HEADER OXYGEN STORAGE/TRANSPORT 03-MAY-02 1LNL

TITLE STRUCTURE OF DEOXYGENATED HEMOCYANIN FROM RAPANA THOMASIANA

CAVEAT 1LNL CAVEAT: CHIRALITY ERROR AT CA CENTER OF CYS A 47

COMPND MOL_ID: 1;

COMPND 2 MOLECULE: HEMOCYANIN;

COMPND 3 CHAIN: A, B, C

SOURCE MOL_ID: 1;

SOURCE 2 ORGANISM_SCIENTIFIC: RAPANA THOMASIANA;

SOURCE 3 ORGANISM_TAXID: 29165

KEYWDS HEMOCYANIN, DEOXYGENATED FORM, OXYGEN, COPPER, METAL

KEYWDS 2 BINDING SITE, COOPERATIVITY, OXYGEN STORAGE/TRANSPORT

KEYWDS 3 COMPLEX

EXPDTA X-RAY DIFFRACTION

AUTHOR M.PERBANDT,E.W.GUTHOEHRLEIN,W.RYPNIEWSKI,K.IDAKIEVA,

AUTHOR 2 S.STOEVA,W.VOELTER,N.GENOV,C.BETZEL

REVDAT 2 24-FEB-09 1LNL 1 VERSN

REVDAT 1 03-JUN-03 1LNL 0

JRNL AUTH M.PERBANDT,E.W.GUTHOEHRLEIN,W.RYPNIEWSKI,

JRNL AUTH 2 K.IDAKIEVA,S.STOEVA,W.VOELTER,N.GENOV,C.BETZEL

JRNL TITL THE STRUCTURE OF A FUNCTIONAL UNIT FROM THE WALL

JRNL TITL 2 OF A GASTROPOD HEMOCYANIN OFFERS A POSSIBLE

JRNL TITL 3 MECHANISM FOR COOPERATIVITY

JRNL REF BIOCHEMISTRY V. 42 6341 2003

JRNL REFN ISSN 0006-2960

JRNL PMID 12767214

JRNL DOI 10.1021/BI020672X

REMARK 1

REMARK 2

REMARK 2 RESOLUTION. 3.30 ANGSTROMS.

REMARK 3

REMARK 3 REFINEMENT.

REMARK 3 PROGRAM : REFMAC 5

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) : 3.30

REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00

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

REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0

REMARK 3 NUMBER OF REFLECTIONS : 30824

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) : 0.250

REMARK 3 R VALUE (WORKING SET) : 0.248

REMARK 3 FREE R VALUE : 0.288

REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100

REMARK 3 FREE R VALUE TEST SET COUNT : 1653

REMARK 3

REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.

REMARK 3 TOTAL NUMBER OF BINS USED : 20

REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.30

REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.38

REMARK 3 REFLECTION IN BIN (WORKING SET) : 2125

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

REMARK 3 BIN R VALUE (WORKING SET) : 0.2960

REMARK 3 BIN FREE R VALUE SET COUNT : 122

REMARK 3 BIN FREE R VALUE : 0.3880

REMARK 3

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

REMARK 3 PROTEIN ATOMS : 9930

REMARK 3 NUCLEIC ACID ATOMS : 0

REMARK 3 HETEROGEN ATOMS : 54

REMARK 3 SOLVENT ATOMS : 0

REMARK 3

REMARK 3 B VALUES.

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

REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.54

REMARK 3 OVERALL ANISOTROPIC B VALUE.

REMARK 3 B11 (A**2) : -0.61000

REMARK 3 B22 (A**2) : -0.61000

REMARK 3 B33 (A**2) : 1.21000

REMARK 3 B12 (A**2) : 0.00000

REMARK 3 B13 (A**2) : 0.00000

REMARK 3 B23 (A**2) : 0.00000

REMARK 3

REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.

REMARK 3 ESU BASED ON R VALUE (A): 2.800

REMARK 3 ESU BASED ON FREE R VALUE (A): 0.549

REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.224

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

REMARK 3

REMARK 3 CORRELATION COEFFICIENTS.

REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.893

REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.853

REMARK 3

REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT

REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10296 ; 0.045 ; 0.021

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

REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 14012 ; 3.100 ; 1.923

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

REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1218 ; 4.980 ; 3.000

REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL

REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1673 ;22.942 ;15.000

REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL

REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1437 ; 0.174 ; 0.200

REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8212 ; 0.011 ; 0.020

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

REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 6599 ; 0.358 ; 0.300

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

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

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

REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 865 ; 0.255 ; 0.500

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): 88 ; 0.450 ; 0.300

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

REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 1 ; 0.056 ; 0.500

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): NULL ; NULL ; NULL

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

REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL

REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL

REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL

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 : 1

REMARK 3

REMARK 3 NCS GROUP NUMBER : 1

REMARK 3 CHAIN NAMES : A B C

REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1

REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE

REMARK 3 1 A 15 A 350 5

REMARK 3 1 B 15 B 350 5

REMARK 3 1 C 15 C 350 5

REMARK 3 GROUP CHAIN COUNT RMS WEIGHT

REMARK 3 TIGHT POSITIONAL 1 A (A): 135 ; 0.28 ; 0.05

REMARK 3 TIGHT POSITIONAL 1 B (A): 135 ; 0.30 ; 0.05

REMARK 3 TIGHT POSITIONAL 1 C (A): 135 ; 0.36 ; 0.05

REMARK 3 MEDIUM POSITIONAL 1 A (A): 1266 ; 0.48 ; 0.50

REMARK 3 MEDIUM POSITIONAL 1 B (A): 1266 ; 0.54 ; 0.50

REMARK 3 MEDIUM POSITIONAL 1 C (A): 1266 ; 0.62 ; 0.50

REMARK 3 LOOSE POSITIONAL 1 A (A): 1305 ; 1.07 ; 5.00

REMARK 3 LOOSE POSITIONAL 1 B (A): 1305 ; 1.03 ; 5.00

REMARK 3 LOOSE POSITIONAL 1 C (A): 1305 ; 1.18 ; 5.00

REMARK 3

REMARK 3 TLS DETAILS

REMARK 3 NUMBER OF TLS GROUPS : 3

REMARK 3

REMARK 3 TLS GROUP : 1

REMARK 3 NUMBER OF COMPONENTS GROUP : 1

REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI

REMARK 3 RESIDUE RANGE : A 1 A 405

REMARK 3 ORIGIN FOR THE GROUP (A): 77.8570 -8.3989 239.2718

REMARK 3 T TENSOR

REMARK 3 T11: 0.3012 T22: 0.1858

REMARK 3 T33: 0.1165 T12: 0.0129

REMARK 3 T13: 0.0114 T23: -0.0016

REMARK 3 L TENSOR

REMARK 3 L11: 1.5604 L22: 2.6479

REMARK 3 L33: 2.3745 L12: -1.0818

REMARK 3 L13: 0.4486 L23: -1.1686

REMARK 3 S TENSOR

REMARK 3 S11: 0.1006 S12: 0.2880 S13: -0.0405

REMARK 3 S21: -0.4023 S22: -0.1323 S23: -0.1023

REMARK 3 S31: 0.4051 S32: 0.0699 S33: 0.0317

REMARK 3

REMARK 3 TLS GROUP : 2

REMARK 3 NUMBER OF COMPONENTS GROUP : 1

REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI

REMARK 3 RESIDUE RANGE : B 1 B 405

REMARK 3 ORIGIN FOR THE GROUP (A): 88.9712 33.4584 263.6536

REMARK 3 T TENSOR

REMARK 3 T11: 0.1674 T22: 0.0429

REMARK 3 T33: 0.0425 T12: 0.0611

REMARK 3 T13: 0.0357 T23: 0.0399

REMARK 3 L TENSOR

REMARK 3 L11: 2.9210 L22: 1.6764

REMARK 3 L33: 2.5854 L12: 0.9601

REMARK 3 L13: -1.0571 L23: -0.9005

REMARK 3 S TENSOR

REMARK 3 S11: 0.0432 S12: 0.2911 S13: 0.0874

REMARK 3 S21: -0.0693 S22: 0.1094 S23: 0.0248

REMARK 3 S31: -0.1339 S32: -0.2500 S33: -0.1526

REMARK 3

REMARK 3 TLS GROUP : 3

REMARK 3 NUMBER OF COMPONENTS GROUP : 1

REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI

REMARK 3 RESIDUE RANGE : C 1 C 405

REMARK 3 ORIGIN FOR THE GROUP (A): 129.2009 14.8898 285.5671

REMARK 3 T TENSOR

REMARK 3 T11: 0.0428 T22: 0.3106

REMARK 3 T33: 0.1653 T12: 0.0130

REMARK 3 T13: 0.0077 T23: 0.0044

REMARK 3 L TENSOR

REMARK 3 L11: 2.7757 L22: 2.5544

REMARK 3 L33: 2.6244 L12: -1.2438

REMARK 3 L13: -0.5346 L23: 0.5887

REMARK 3 S TENSOR

REMARK 3 S11: 0.1275 S12: 0.3355 S13: -0.3611

REMARK 3 S21: -0.3050 S22: -0.1548 S23: 0.0886

REMARK 3 S31: 0.0462 S32: 0.0985 S33: 0.0272

REMARK 3

REMARK 3 BULK SOLVENT MODELLING.

REMARK 3 METHOD USED : MASK

REMARK 3 PARAMETERS FOR MASK CALCULATION

REMARK 3 VDW PROBE RADIUS : 1.40

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 1LNL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08

REMARK 100

REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-MAY-02.

REMARK 100 THE RCSB ID CODE IS RCSB016109.

REMARK 200

REMARK 200 EXPERIMENTAL DETAILS

REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION

REMARK 200 DATE OF DATA COLLECTION : 20-MAR-00

REMARK 200 TEMPERATURE (KELVIN) : 243

REMARK 200 PH : 7.5

REMARK 200 NUMBER OF CRYSTALS USED : 1

REMARK 200

REMARK 200 SYNCHROTRON (Y/N) : Y

REMARK 200 RADIATION SOURCE : APS

REMARK 200 BEAMLINE : 14-BM-C

REMARK 200 X-RAY GENERATOR MODEL : NULL

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

REMARK 200 WAVELENGTH OR RANGE (A) : 0.921

REMARK 200 MONOCHROMATOR : SYNCHROTRON

REMARK 200 OPTICS : NULL

REMARK 200

REMARK 200 DETECTOR TYPE : CCD

REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH

REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO

REMARK 200 DATA SCALING SOFTWARE : SCALEPACK

REMARK 200

REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33066

REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300

REMARK 200 RESOLUTION RANGE LOW (A) : 20.000

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

REMARK 200

REMARK 200 OVERALL.

REMARK 200 COMPLETENESS FOR RANGE (%) : NULL

REMARK 200 DATA REDUNDANCY : NULL

REMARK 200 R MERGE (I) : NULL

REMARK 200 R SYM (I) : NULL

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

REMARK 200

REMARK 200 IN THE HIGHEST RESOLUTION SHELL.

REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30

REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.38

REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1

REMARK 200 DATA REDUNDANCY IN SHELL : NULL

REMARK 200 R MERGE FOR SHELL (I) : NULL

REMARK 200 R SYM FOR SHELL (I) : NULL

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

REMARK 200

REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH

REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT

REMARK 200 SOFTWARE USED: AMORE

REMARK 200 STARTING MODEL: NULL

REMARK 200

REMARK 200 REMARK: NULL

REMARK 280

REMARK 280 CRYSTAL

REMARK 280 SOLVENT CONTENT, VS (%): 66.88

REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.71

REMARK 280

REMARK 280 CRYSTALLIZATION CONDITIONS: MG FORMATE, PH 7.5, VAPOR

REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K

REMARK 290

REMARK 290 CRYSTALLOGRAPHIC SYMMETRY

REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2

REMARK 290

REMARK 290 SYMOP SYMMETRY

REMARK 290 NNNMMM OPERATOR

REMARK 290 1555 X,Y,Z

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

REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4

REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4

REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4

REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4

REMARK 290 7555 Y,X,-Z

REMARK 290 8555 -Y,-X,-Z+1/2

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 0.00000

REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000

REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 187.49400

REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 52.74300

REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 52.74300

REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 281.24100

REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 52.74300

REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 52.74300

REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 93.74700

REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 52.74300

REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 52.74300

REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 281.24100

REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 52.74300

REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 52.74300

REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 93.74700

REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000

REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000

REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000

REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000

REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000

REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 187.49400

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: HEXAMERIC

REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C

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 350 BIOMT1 2 0.000000 -1.000000 0.000000 105.48600

REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 105.48600

REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 562.48200

REMARK 480

REMARK 480 ZERO OCCUPANCY ATOM

REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO

REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS

REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;

REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):

REMARK 480 M RES C SSEQI ATOMS

REMARK 480 ARG C 82 CZ NH1 NH2

REMARK 500

REMARK 500 GEOMETRY AND STEREOCHEMISTRY

REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT

REMARK 500

REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.

REMARK 500

REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE

REMARK 500 SG CYS B 59 CE1 HIS B 61 1.71

REMARK 500 NE2 HIS B 181 NE2 HIS B 212 1.84

REMARK 500 O GLY C 149 N GLY C 152 1.96

REMARK 500 O GLU C 78 N ALA C 80 2.03

REMARK 500 OE1 GLU C 174 OE2 GLU C 178 2.05

REMARK 500 O SER C 86 N VAL C 88 2.06

REMARK 500 O HIS A 198 N HIS A 200 2.08

REMARK 500 O ARG A -1 ND1 HIS A 279 2.09

REMARK 500 O LEU B 37 OH TYR B 73 2.10

REMARK 500 O SER B 11 N GLU B 14 2.13

REMARK 500 O ILE C 140 N VAL C 142 2.14

REMARK 500 O PRO C 268 N ASP C 270 2.17

REMARK 500 SG CYS C 59 CE1 HIS C 61 2.18

REMARK 500 O ASP C 386 N GLU C 388 2.19

REMARK 500 O ASP A 169 N ASP A 172 2.19

REMARK 500

REMARK 500 REMARK: NULL

REMARK 500

REMARK 500 GEOMETRY AND STEREOCHEMISTRY

REMARK 500 SUBTOPIC: CLOSE CONTACTS

REMARK 500

REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC

REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15

REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A

REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375

REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE

REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.

REMARK 500

REMARK 500 DISTANCE CUTOFF:

REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS

REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS

REMARK 500

REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE

REMARK 500 CA HIS A -2 CU CU B 5503 6456 1.67

REMARK 500 O HIS A -2 CU CU B 5503 6456 1.69

REMARK 500

REMARK 500 REMARK: NULL

REMARK 500

REMARK 500 GEOMETRY AND STEREOCHEMISTRY

REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS

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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)

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 RES CSSEQI ATM2 DEVIATION

REMARK 500 GLU A 27 CD GLU A 27 OE1 0.077

REMARK 500 ALA A 38 CA ALA A 38 CB -0.149

REMARK 500 PHE A 66 C PHE A 66 O -0.122

REMARK 500 VAL A 142 CB VAL A 142 CG1 0.139

REMARK 500 TYR A 153 CG TYR A 153 CD2 0.103

REMARK 500 TYR A 153 CE1 TYR A 153 CZ 0.107

REMARK 500 TYR A 153 CZ TYR A 153 CE2 0.092

REMARK 500 TYR A 163 CZ TYR A 163 CE2 -0.099

REMARK 500 GLU A 166 CD GLU A 166 OE2 0.068

REMARK 500 TYR A 170 CE2 TYR A 170 CD2 -0.107

REMARK 500 VAL A 175 CA VAL A 175 CB -0.135

REMARK 500 TRP A 187 CB TRP A 187 CG -0.120

REMARK 500 TYR A 204 CG TYR A 204 CD1 -0.084

REMARK 500 TRP A 222 CG TRP A 222 CD1 -0.089

REMARK 500 GLU A 264 CD GLU A 264 OE2 0.096

REMARK 500 GLU A 269 CD GLU A 269 OE2 0.068

REMARK 500 GLU A 281 CD GLU A 281 OE1 0.070

REMARK 500 GLU A 315 CD GLU A 315 OE1 0.083

REMARK 500 GLU A 315 CD GLU A 315 OE2 0.087

REMARK 500 GLU A 333 CD GLU A 333 OE1 0.081

REMARK 500 ARG A 355 CB ARG A 355 CG -0.185

REMARK 500 GLY B -3 N GLY B -3 CA 0.103

REMARK 500 ALA B 16 CA ALA B 16 CB -0.160

REMARK 500 ALA B 20 CA ALA B 20 CB 0.132

REMARK 500 CYS B 58 CA CYS B 58 C -0.162

REMARK 500 VAL B 60 CB VAL B 60 CG1 -0.165

REMARK 500 VAL B 60 CB VAL B 60 CG2 -0.151

REMARK 500 ALA B 64 CA ALA B 64 CB -0.132

REMARK 500 LEU B 72 C LEU B 72 O -0.129

REMARK 500 TYR B 73 CG TYR B 73 CD1 -0.082

REMARK 500 TYR B 73 CE1 TYR B 73 CZ -0.092

REMARK 500 TYR B 92 CB TYR B 92 CG 0.114

REMARK 500 ALA B 104 CA ALA B 104 CB -0.172

REMARK 500 TRP B 111 CB TRP B 111 CG -0.113

REMARK 500 ALA B 118 CA ALA B 118 CB -0.129

REMARK 500 LYS B 135 CD LYS B 135 CE 0.160

REMARK 500 ALA B 137 CA ALA B 137 CB -0.196

REMARK 500 GLU B 148 CD GLU B 148 OE2 0.091

REMARK 500 TRP B 156 CB TRP B 156 CG 0.128

REMARK 500 ALA B 164 CA ALA B 164 CB -0.151

REMARK 500 PHE B 177 CG PHE B 177 CD1 -0.111

REMARK 500 GLU B 178 CD GLU B 178 OE1 -0.078

REMARK 500 TRP B 187 CB TRP B 187 CG -0.121

REMARK 500 TYR B 201 CD1 TYR B 201 CE1 -0.110

REMARK 500 GLU B 224 CD GLU B 224 OE2 0.074

REMARK 500 GLU B 235 CG GLU B 235 CD 0.114

REMARK 500 CYS B 238 CB CYS B 238 SG -0.171

REMARK 500 TYR B 274 CG TYR B 274 CD1 -0.085

REMARK 500 TYR B 274 CE1 TYR B 274 CZ -0.078

REMARK 500 LYS B 303 CD LYS B 303 CE 0.217

REMARK 500

REMARK 500 THIS ENTRY HAS 93 BOND DEVIATIONS.

REMARK 500

REMARK 500 REMARK: NULL

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 GLU A 27 OE1 - CD - OE2 ANGL. DEV. = 7.8 DEGREES

REMARK 500 ASP A 28 CB - CG - OD2 ANGL. DEV. = 6.4 DEGREES

REMARK 500 CYS A 47 CA - CB - SG ANGL. DEV. = -12.9 DEGREES

REMARK 500 CYS A 47 N - CA - C ANGL. DEV. = 17.6 DEGREES

REMARK 500 PRO A 48 N - CD - CG ANGL. DEV. = -11.3 DEGREES

REMARK 500 PRO A 67 N - CD - CG ANGL. DEV. = -9.2 DEGREES

REMARK 500 ARG A 71 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES

REMARK 500 ARG A 71 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES

REMARK 500 LEU A 72 CB - CG - CD1 ANGL. DEV. = -14.5 DEGREES

REMARK 500 LEU A 81 CB - CG - CD1 ANGL. DEV. = -15.3 DEGREES

REMARK 500 LEU A 81 CB - CG - CD2 ANGL. DEV. = 11.5 DEGREES

REMARK 500 ARG A 82 NE - CZ - NH1 ANGL. DEV. = -5.0 DEGREES

REMARK 500 ARG A 82 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES

REMARK 500 ARG A 83 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES

REMARK 500 ASP A 94 CB - CG - OD2 ANGL. DEV. = 7.8 DEGREES

REMARK 500 ASP A 108 CB - CG - OD2 ANGL. DEV. = 6.8 DEGREES

REMARK 500 ASP A 113 N - CA - C ANGL. DEV. = 17.6 DEGREES

REMARK 500 ASP A 128 CB - CG - OD2 ANGL. DEV. = 7.8 DEGREES

REMARK 500 ASP A 143 OD1 - CG - OD2 ANGL. DEV. = -11.5 DEGREES

REMARK 500 ASP A 143 CB - CG - OD2 ANGL. DEV. = 6.9 DEGREES

REMARK 500 ASP A 169 CB - CG - OD2 ANGL. DEV. = 9.0 DEGREES

REMARK 500 ILE A 209 CG1 - CB - CG2 ANGL. DEV. = -15.2 DEGREES

REMARK 500 LEU A 210 CA - CB - CG ANGL. DEV. = -16.3 DEGREES

REMARK 500 ARG A 217 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES

REMARK 500 LEU A 218 CB - CG - CD2 ANGL. DEV. = -22.2 DEGREES

REMARK 500 PRO A 233 N - CD - CG ANGL. DEV. = -12.8 DEGREES

REMARK 500 LEU A 240 CB - CG - CD2 ANGL. DEV. = -10.6 DEGREES

REMARK 500 MET A 243 CG - SD - CE ANGL. DEV. = 10.0 DEGREES

REMARK 500 ARG A 244 NE - CZ - NH1 ANGL. DEV. = -5.2 DEGREES

REMARK 500 ARG A 244 NE - CZ - NH2 ANGL. DEV. = 3.9 DEGREES

REMARK 500 ASP A 283 CB - CG - OD2 ANGL. DEV. = 9.1 DEGREES

REMARK 500 LEU A 285 CB - CG - CD1 ANGL. DEV. = -13.6 DEGREES

REMARK 500 ASP A 297 CB - CG - OD2 ANGL. DEV. = 6.5 DEGREES

REMARK 500 ASP A 306 CB - CG - OD2 ANGL. DEV. = 7.0 DEGREES

REMARK 500 VAL A 308 CB - CA - C ANGL. DEV. = -11.5 DEGREES

REMARK 500 ASP A 324 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES

REMARK 500 ARG A 355 NE - CZ - NH2 ANGL. DEV. = 3.1 DEGREES

REMARK 500 TYR A 359 CA - CB - CG ANGL. DEV. = 12.1 DEGREES

REMARK 500 ASP A 386 CB - CG - OD2 ANGL. DEV. = 10.8 DEGREES

REMARK 500 ASP A 393 CB - CG - OD2 ANGL. DEV. = 7.2 DEGREES

REMARK 500 ARG B -1 NE - CZ - NH2 ANGL. DEV. = -5.0 DEGREES

REMARK 500 LEU B 22 CB - CG - CD1 ANGL. DEV. = 10.5 DEGREES

REMARK 500 ASP B 28 CB - CG - OD1 ANGL. DEV. = -6.7 DEGREES

REMARK 500 ASP B 28 CB - CG - OD2 ANGL. DEV. = 8.0 DEGREES

REMARK 500 ASP B 32 OD1 - CG - OD2 ANGL. DEV. = -11.4 DEGREES

REMARK 500 ASP B 32 CB - CG - OD1 ANGL. DEV. = 11.6 DEGREES

REMARK 500 PRO B 45 N - CD - CG ANGL. DEV. = -9.8 DEGREES

REMARK 500 LEU B 46 CA - CB - CG ANGL. DEV. = 15.6 DEGREES

REMARK 500 CYS B 47 CA - CB - SG ANGL. DEV. = -29.1 DEGREES

REMARK 500 CYS B 47 N - CA - C ANGL. DEV. = 17.0 DEGREES

REMARK 500

REMARK 500 THIS ENTRY HAS 120 ANGLE DEVIATIONS.

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 HIS A -2 -68.05 12.44

REMARK 500 ALA A 31 -8.02 -55.01

REMARK 500 PHE A 34 -90.16 -1.45

REMARK 500 LEU A 37 27.29 -64.78

REMARK 500 HIS A 41 -71.79 -69.26

REMARK 500 ALA A 42 -111.43 -127.36

REMARK 500 LEU A 46 29.51 -152.53

REMARK 500 ALA A 49 135.74 171.33

REMARK 500 ASN A 53 -74.74 -79.19

REMARK 500 ALA A 57 -120.77 -62.23

REMARK 500 CYS A 58 -2.67 174.87

REMARK 500 HIS A 70 -19.05 -47.88

REMARK 500 ARG A 83 -7.22 -58.93

REMARK 500 VAL A 96 -70.42 -52.06

REMARK 500 PRO A 103 145.83 -38.31

REMARK 500 PHE A 105 -46.31 -18.87

REMARK 500 ASP A 112 -94.69 -91.62

REMARK 500 ASP A 113 147.33 39.97

REMARK 500 ALA A 114 155.72 -13.64

REMARK 500 LEU A 115 -67.84 81.58

REMARK 500 ASN A 119 90.47 177.28

REMARK 500 PHE A 124 33.02 -83.31

REMARK 500 ALA A 127 -149.95 -126.12

REMARK 500 GLN A 134 -159.88 -102.00

REMARK 500 LYS A 147 97.23 68.01

REMARK 500 ASP A 154 74.64 -104.12

REMARK 500 TRP A 156 -100.73 -41.03

REMARK 500 SER A 157 -35.62 -24.78

REMARK 500 GLN A 160 -71.33 -66.64

REMARK 500 GLN A 167 126.27 -170.31

REMARK 500 ASP A 169 61.33 -103.28

REMARK 500 TYR A 170 -70.21 4.19

REMARK 500 PHE A 177 -29.11 -39.54

REMARK 500 ASN A 182 -16.93 -48.67

REMARK 500 HIS A 185 -39.32 -39.26

REMARK 500 GLU A 193 -15.57 -44.19

REMARK 500 SER A 195 -173.94 -178.68

REMARK 500 MET A 196 -2.42 -51.69

REMARK 500 LEU A 199 -52.32 -15.80

REMARK 500 HIS A 200 -72.81 -63.05

REMARK 500 HIS A 212 16.85 -65.23

REMARK 500 ASN A 237 38.19 -94.80

REMARK 500 ALA A 239 61.82 19.26

REMARK 500 MET A 243 22.00 -71.74

REMARK 500 ARG A 244 -6.22 -143.30

REMARK 500 THR A 261 11.98 -64.84

REMARK 500 GLU A 264 -11.66 -49.08

REMARK 500 LYS A 267 107.84 -56.32

REMARK 500 GLU A 269 -42.62 -26.67

REMARK 500 HIS A 279 75.38 39.40

REMARK 500 LEU A 285 89.67 -150.93

REMARK 500 GLN A 288 38.77 70.50

REMARK 500 ASN A 291 -179.20 -61.80

REMARK 500 ASP A 297 17.11 -68.78

REMARK 500 TYR A 298 -63.48 -122.40

REMARK 500 SER A 320 150.34 -48.00

REMARK 500 ASP A 331 -95.67 -56.27

REMARK 500 TYR A 339 147.15 -171.03

REMARK 500 SER A 346 45.83 -104.77

REMARK 500 LEU A 347 26.01 -156.75

REMARK 500 PRO A 350 153.87 -38.10

REMARK 500 THR A 362 -87.10 -39.75

REMARK 500 SER A 367 52.71 -65.00

REMARK 500 LYS A 368 15.70 -173.11

REMARK 500 HIS A 373 59.26 -106.74

REMARK 500 VAL A 375 94.57 -51.69

REMARK 500 SER A 384 -177.83 -51.79

REMARK 500 ASP A 386 -106.03 -80.13

REMARK 500 ASN A 387 48.90 -176.16

REMARK 500 PRO A 404 -168.81 -74.02

REMARK 500 HIS B -2 -85.48 -118.83

REMARK 500 VAL B 7 21.11 -75.28

REMARK 500 ARG B 8 -50.92 -131.66

REMARK 500 ASN B 9 44.35 -74.77

REMARK 500 ASP B 32 30.19 -96.42

REMARK 500 PHE B 34 -71.98 -47.09

REMARK 500 ALA B 42 -71.31 -151.23

REMARK 500 LEU B 46 72.44 -151.74

REMARK 500 CYS B 47 -81.78 -102.25

REMARK 500 PRO B 67 -7.87 -55.52

REMARK 500 HIS B 84 48.64 -104.31

REMARK 500 PHE B 105 -49.55 -29.69

REMARK 500 ASP B 113 -52.92 -15.97

REMARK 500 LEU B 115 20.61 160.63

REMARK 500 PHE B 116 -9.18 164.96

REMARK 500 HIS B 117 110.23 53.57

REMARK 500 PHE B 124 19.30 -56.91

REMARK 500 ASP B 139 102.37 -172.56

REMARK 500 ASN B 141 -68.38 18.13

REMARK 500 VAL B 142 77.34 -107.39

REMARK 500 PRO B 150 -7.79 -56.11

REMARK 500 LYS B 151 38.39 -160.71

REMARK 500 ASP B 154 63.54 -63.73

REMARK 500 HIS B 181 4.68 -63.05

REMARK 500 SER B 195 -139.77 -141.16

REMARK 500 HIS B 200 -84.29 -51.49

REMARK 500 HIS B 212 6.89 -65.81

REMARK 500 GLN B 223 -19.58 -47.28

REMARK 500 PRO B 233 -76.37 -41.08

REMARK 500 ASN B 234 -16.67 -37.92

REMARK 500 ASN B 237 42.19 -105.12

REMARK 500 PHE B 252 -49.35 -28.67

REMARK 500 LYS B 263 -72.38 -61.12

REMARK 500 GLU B 264 -21.84 -39.43

REMARK 500 ASP B 270 22.16 -66.17

REMARK 500 HIS B 277 -60.30 -102.20

REMARK 500 TYR B 280 134.89 -179.14

REMARK 500 LYS B 303 40.88 -61.01

REMARK 500 LEU B 313 76.49 -102.01

REMARK 500 SER B 326 -144.67 -99.23

REMARK 500 ILE B 327 64.40 -172.18

REMARK 500 TYR B 359 110.35 -165.98

REMARK 500 LYS B 368 4.73 -172.02

REMARK 500 ASN B 387 92.61 -18.53

REMARK 500 PRO B 404 -131.61 -64.68

REMARK 500 ASN C 9 42.46 -79.35

REMARK 500 GLU C 27 43.87 -109.50

REMARK 500 SER C 29 4.99 -62.36

REMARK 500 PHE C 34 -97.00 -30.18

REMARK 500 GLN C 35 -26.04 -21.92

REMARK 500 SER C 39 -6.01 -53.52

REMARK 500 ALA C 42 -90.46 -153.05

REMARK 500 LEU C 46 70.38 -176.44

REMARK 500 ALA C 51 62.12 -176.77

REMARK 500 ALA C 52 -119.66 -105.41

REMARK 500 ASN C 53 -88.22 -90.19

REMARK 500 CYS C 59 77.18 138.28

REMARK 500 VAL C 60 96.68 -28.95

REMARK 500 THR C 65 21.25 -73.93

REMARK 500 TRP C 69 -70.37 -51.04

REMARK 500 ASP C 79 30.87 -52.50

REMARK 500 ALA C 80 -20.62 -146.36

REMARK 500 SER C 86 72.55 -63.19

REMARK 500 VAL C 87 -22.17 -21.47

REMARK 500 VAL C 96 23.44 -66.06

REMARK 500 GLU C 100 -83.23 -47.84

REMARK 500 TRP C 111 105.58 -167.39

REMARK 500 LEU C 115 -51.64 -177.48

REMARK 500 ALA C 118 139.61 -176.89

REMARK 500 ASN C 119 76.80 -162.20

REMARK 500 PHE C 120 -151.58 -150.41

REMARK 500 PHE C 124 42.94 -77.36

REMARK 500 ASP C 130 -84.52 -62.38

REMARK 500 ASN C 132 82.91 -64.31

REMARK 500 HIS C 133 70.48 -64.38

REMARK 500 ASN C 141 -63.28 44.77

REMARK 500 LYS C 144 52.65 -95.42

REMARK 500 LYS C 147 -131.10 -96.81

REMARK 500 GLU C 148 -169.46 -49.01

REMARK 500 ASP C 154 59.22 -63.56

REMARK 500 GLN C 160 -73.43 -56.25

REMARK 500 TRP C 187 1.50 -41.61

REMARK 500 VAL C 188 -53.76 -129.32

REMARK 500 GLU C 193 -84.62 -77.19

REMARK 500 TYR C 194 91.68 -61.21

REMARK 500 SER C 195 -164.26 -163.57

REMARK 500 HIS C 200 -18.87 -49.54

REMARK 500 SER C 203 -47.95 -28.15

REMARK 500 ALA C 239 33.45 75.32

REMARK 500 PRO C 246 -160.51 -33.67

REMARK 500 PHE C 250 -28.40 -36.06

REMARK 500 PRO C 255 40.20 -100.58

REMARK 500 LEU C 258 24.82 -77.11

REMARK 500 HIS C 265 58.60 -111.36

REMARK 500 GLU C 269 -39.34 -17.84

REMARK 500 THR C 271 -4.62 -149.72

REMARK 500 PHE C 272 -73.06 -55.00

REMARK 500 ASP C 273 86.36 -69.42

REMARK 500 HIS C 279 94.10 -66.73

REMARK 500 LEU C 285 83.34 -66.17

REMARK 500 GLN C 288 73.02 50.29

REMARK 500 GLU C 304 7.03 -60.06

REMARK 500 SER C 346 -72.48 -86.00

REMARK 500 LEU C 347 -2.47 -55.86

REMARK 500 PRO C 350 137.91 -17.42

REMARK 500 ASP C 354 37.92 -86.16

REMARK 500 ARG C 355 170.31 174.18

REMARK 500 TYR C 359 101.46 -166.87

REMARK 500 ILE C 361 15.96 -142.78

REMARK 500 HIS C 373 36.03 -92.38

REMARK 500 THR C 381 88.45 -159.67

REMARK 500 SER C 384 -174.45 -60.81

REMARK 500 ASN C 387 79.66 -26.12

REMARK 500 THR C 392 42.10 -92.42

REMARK 500 ASP C 393 -93.14 -77.60

REMARK 500 PRO C 404 -134.61 -59.03

REMARK 500

REMARK 500 REMARK: NULL

REMARK 500

REMARK 500 GEOMETRY AND STEREOCHEMISTRY

REMARK 500 SUBTOPIC: PLANAR GROUPS

REMARK 500

REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL

REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE

REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN

REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS

REMARK 500 AN RMSD GREATER THAN THIS VALUE

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

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

REMARK 500

REMARK 500 M RES CSSEQI RMS TYPE

REMARK 500 ARG C 82 0.08 SIDE_CHAIN

REMARK 500

REMARK 500 REMARK: NULL

REMARK 620

REMARK 620 METAL COORDINATION

REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;

REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):

REMARK 620

REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL

REMARK 620 CU B5506 CU

REMARK 620 N RES CSSEQI ATOM

REMARK 620 1 ARG B -1 NH1

REMARK 620 2 ARG B -1 CZ 103.5

REMARK 620 3 ARG B -1 NE 81.7 25.0

REMARK 620 4 ARG B -1 NH2 131.1 31.7 56.7

REMARK 620 5 HIS B -2 NE2 71.2 131.4 112.4 144.3

REMARK 620 6 HIS C 277 NE2 131.6 117.3 142.3 85.6 97.3

REMARK 620 N 1 2 3 4 5

REMARK 620

REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL

REMARK 620 CU C5509 CU

REMARK 620 N RES CSSEQI ATOM

REMARK 620 1 HIS C -2 NE2

REMARK 620 2 HIS C -2 CE1 90.9

REMARK 620 3 HIS C -2 CD2 56.9 107.0

REMARK 620 4 ARG C -1 NE 101.0 153.1 62.1

REMARK 620 5 ARG C -1 NH2 133.8 126.5 121.0 58.9

REMARK 620 6 HIS C -2 ND1 102.8 44.8 78.0 108.6 122.6

REMARK 620 7 HIS B 277 NE2 71.8 104.4 118.9 102.2 73.0 149.2

REMARK 620 N 1 2 3 4 5 6

REMARK 620

REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL

REMARK 620 CU B5015 CU

REMARK 620 N RES CSSEQI ATOM

REMARK 620 1 HIS B 181 NE2

REMARK 620 2 HIS B 185 NE2 78.7

REMARK 620 3 HIS B 212 NE2 65.8 94.5

REMARK 620 N 1 2

REMARK 620

REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL

REMARK 620 CU C5018 CU

REMARK 620 N RES CSSEQI ATOM

REMARK 620 1 HIS C 181 CE1

REMARK 620 2 HIS C 212 NE2 83.3

REMARK 620 3 HIS C 181 NE2 39.8 63.2

REMARK 620 4 HIS C 185 NE2 92.9 94.8 62.7

REMARK 620 N 1 2 3

REMARK 620

REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL

REMARK 620 CU A5001 CU

REMARK 620 N RES CSSEQI ATOM

REMARK 620 1 HIS A 61 NE2

REMARK 620 2 HIS A 70 NE2 106.3

REMARK 620 3 HIS A 41 NE2 103.1 104.2

REMARK 620 N 1 2

REMARK 620

REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL

REMARK 620 CU A5012 CU

REMARK 620 N RES CSSEQI ATOM

REMARK 620 1 HIS A 181 NE2

REMARK 620 2 HIS A 185 NE2 72.1

REMARK 620 3 HIS A 212 NE2 61.6 91.2

REMARK 620 N 1 2

REMARK 620

REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL

REMARK 620 CU B5004 CU

REMARK 620 N RES CSSEQI ATOM

REMARK 620 1 CU B5015 CU

REMARK 620 2 HIS B 61 NE2 125.5

REMARK 620 3 HIS B 41 NE2 134.9 91.0

REMARK 620 4 HIS B 70 NE2 88.0 108.2 106.4

REMARK 620 N 1 2 3

REMARK 620

REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL

REMARK 620 CU B5503 CU

REMARK 620 N RES CSSEQI ATOM

REMARK 620 1 HIS B 117 NE2

REMARK 620 2 HIS A -2 O 117.3

REMARK 620 3 HIS A -2 ND1 68.9 90.6

REMARK 620 N 1 2

REMARK 620

REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL

REMARK 620 CU C5007 CU

REMARK 620 N RES CSSEQI ATOM

REMARK 620 1 HIS C 61 NE2

REMARK 620 2 HIS C 70 NE2 95.8

REMARK 620 3 CU C5018 CU 132.4 82.7

REMARK 620 4 HIS C 41 NE2 82.3 109.7 143.0

REMARK 620 N 1 2 3

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 600

REMARK 800 SITE_IDENTIFIER: AC2

REMARK 800 EVIDENCE_CODE: SOFTWARE

REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 650

REMARK 800 SITE_IDENTIFIER: AC3

REMARK 800 EVIDENCE_CODE: SOFTWARE

REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 651

REMARK 800 SITE_IDENTIFIER: AC4

REMARK 800 EVIDENCE_CODE: SOFTWARE

REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 5001

REMARK 800 SITE_IDENTIFIER: AC5

REMARK 800 EVIDENCE_CODE: SOFTWARE

REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 5012

REMARK 800 SITE_IDENTIFIER: AC6

REMARK 800 EVIDENCE_CODE: SOFTWARE

REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU B 5503

REMARK 800 SITE_IDENTIFIER: AC7

REMARK 800 EVIDENCE_CODE: SOFTWARE

REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU B 5004

REMARK 800 SITE_IDENTIFIER: AC8

REMARK 800 EVIDENCE_CODE: SOFTWARE

REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU B 5015

REMARK 800 SITE_IDENTIFIER: AC9

REMARK 800 EVIDENCE_CODE: SOFTWARE

REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU B 5506

REMARK 800 SITE_IDENTIFIER: BC1

REMARK 800 EVIDENCE_CODE: SOFTWARE

REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU C 5007

REMARK 800 SITE_IDENTIFIER: BC2

REMARK 800 EVIDENCE_CODE: SOFTWARE

REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU C 5018

REMARK 800 SITE_IDENTIFIER: BC3

REMARK 800 EVIDENCE_CODE: SOFTWARE

REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU C 5509

REMARK 999

REMARK 999 SEQUENCE

REMARK 999 AUTHORS INFORMED THAT PROTEIN SEQUENCE HAS NOT

REMARK 999 YET BEEN DEPOSITED IN A REFERENCE DATABASE.

REMARK 999 SEQUENCE PUBLISHED BY STOEVA ET AL., ARCH.

REMARK 999 BIOCHEM. BIOPHYS. 339, 149-158 (2002).

REMARK 999 AUTHORS ALSO INFORMED THAT THEY ARE UNSURE IF

REMARK 999 A RESIDUE IS PRESENT BETWEEN ARG -1 AND ASN 1

REMARK 999 ON CHAINS A,B AND C.

DBREF 1LNL A -2 405 UNP P83040 HCY2E_RAPTH 7 413

DBREF 1LNL B -2 405 UNP P83040 HCY2E_RAPTH 7 413

DBREF 1LNL C -2 405 UNP P83040 HCY2E_RAPTH 7 413

SEQRES 1 A 408 GLY HIS ARG ASN LEU VAL ARG LYS SER VAL ARG ASN LEU

SEQRES 2 A 408 SER PRO ALA GLU ARG ALA SER LEU VAL ALA ALA LEU LYS

SEQRES 3 A 408 SER LEU GLN GLU ASP SER SER ALA ASP GLY PHE GLN SER

SEQRES 4 A 408 LEU ALA SER PHE HIS ALA GLN PRO PRO LEU CYS PRO ALA

SEQRES 5 A 408 PRO ALA ALA ASN LYS ALA PHE ALA CYS CYS VAL HIS GLY

SEQRES 6 A 408 MET ALA THR PHE PRO GLU TRP HIS ARG LEU TYR THR VAL

SEQRES 7 A 408 GLN PHE GLU ASP ALA LEU ARG ARG HIS GLY SER VAL VAL

SEQRES 8 A 408 GLY ILE PRO TYR TRP ASP THR VAL VAL PRO GLN GLU ASP

SEQRES 9 A 408 LEU PRO ALA PHE PHE ASN ASP GLU ILE TRP ASP ASP ALA

SEQRES 10 A 408 LEU PHE HIS ALA ASN PHE THR ASN PRO PHE ASN GLY ALA

SEQRES 11 A 408 ASP ILE ASP PHE ASN HIS GLN LYS ILE ALA ARG ASP ILE

SEQRES 12 A 408 ASN VAL ASP LYS LEU ALA LYS GLU GLY PRO LYS GLY TYR

SEQRES 13 A 408 ASP THR TRP SER PHE LYS GLN TYR ILE TYR ALA LEU GLU

SEQRES 14 A 408 GLN GLU ASP TYR CYS ASP PHE GLU VAL GLN PHE GLU ILE

SEQRES 15 A 408 ALA HIS ASN ALA ILE HIS ALA TRP VAL GLY GLY THR GLU

SEQRES 16 A 408 GLU TYR SER MET GLY HIS LEU HIS TYR ALA SER TYR ASP

SEQRES 17 A 408 PRO VAL PHE ILE LEU HIS HIS SER ASN THR ASP ARG LEU

SEQRES 18 A 408 PHE ALA LEU TRP GLN GLU LEU GLN LYS PHE ARG GLY HIS

SEQRES 19 A 408 ASP PRO ASN GLU VAL ASN CYS ALA LEU GLU MET MET ARG

SEQRES 20 A 408 GLU PRO LEU LYS PRO PHE SER PHE GLY ALA PRO TYR ASN

SEQRES 21 A 408 LEU ASN PRO THR THR LYS GLU HIS SER LYS PRO GLU ASP

SEQRES 22 A 408 THR PHE ASP TYR LYS GLY HIS PHE HIS TYR GLU TYR ASP

SEQRES 23 A 408 HIS LEU GLU LEU GLN GLY MET ASN VAL GLN ARG LEU HIS

SEQRES 24 A 408 ASP TYR ILE ASN GLN GLN LYS GLU ALA ASP ARG VAL PHE

SEQRES 25 A 408 ALA GLY PHE LEU LEU GLU GLY ILE GLY THR SER ALA HIS

SEQRES 26 A 408 LEU ASP PHE SER ILE CYS ALA ILE ASP GLY GLU CYS THR

SEQRES 27 A 408 HIS ALA GLY TYR PHE ASP VAL LEU GLY GLY SER LEU GLU

SEQRES 28 A 408 THR PRO TRP GLN PHE ASP ARG LEU TYR LYS TYR GLU ILE

SEQRES 29 A 408 THR ASP VAL LEU GLU SER LYS GLY LEU ASP VAL HIS ASP

SEQRES 30 A 408 VAL PHE ASP ILE LYS ILE THR GLN THR SER TRP ASP ASN

SEQRES 31 A 408 GLU ASP ILE SER THR ASP ARG PHE PRO PRO PRO SER VAL

SEQRES 32 A 408 ILE TYR VAL PRO LYS

SEQRES 1 B 408 GLY HIS ARG ASN LEU VAL ARG LYS SER VAL ARG ASN LEU

SEQRES 2 B 408 SER PRO ALA GLU ARG ALA SER LEU VAL ALA ALA LEU LYS

SEQRES 3 B 408 SER LEU GLN GLU ASP SER SER ALA ASP GLY PHE GLN SER

SEQRES 4 B 408 LEU ALA SER PHE HIS ALA GLN PRO PRO LEU CYS PRO ALA

SEQRES 5 B 408 PRO ALA ALA ASN LYS ALA PHE ALA CYS CYS VAL HIS GLY

SEQRES 6 B 408 MET ALA THR PHE PRO GLU TRP HIS ARG LEU TYR THR VAL

SEQRES 7 B 408 GLN PHE GLU ASP ALA LEU ARG ARG HIS GLY SER VAL VAL

SEQRES 8 B 408 GLY ILE PRO TYR TRP ASP THR VAL VAL PRO GLN GLU ASP

SEQRES 9 B 408 LEU PRO ALA PHE PHE ASN ASP GLU ILE TRP ASP ASP ALA

SEQRES 10 B 408 LEU PHE HIS ALA ASN PHE THR ASN PRO PHE ASN GLY ALA

SEQRES 11 B 408 ASP ILE ASP PHE ASN HIS GLN LYS ILE ALA ARG ASP ILE

SEQRES 12 B 408 ASN VAL ASP LYS LEU ALA LYS GLU GLY PRO LYS GLY TYR

SEQRES 13 B 408 ASP THR TRP SER PHE LYS GLN TYR ILE TYR ALA LEU GLU

SEQRES 14 B 408 GLN GLU ASP TYR CYS ASP PHE GLU VAL GLN PHE GLU ILE

SEQRES 15 B 408 ALA HIS ASN ALA ILE HIS ALA TRP VAL GLY GLY THR GLU

SEQRES 16 B 408 GLU TYR SER MET GLY HIS LEU HIS TYR ALA SER TYR ASP

SEQRES 17 B 408 PRO VAL PHE ILE LEU HIS HIS SER ASN THR ASP ARG LEU

SEQRES 18 B 408 PHE ALA LEU TRP GLN GLU LEU GLN LYS PHE ARG GLY HIS

SEQRES 19 B 408 ASP PRO ASN GLU VAL ASN CYS ALA LEU GLU MET MET ARG

SEQRES 20 B 408 GLU PRO LEU LYS PRO PHE SER PHE GLY ALA PRO TYR ASN

SEQRES 21 B 408 LEU ASN PRO THR THR LYS GLU HIS SER LYS PRO GLU ASP

SEQRES 22 B 408 THR PHE ASP TYR LYS GLY HIS PHE HIS TYR GLU TYR ASP

SEQRES 23 B 408 HIS LEU GLU LEU GLN GLY MET ASN VAL GLN ARG LEU HIS

SEQRES 24 B 408 ASP TYR ILE ASN GLN GLN LYS GLU ALA ASP ARG VAL PHE

SEQRES 25 B 408 ALA GLY PHE LEU LEU GLU GLY ILE GLY THR SER ALA HIS

SEQRES 26 B 408 LEU ASP PHE SER ILE CYS ALA ILE ASP GLY GLU CYS THR

SEQRES 27 B 408 HIS ALA GLY TYR PHE ASP VAL LEU GLY GLY SER LEU GLU

SEQRES 28 B 408 THR PRO TRP GLN PHE ASP ARG LEU TYR LYS TYR GLU ILE

SEQRES 29 B 408 THR ASP VAL LEU GLU SER LYS GLY LEU ASP VAL HIS ASP

SEQRES 30 B 408 VAL PHE ASP ILE LYS ILE THR GLN THR SER TRP ASP ASN

SEQRES 31 B 408 GLU ASP ILE SER THR ASP ARG PHE PRO PRO PRO SER VAL

SEQRES 32 B 408 ILE TYR VAL PRO LYS

SEQRES 1 C 408 GLY HIS ARG ASN LEU VAL ARG LYS SER VAL ARG ASN LEU

SEQRES 2 C 408 SER PRO ALA GLU ARG ALA SER LEU VAL ALA ALA LEU LYS

SEQRES 3 C 408 SER LEU GLN GLU ASP SER SER ALA ASP GLY PHE GLN SER

SEQRES 4 C 408 LEU ALA SER PHE HIS ALA GLN PRO PRO LEU CYS PRO ALA

SEQRES 5 C 408 PRO ALA ALA ASN LYS ALA PHE ALA CYS CYS VAL HIS GLY

SEQRES 6 C 408 MET ALA THR PHE PRO GLU TRP HIS ARG LEU TYR THR VAL

SEQRES 7 C 408 GLN PHE GLU ASP ALA LEU ARG ARG HIS GLY SER VAL VAL

SEQRES 8 C 408 GLY ILE PRO TYR TRP ASP THR VAL VAL PRO GLN GLU ASP

SEQRES 9 C 408 LEU PRO ALA PHE PHE ASN ASP GLU ILE TRP ASP ASP ALA

SEQRES 10 C 408 LEU PHE HIS ALA ASN PHE THR ASN PRO PHE ASN GLY ALA

SEQRES 11 C 408 ASP ILE ASP PHE ASN HIS GLN LYS ILE ALA ARG ASP ILE

SEQRES 12 C 408 ASN VAL ASP LYS LEU ALA LYS GLU GLY PRO LYS GLY TYR

SEQRES 13 C 408 ASP THR TRP SER PHE LYS GLN TYR ILE TYR ALA LEU GLU

SEQRES 14 C 408 GLN GLU ASP TYR CYS ASP PHE GLU VAL GLN PHE GLU ILE

SEQRES 15 C 408 ALA HIS ASN ALA ILE HIS ALA TRP VAL GLY GLY THR GLU

SEQRES 16 C 408 GLU TYR SER MET GLY HIS LEU HIS TYR ALA SER TYR ASP

SEQRES 17 C 408 PRO VAL PHE ILE LEU HIS HIS SER ASN THR ASP ARG LEU

SEQRES 18 C 408 PHE ALA LEU TRP GLN GLU LEU GLN LYS PHE ARG GLY HIS

SEQRES 19 C 408 ASP PRO ASN GLU VAL ASN CYS ALA LEU GLU MET MET ARG

SEQRES 20 C 408 GLU PRO LEU LYS PRO PHE SER PHE GLY ALA PRO TYR ASN

SEQRES 21 C 408 LEU ASN PRO THR THR LYS GLU HIS SER LYS PRO GLU ASP

SEQRES 22 C 408 THR PHE ASP TYR LYS GLY HIS PHE HIS TYR GLU TYR ASP

SEQRES 23 C 408 HIS LEU GLU LEU GLN GLY MET ASN VAL GLN ARG LEU HIS

SEQRES 24 C 408 ASP TYR ILE ASN GLN GLN LYS GLU ALA ASP ARG VAL PHE

SEQRES 25 C 408 ALA GLY PHE LEU LEU GLU GLY ILE GLY THR SER ALA HIS

SEQRES 26 C 408 LEU ASP PHE SER ILE CYS ALA ILE ASP GLY GLU CYS THR

SEQRES 27 C 408 HIS ALA GLY TYR PHE ASP VAL LEU GLY GLY SER LEU GLU

SEQRES 28 C 408 THR PRO TRP GLN PHE ASP ARG LEU TYR LYS TYR GLU ILE

SEQRES 29 C 408 THR ASP VAL LEU GLU SER LYS GLY LEU ASP VAL HIS ASP

SEQRES 30 C 408 VAL PHE ASP ILE LYS ILE THR GLN THR SER TRP ASP ASN

SEQRES 31 C 408 GLU ASP ILE SER THR ASP ARG PHE PRO PRO PRO SER VAL

SEQRES 32 C 408 ILE TYR VAL PRO LYS

HET NAG A 600 15

HET NAG C 650 15

HET NAG C 651 15

HET CU A5001 1

HET CU A5012 1

HET CU B5503 1

HET CU B5004 1

HET CU B5015 1

HET CU B5506 1

HET CU C5007 1

HET CU C5018 1

HET CU C5509 1