1.00 41.25 O

ATOM 103 CB ARG A 13 36.146 1.490 40.600 1.00 41.37 C

ATOM 104 CG ARG A 13 37.551 0.912 40.391 1.00 43.31 C

ATOM 105 CD ARG A 13 37.889 -0.301 41.283 1.00 44.76 C

ATOM 106 NE ARG A 13 38.922 0.123 42.214 1.00 47.58 N

ATOM 107 CZ ARG A 13 40.107 -0.457 42.354 1.00 49.39 C

ATOM 108 NH1 ARG A 13 40.408 -1.551 41.673 1.00 49.01 N

ATOM 109 NH2 ARG A 13 40.979 0.036 43.226 1.00 51.16 N

ATOM 110 N GLY A 14 37.161 4.464 41.650 1.00 42.13 N

ATOM 111 CA GLY A 14 38.283 5.358 41.893 1.00 43.10 C

ATOM 112 C GLY A 14 38.179 6.204 43.134 1.00 43.93 C

ATOM 113 O GLY A 14 39.143 6.883 43.516 1.00 45.13 O

ATOM 114 N GLY A 15 37.017 6.210 43.774 1.00 44.28 N

ATOM 115 CA GLY A 15 36.874 7.019 44.974 1.00 44.13 C

ATOM 116 C GLY A 15 35.479 7.534 45.222 1.00 44.35 C

ATOM 117 O GLY A 15 34.500 6.990 44.676 1.00 44.22 O

ATOM 118 N GLN A 16 35.413 8.588 46.047 1.00 44.23 N

ATOM 119 CA GLN A 16 34.174 9.193 46.525 1.00 44.41 C

ATOM 120 C GLN A 16 33.764 10.427 45.740 1.00 44.39 C

ATOM 121 O GLN A 16 34.611 11.296 45.445 1.00 44.58 O

ATOM 122 CB GLN A 16 34.338 9.603 47.980 1.00 44.77 C

ATOM 123 CG GLN A 16 34.052 8.496 48.966 1.00 46.85 C

ATOM 124 CD GLN A 16 34.290 8.941 50.401 1.00 49.89 C

ATOM 125 OE1 GLN A 16 35.440 9.207 50.795 1.00 50.72 O

ATOM 126 NE2 GLN A 16 33.206 9.032 51.193 1.00 48.72 N

ATOM 127 N LEU A 17 32.464 10.535 45.438 1.00 43.83 N

ATOM 128 CA LEU A 17 31.954 11.655 44.637 1.00 43.54 C

ATOM 129 C LEU A 17 30.881 12.440 45.350 1.00 43.59 C

ATOM 130 O LEU A 17 30.045 11.861 46.041 1.00 44.42 O

ATOM 131 CB LEU A 17 31.367 11.150 43.325 1.00 42.90 C

ATOM 132 CG LEU A 17 32.299 10.430 42.365 1.00 43.04 C

ATOM 133 CD1 LEU A 17 31.455 9.720 41.326 1.00 43.60 C

ATOM 134 CD2 LEU A 17 33.245 11.414 41.718 1.00 42.61 C

ATOM 135 N ARG A 18 30.889 13.751 45.163 1.00 43.16 N

ATOM 136 CA ARG A 18 29.766 14.589 45.568 1.00 43.67 C

ATOM 137 C ARG A 18 29.149 15.239 44.336 1.00 42.69 C

ATOM 138 O ARG A 18 29.831 15.927 43.576 1.00 42.02 O

ATOM 139 CB ARG A 18 30.185 15.661 46.574 1.00 43.38 C

ATOM 140 CG ARG A 18 28.997 16.341 47.267 1.00 45.82 C

ATOM 141 CD ARG A 18 29.416 17.516 48.159 1.00 46.42 C

ATOM 142 NE ARG A 18 30.664 18.101 47.685 1.00 52.07 N

ATOM 143 CZ ARG A 18 31.845 18.011 48.297 1.00 53.14 C

ATOM 144 NH1 ARG A 18 31.986 17.386 49.471 1.00 51.78 N

ATOM 145 NH2 ARG A 18 32.900 18.571 47.711 1.00 55.70 N

ATOM 146 N GLY A 19 27.857 15.002 44.145 1.00 42.38 N

ATOM 147 CA GLY A 19 27.137 15.541 43.017 1.00 42.36 C

ATOM 148 C GLY A 19 26.336 16.759 43.415 1.00 42.50 C

ATOM 149 O GLY A 19 26.557 17.335 44.492 1.00 42.43 O

ATOM 150 N ILE A 20 25.388 17.128 42.553 1.00 42.09 N

ATOM 151 CA ILE A 20 24.562 18.300 42.768 1.00 42.09 C

ATOM 152 C ILE A 20 23.089 17.989 42.479 1.00 42.50 C

ATOM 153 O ILE A 20 22.777 17.245 41.550 1.00 42.38 O

ATOM 154 CB ILE A 20 25.091 19.496 41.928 1.00 42.19 C

ATOM 155 CG1 ILE A 20 24.323 20.789 42.249 1.00 42.36 C

ATOM 156 CG2 ILE A 20 25.127 19.164 40.411 1.00 40.93 C

ATOM 157 CD1 ILE A 20 24.998 22.079 41.748 1.00 41.28 C

ATOM 158 N ARG A 21 22.204 18.538 43.304 1.00 43.04 N

ATOM 159 CA ARG A 21 20.757 18.448 43.114 1.00 44.61 C

ATOM 160 C ARG A 21 20.396 19.553 42.129 1.00 44.57 C

ATOM 161 O ARG A 21 20.609 20.734 42.409 1.00 45.22 O

ATOM 162 CB ARG A 21 20.065 18.657 44.468 1.00 44.35 C

ATOM 163 CG ARG A 21 18.573 18.359 44.542 1.00 45.82 C

ATOM 164 CD ARG A 21 17.969 18.910 45.856 1.00 46.86 C

ATOM 165 NE ARG A 21 16.799 19.718 45.512 1.00 55.24 N

ATOM 166 CZ ARG A 21 15.533 19.488 45.883 1.00 59.01 C

ATOM 167 NH1 ARG A 21 15.206 18.474 46.691 1.00 61.43 N

ATOM 168 NH2 ARG A 21 14.572 20.300 45.442 1.00 60.00 N

ATOM 169 N LEU A 22 19.904 19.170 40.962 1.00 44.83 N

ATOM 170 CA LEU A 22 19.566 20.121 39.909 1.00 45.79 C

ATOM 171 C LEU A 22 18.053 20.201 39.733 1.00 46.51 C

ATOM 172 O LEU A 22 17.369 19.202 39.944 1.00 46.51 O

ATOM 173 CB LEU A 22 20.217 19.718 38.582 1.00 44.93 C

ATOM 174 CG LEU A 22 21.735 19.786 38.345 1.00 44.28 C

ATOM 175 CD1 LEU A 22 21.979 19.557 36.858 1.00 44.28 C

ATOM 176 CD2 LEU A 22 22.404 21.078 38.788 1.00 40.02 C

ATOM 177 N LYS A 23 17.536 21.377 39.348 1.00 47.91 N

ATOM 178 CA LYS A 23 16.083 21.542 39.076 1.00 48.69 C

ATOM 179 C LYS A 23 15.806 21.173 37.656 1.00 48.18 C

ATOM 180 O LYS A 23 16.437 21.687 36.746 1.00 47.92 O

ATOM 181 CB LYS A 23 15.585 22.974 39.272 1.00 49.70 C

ATOM 182 CG LYS A 23 15.382 23.408 40.711 1.00 52.93 C

ATOM 183 CD LYS A 23 16.650 24.147 41.260 1.00 59.07 C

ATOM 184 CE LYS A 23 16.423 24.801 42.645 1.00 57.18 C

ATOM 185 NZ LYS A 23 15.349 25.852 42.554 1.00 60.39 N

ATOM 186 N ALA A 24 14.882 20.250 37.464 1.00 48.14 N

ATOM 187 CA ALA A 24 14.273 20.088 36.161 1.00 48.18 C

ATOM 188 C ALA A 24 12.867 20.658 36.312 1.00 48.21 C

ATOM 189 O ALA A 24 12.428 20.908 37.440 1.00 48.00 O

ATOM 190 CB ALA A 24 14.242 18.641 35.759 1.00 47.88 C

ATOM 191 N PRO A 25 12.176 20.919 35.185 1.00 48.40 N

ATOM 192 CA PRO A 25 10.789 21.413 35.250 1.00 48.15 C

ATOM 193 C PRO A 25 9.895 20.584 36.172 1.00 47.89 C

ATOM 194 O PRO A 25 9.189 21.150 36.981 1.00 48.09 O

ATOM 195 CB PRO A 25 10.314 21.305 33.804 1.00 48.08 C

ATOM 196 CG PRO A 25 11.586 21.513 32.997 1.00 48.41 C

ATOM 197 CD PRO A 25 12.658 20.806 33.791 1.00 48.43 C

ATOM 198 N GLY A 26 9.939 19.262 36.084 1.00 47.72 N

ATOM 199 CA GLY A 26 9.038 18.439 36.894 1.00 47.46 C

ATOM 200 C GLY A 26 9.528 18.063 38.285 1.00 47.62 C

ATOM 201 O GLY A 26 8.916 17.215 38.926 1.00 47.84 O

ATOM 202 N GLY A 27 10.619 18.674 38.763 1.00 47.23 N

ATOM 203 CA GLY A 27 11.219 18.305 40.055 1.00 46.43 C

ATOM 204 C GLY A 27 12.736 18.130 39.987 1.00 46.76 C

ATOM 205 O GLY A 27 13.346 18.359 38.936 1.00 46.84 O

ATOM 206 N PRO A 28 13.368 17.684 41.096 1.00 46.72 N

ATOM 207 CA PRO A 28 14.845 17.674 41.160 1.00 45.92 C

ATOM 208 C PRO A 28 15.474 16.453 40.473 1.00 45.46 C

ATOM 209 O PRO A 28 14.805 15.413 40.349 1.00 45.00 O

ATOM 210 CB PRO A 28 15.121 17.616 42.657 1.00 46.19 C

ATOM 211 CG PRO A 28 13.927 16.859 43.237 1.00 46.15 C

ATOM 212 CD PRO A 28 12.748 17.100 42.309 1.00 46.61 C

ATOM 213 N VAL A 29 16.726 16.601 40.016 1.00 44.40 N

ATOM 214 CA VAL A 29 17.545 15.472 39.528 1.00 43.77 C

ATOM 215 C VAL A 29 18.958 15.452 40.152 1.00 43.70 C

ATOM 216 O VAL A 29 19.467 16.493 40.592 1.00 42.91 O

ATOM 217 CB VAL A 29 17.669 15.404 37.972 1.00 43.64 C

ATOM 218 CG1 VAL A 29 16.319 15.303 37.330 1.00 42.72 C

ATOM 219 CG2 VAL A 29 18.458 16.564 37.418 1.00 42.91 C

ATOM 220 N SER A 30 19.579 14.271 40.207 1.00 43.09 N

ATOM 221 CA SER A 30 20.975 14.196 40.651 1.00 43.35 C

ATOM 222 C SER A 30 21.916 14.303 39.480 1.00 42.38 C

ATOM 223 O SER A 30 21.701 13.667 38.452 1.00 42.45 O

ATOM 224 CB SER A 30 21.255 12.880 41.349 1.00 43.62 C

ATOM 225 OG SER A 30 20.371 12.711 42.432 1.00 46.58 O

ATOM 226 N ALA A 31 22.974 15.082 39.633 1.00 41.24 N

ATOM 227 CA ALA A 31 23.968 15.155 38.584 1.00 40.28 C

ATOM 228 C ALA A 31 25.366 14.961 39.148 1.00 39.93 C

ATOM 229 O ALA A 31 25.721 15.564 40.173 1.00 40.74 O

ATOM 230 CB ALA A 31 23.868 16.469 37.863 1.00 40.51 C

ATOM 231 N PHE A 32 26.162 14.118 38.487 1.00 38.40 N

ATOM 232 CA PHE A 32 27.566 13.936 38.855 1.00 36.45 C

ATOM 233 C PHE A 32 28.402 14.316 37.660 1.00 36.33 C

ATOM 234 O PHE A 32 28.455 13.603 36.673 1.00 35.26 O

ATOM 235 CB PHE A 32 27.813 12.502 39.305 1.00 35.71 C

ATOM 236 CG PHE A 32 27.039 12.137 40.508 1.00 34.19 C

ATOM 237 CD1 PHE A 32 25.735 11.673 40.395 1.00 33.35 C

ATOM 238 CD2 PHE A 32 27.578 12.323 41.773 1.00 33.41 C

ATOM 239 CE1 PHE A 32 24.991 11.353 41.536 1.00 32.20 C

ATOM 240 CE2 PHE A 32 26.829 12.009 42.920 1.00 32.96 C

ATOM 241 CZ PHE A 32 25.541 11.532 42.796 1.00 30.92 C

ATOM 242 N LEU A 33 29.022 15.490 37.744 1.00 37.10 N

ATOM 243 CA LEU A 33 29.595 16.130 36.560 1.00 37.25 C

ATOM 244 C LEU A 33 31.081 16.181 36.665 1.00 37.11 C

ATOM 245 O LEU A 33 31.610 16.454 37.733 1.00 37.37 O

ATOM 246 CB LEU A 33 29.030 17.546 36.382 1.00 37.15 C

ATOM 247 CG LEU A 33 27.505 17.664 36.273 1.00 38.01 C

ATOM 248 CD1 LEU A 33 27.040 19.140 36.158 1.00 39.79 C

ATOM 249 CD2 LEU A 33 26.962 16.832 35.121 1.00 36.28 C

ATOM 250 N GLY A 34 31.749 15.918 35.551 1.00 37.66 N

ATOM 251 CA GLY A 34 33.212 15.908 35.505 1.00 37.93 C

ATOM 252 C GLY A 34 33.880 14.809 36.324 1.00 38.10 C

ATOM 253 O GLY A 34 34.896 15.063 36.995 1.00 38.11 O

ATOM 254 N ILE A 35 33.316 13.596 36.295 1.00 37.64 N

ATOM 255 CA ILE A 35 33.992 12.443 36.888 1.00 37.35 C

ATOM 256 C ILE A 35 35.131 12.042 35.956 1.00 37.67 C

ATOM 257 O ILE A 35 34.886 11.771 34.785 1.00 37.57 O

ATOM 258 CB ILE A 35 33.056 11.234 37.015 1.00 37.64 C

ATOM 259 CG1 ILE A 35 31.795 11.605 37.824 1.00 36.82 C

ATOM 260 CG2 ILE A 35 33.830 10.011 37.567 1.00 36.36 C

ATOM 261 CD1 ILE A 35 30.650 10.659 37.592 1.00 34.69 C

ATOM 262 N PRO A 36 36.378 11.996 36.463 1.00 37.87 N

ATOM 263 CA PRO A 36 37.524 11.577 35.619 1.00 38.07 C

ATOM 264 C PRO A 36 37.482 10.067 35.360 1.00 38.25 C

ATOM 265 O PRO A 36 37.249 9.307 36.288 1.00 38.43 O

ATOM 266 CB PRO A 36 38.732 11.914 36.495 1.00 37.80 C

ATOM 267 CG PRO A 36 38.184 11.771 37.940 1.00 37.48 C

ATOM 268 CD PRO A 36 36.781 12.293 37.852 1.00 37.35 C

ATOM 269 N PHE A 37 37.694 9.632 34.125 1.00 38.69 N

ATOM 270 CA PHE A 37 37.650 8.194 33.829 1.00 38.88 C

ATOM 271 C PHE A 37 38.969 7.674 33.246 1.00 39.70 C

ATOM 272 O PHE A 37 39.122 6.474 33.025 1.00 40.58 O

ATOM 273 CB PHE A 37 36.441 7.821 32.940 1.00 38.51 C

ATOM 274 CG PHE A 37 36.489 8.397 31.549 1.00 38.16 C

ATOM 275 CD1 PHE A 37 37.034 7.664 30.498 1.00 37.83 C

ATOM 276 CD2 PHE A 37 35.965 9.663 31.281 1.00 37.87 C

ATOM 277 CE1 PHE A 37 37.091 8.186 29.191 1.00 39.65 C

ATOM 278 CE2 PHE A 37 36.009 10.196 29.983 1.00 39.07 C

ATOM 279 CZ PHE A 37 36.589 9.459 28.930 1.00 38.68 C

ATOM 280 N ALA A 38 39.912 8.585 33.005 1.00 40.37 N

ATOM 281 CA ALA A 38 41.233 8.256 32.463 1.00 40.35 C

ATOM 282 C ALA A 38 42.260 9.158 33.084 1.00 40.64 C

ATOM 283 O ALA A 38 41.924 10.224 33.589 1.00 41.13 O

ATOM 284 CB ALA A 38 41.271 8.439 30.976 1.00 40.72 C

ATOM 285 N GLU A 39 43.518 8.741 33.037 1.00 40.41 N

ATOM 286 CA GLU A 39 44.578 9.656 33.363 1.00 40.56 C

ATOM 287 C GLU A 39 44.576 10.761 32.315 1.00 39.77 C

ATOM 288 O GLU A 39 44.432 10.497 31.118 1.00 38.51 O

ATOM 289 CB GLU A 39 45.938 8.938 33.395 1.00 41.19 C

ATOM 290 CG GLU A 39 46.195 8.123 34.669 1.00 43.27 C

ATOM 291 CD GLU A 39 46.181 8.975 35.917 1.00 46.57 C

ATOM 292 OE1 GLU A 39 46.975 9.935 35.994 1.00 51.43 O

ATOM 293 OE2 GLU A 39 45.371 8.706 36.821 1.00 46.71 O

ATOM 294 N PRO A 40 44.751 12.002 32.761 1.00 39.79 N

ATOM 295 CA PRO A 40 44.818 13.111 31.810 1.00 40.27 C

ATOM 296 C PRO A 40 45.764 12.780 30.646 1.00 40.48 C

ATOM 297 O PRO A 40 46.936 12.580 30.881 1.00 41.12 O

ATOM 298 CB PRO A 40 45.383 14.252 32.657 1.00 39.78 C

ATOM 299 CG PRO A 40 44.960 13.936 34.065 1.00 39.27 C

ATOM 300 CD PRO A 40 44.917 12.439 34.160 1.00 39.75 C

ATOM 301 N PRO A 41 45.262 12.711 29.397 1.00 40.77 N

ATOM 302 CA PRO A 41 46.138 12.288 28.290 1.00 40.88 C

ATOM 303 C PRO A 41 47.127 13.375 27.823 1.00 41.18 C

ATOM 304 O PRO A 41 47.152 13.763 26.652 1.00 40.66 O

ATOM 305 CB PRO A 41 45.155 11.909 27.190 1.00 40.26 C

ATOM 306 CG PRO A 41 43.994 12.815 27.440 1.00 41.03 C

ATOM 307 CD PRO A 41 43.894 13.002 28.934 1.00 40.69 C

ATOM 308 N VAL A 42 47.969 13.817 28.740 1.00 41.31 N

ATOM 309 CA VAL A 42 48.831 14.949 28.477 1.00 42.45 C

ATOM 310 C VAL A 42 50.321 14.556 28.354 1.00 43.57 C

ATOM 311 O VAL A 42 50.705 13.407 28.663 1.00 44.42 O

ATOM 312 CB VAL A 42 48.621 16.018 29.561 1.00 42.30 C

ATOM 313 CG1 VAL A 42 47.119 16.450 29.588 1.00 42.14 C

ATOM 314 CG2 VAL A 42 49.048 15.492 30.914 1.00 40.77 C

ATOM 315 N GLY A 43 51.144 15.501 27.893 1.00 43.65 N

ATOM 316 CA GLY A 43 52.590 15.340 27.894 1.00 43.99 C

ATOM 317 C GLY A 43 52.941 14.149 27.043 1.00 44.69 C

ATOM 318 O GLY A 43 52.561 14.094 25.874 1.00 45.59 O

ATOM 319 N SER A 44 53.628 13.169 27.620 1.00 45.07 N

ATOM 320 CA SER A 44 53.999 11.955 26.860 1.00 45.44 C

ATOM 321 C SER A 44 52.796 11.080 26.471 1.00 45.08 C

ATOM 322 O SER A 44 52.950 10.119 25.717 1.00 45.14 O

ATOM 323 CB SER A 44 54.972 11.111 27.663 1.00 45.53 C

ATOM 324 OG SER A 44 54.351 10.715 28.877 1.00 47.44 O

ATOM 325 N ARG A 45 51.602 11.417 26.964 1.00 44.59 N

ATOM 326 CA ARG A 45 50.441 10.554 26.736 1.00 44.24 C

ATOM 327 C ARG A 45 49.585 10.962 25.527 1.00 43.37 C

ATOM 328 O ARG A 45 48.650 10.246 25.150 1.00 42.77 O

ATOM 329 CB ARG A 45 49.610 10.416 28.008 1.00 44.52 C

ATOM 330 CG ARG A 45 50.407 9.922 29.204 1.00 47.76 C