HEADER BLOOD CLOTTING 19-DEC-05 2FFD
TITLE FIBRINOGEN FRAGMENT D WITH "A" KNOB PEPTIDE MIMIC GPRVVE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FIBRINOGEN ALPHA/ALPHA-E CHAIN;
COMPND 3 CHAIN: A, D;
COMPND 4 FRAGMENT: RESIDUES 145-210;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: FIBRINOGEN BETA CHAIN;
COMPND 8 CHAIN: B, E;
COMPND 9 FRAGMENT: RESIDUES 179-491;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: FIBRINOGEN GAMMA CHAIN;
COMPND 13 CHAIN: C, F;
COMPND 14 FRAGMENT: RESIDUES 122-432;
COMPND 15 ENGINEERED: YES;
COMPND 16 MOL_ID: 4;
COMPND 17 MOLECULE: GLY-PRO-ARG-VAL-VAL-GLU PEPTIDE;
COMPND 18 CHAIN: G, H, I, J;
COMPND 19 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: FGA;
SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: OVARY CELLS;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 GENE: FGB;
SOURCE 15 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 16 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 18 EXPRESSION_SYSTEM_CELL_LINE: OVARY CELLS;
SOURCE 19 MOL_ID: 3;
SOURCE 20 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 21 ORGANISM_COMMON: HUMAN;
SOURCE 22 ORGANISM_TAXID: 9606;
SOURCE 23 GENE: FGG;
SOURCE 24 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 25 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 26 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 27 EXPRESSION_SYSTEM_CELL_LINE: OVARY CELLS;
SOURCE 28 MOL_ID: 4;
SOURCE 29 SYNTHETIC: YES;
SOURCE 30 OTHER_DETAILS: SYNTHETIC CONSTRUCT
KEYWDS COMPLEX OF FIBRINOGEN WITH "A" SITE MIMIC GPRVVE IN BOTH "A" AND "B"
KEYWDS 2 SITES, BLOOD CLOTTING
EXPDTA X-RAY DIFFRACTION
AUTHOR L.BETTS
REVDAT 6 30-AUG-23 2FFD 1 HETSYN
REVDAT 5 29-JUL-20 2FFD 1 COMPND REMARK HETNAM LINK
REVDAT 5 2 1 SITE ATOM
REVDAT 4 18-OCT-17 2FFD 1 REMARK
REVDAT 3 13-JUL-11 2FFD 1 VERSN
REVDAT 2 24-FEB-09 2FFD 1 VERSN
REVDAT 1 04-JUL-06 2FFD 0
JRNL AUTH L.BETTS,B.K.MERENBLOOM,S.T.LORD
JRNL TITL THE STRUCTURE OF FIBRINOGEN FRAGMENT D WITH THE 'A' KNOB
JRNL TITL 2 PEPTIDE GPRVVE.
JRNL REF THROMB.HAEMOST. V. 4 1139 2006
JRNL REFN ISSN 0340-6245
JRNL PMID 16689770
JRNL DOI 10.1111/J.1538-7836.2006.01902.X
REMARK 2
REMARK 2 RESOLUTION. 2.89 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.89
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 42903
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) : 0.214
REMARK 3 R VALUE (WORKING SET) : 0.211
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2160
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) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.97
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2829
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.72
REMARK 3 BIN R VALUE (WORKING SET) : 0.2920
REMARK 3 BIN FREE R VALUE SET COUNT : 155
REMARK 3 BIN FREE R VALUE : 0.4100
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10583
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 80
REMARK 3 SOLVENT ATOMS : 231
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 55.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.57
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.86000
REMARK 3 B22 (A**2) : -2.06000
REMARK 3 B33 (A**2) : -0.80000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.411
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.293
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.607
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.914
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.851
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10862 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 14675 ; 1.097 ; 1.929
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1309 ; 5.576 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 556 ;35.437 ;24.568
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1870 ;17.039 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 63 ;18.196 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1474 ; 0.078 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8437 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 5390 ; 0.200 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 7362 ; 0.304 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 508 ; 0.140 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 9 ; 0.128 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 58 ; 0.211 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 9 ; 0.127 ; 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): 6668 ; 0.465 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10437 ; 0.847 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4906 ; 0.757 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4238 ; 1.304 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER 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 : 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 : 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2FFD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JAN-06.
REMARK 100 THE DEPOSITION ID IS D_1000035812.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-APR-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : OSMIC CONFOCAL BLUE
REMARK 200 OPTICS : OSMIC CONFOCAL BLUE
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42946
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
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 (%) : 98.4
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.16200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.50000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
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: PDB ENTRY 1LTJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG3350, 12.5 MM CACL2, PH 8.5,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, 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 44.76050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 113.74500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.32600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 113.74500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 44.76050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 47.32600
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: PENTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28490 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -76.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, G, J, K
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -71.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F, H, I, L
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 LYS A 191
REMARK 465 HIS B 149
REMARK 465 GLN B 150
REMARK 465 LEU B 151
REMARK 465 TYR B 152
REMARK 465 ILE B 153
REMARK 465 ASP B 154
REMARK 465 GLU B 155
REMARK 465 THR B 156
REMARK 465 GLN B 460
REMARK 465 GLN B 461
REMARK 465 ILE C 394
REMARK 465 GLY C 395
REMARK 465 GLU C 396
REMARK 465 GLY C 397
REMARK 465 GLN C 398
REMARK 465 GLN C 399
REMARK 465 HIS C 400
REMARK 465 HIS C 401
REMARK 465 LEU C 402
REMARK 465 GLY C 403
REMARK 465 GLY C 404
REMARK 465 ALA C 405
REMARK 465 LYS C 406
REMARK 465 VAL D 126
REMARK 465 ILE D 127
REMARK 465 GLU D 128
REMARK 465 LYS D 129
REMARK 465 VAL D 130
REMARK 465 GLN D 131
REMARK 465 HIS D 132
REMARK 465 ALA D 190
REMARK 465 LYS D 191
REMARK 465 HIS E 149
REMARK 465 GLN E 150
REMARK 465 LEU E 151
REMARK 465 TYR E 152
REMARK 465 ILE E 153
REMARK 465 ASP E 154
REMARK 465 GLU E 155
REMARK 465 THR E 156
REMARK 465 VAL E 157
REMARK 465 ASN E 158
REMARK 465 SER E 159
REMARK 465 ASN E 160
REMARK 465 ILE E 161
REMARK 465 PRO E 162
REMARK 465 THR E 163
REMARK 465 ASN E 164
REMARK 465 GLN E 460
REMARK 465 GLN E 461
REMARK 465 TYR F 96
REMARK 465 GLU F 97
REMARK 465 ALA F 98
REMARK 465 SER F 99
REMARK 465 ILE F 100
REMARK 465 LEU F 101
REMARK 465 THR F 102
REMARK 465 HIS F 103
REMARK 465 ASP F 104
REMARK 465 SER F 105
REMARK 465 SER F 106
REMARK 465 ILE F 107
REMARK 465 ARG F 108
REMARK 465 TYR F 109
REMARK 465 GLY F 395
REMARK 465 GLU F 396
REMARK 465 GLY F 397
REMARK 465 GLN F 398
REMARK 465 GLN F 399
REMARK 465 HIS F 400
REMARK 465 HIS F 401
REMARK 465 LEU F 402
REMARK 465 GLY F 403
REMARK 465 GLY F 404
REMARK 465 ALA F 405
REMARK 465 LYS F 406
REMARK 465 VAL G 5
REMARK 465 GLU G 6
REMARK 465 VAL H 5
REMARK 465 GLU H 6
REMARK 465 VAL I 5
REMARK 465 GLU I 6
REMARK 465 VAL J 5
REMARK 465 GLU J 6
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 SER A 164 -31.64 -135.36
REMARK 500 GLU B 245 67.12 39.74
REMARK 500 GLN B 256 -32.15 -156.47
REMARK 500 LYS B 265 -175.05 -66.95
REMARK 500 ASP B 281 119.88 84.22
REMARK 500 ARG B 380 101.44 -161.76
REMARK 500 LYS B 392 61.34 -101.28
REMARK 500 ASN B 405 -92.26 -99.78
REMARK 500 ARG B 406 62.13 -156.35
REMARK 500 ASN B 439 -5.53 -57.64
REMARK 500 TRP B 440 -50.15 -123.10
REMARK 500 GLU C 97 118.22 90.95
REMARK 500 ASN C 175 -70.07 -86.07
REMARK 500 LEU C 198 -33.09 -168.30
REMARK 500 SER C 240 102.97 -17.28
REMARK 500 ASN C 254 13.23 -141.85
REMARK 500 ASP C 272 39.37 -99.08
REMARK 500 ASP C 285 22.92 -74.45
REMARK 500 ASP C 288 88.44 -68.39
REMARK 500 ASP C 298 147.02 -179.58
REMARK 500 PHE C 304 3.75 -69.94
REMARK 500 ASN C 317 76.37 -161.51
REMARK 500 ASN C 337 -95.52 -106.73
REMARK 500 LYS C 338 57.76 -151.39
REMARK 500 ARG C 375 7.85 -63.32
REMARK 500 ASN C 390 -9.69 -55.91
REMARK 500 SER D 164 -40.45 -135.15
REMARK 500 GLN E 256 -30.48 -154.98
REMARK 500 ASP E 257 -154.61 -133.73
REMARK 500 ASP E 281 80.96 29.64
REMARK 500 ARG E 380 94.55 -160.56
REMARK 500 ASN E 405 -83.02 -122.22
REMARK 500 ARG E 406 59.80 -166.86
REMARK 500 ASP E 425 33.52 -82.86
REMARK 500 MET E 426 -32.67 -131.65
REMARK 500 LYS F 173 31.02 -90.96
REMARK 500 SER F 187 14.29 -140.82
REMARK 500 LEU F 198 -20.66 -159.92
REMARK 500 ASP F 199 10.99 -149.63
REMARK 500 SER F 240 121.00 -21.23
REMARK 500 TRP F 253 32.76 -92.55
REMARK 500 PRO F 299 -15.87 -43.50
REMARK 500 ASN F 317 85.43 -158.53
REMARK 500 ASN F 337 -88.82 -116.88
REMARK 500 LYS F 338 61.16 -164.44
REMARK 500 HIS F 343 76.07 -151.78
REMARK 500 ASN F 390 -3.76 -58.21
REMARK 500 PRO G 2 -145.44 -95.70
REMARK 500 ARG J 3 103.71 -175.19
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 CA B 600 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 381 OD2
REMARK 620 2 ASP B 381 OD1 51.1
REMARK 620 3 ASP B 383 OD1 124.0 73.1
REMARK 620 4 TRP B 385 O 146.6 148.4 81.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 601 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 318 OD1
REMARK 620 2 ASP C 318 OD2 47.6
REMARK 620 3 ASP C 320 OD1 71.2 103.2
REMARK 620 4 PHE C 322 O 136.9 129.4 69.0
REMARK 620 5 GLY C 324 O 101.2 68.0 87.9 61.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 602 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 381 OD1
REMARK 620 2 ASP E 381 OD2 48.8
REMARK 620 3 ASP E 383 OD1 65.9 87.4
REMARK 620 4 TRP E 385 O 142.1 144.9 78.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 603 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 318 OD2
REMARK 620 2 ASP F 318 OD1 48.6
REMARK 620 3 ASP F 320 OD1 94.8 66.1
REMARK 620 4 PHE F 322 O 154.8 138.6 75.8
REMARK 620 5 GLY F 324 O 73.8 113.8 94.0 83.5
REMARK 620 6 HOH F 627 O 111.8 65.1 68.4 86.8 161.6
REMARK 620 N 1 2 3 4 5
DBREF 2FFD A 126 191 UNP P02671 FIBA_HUMAN 145 210
DBREF 2FFD D 126 191 UNP P02671 FIBA_HUMAN 145 210
DBREF 2FFD B 149 461 UNP P02675 FIBB_HUMAN 187 499
DBREF 2FFD E 149 461 UNP P02675 FIBB_HUMAN 187 499
DBREF 2FFD C 96 406 UNP P02679 FIBG_HUMAN 122 432
DBREF 2FFD F 96 406 UNP P02679 FIBG_HUMAN 122 432
DBREF 2FFD G 1 6 PDB 2FFD 2FFD 1 6
DBREF 2FFD H 1 6 PDB 2FFD 2FFD 1 6
DBREF 2FFD I 1 6 PDB 2FFD 2FFD 1 6
DBREF 2FFD J 1 6 PDB 2FFD 2FFD 1 6
SEQRES 1 A 66 VAL ILE GLU LYS VAL GLN HIS ILE GLN LEU LEU GLN LYS
SEQRES 2 A 66 ASN VAL ARG ALA GLN LEU VAL ASP MET LYS ARG LEU GLU
SEQRES 3 A 66 VAL ASP ILE ASP ILE LYS ILE ARG SER CYS ARG GLY SER
SEQRES 4 A 66 CYS SER ARG ALA LEU ALA ARG GLU VAL ASP LEU LYS ASP
SEQRES 5 A 66 TYR GLU ASP GLN GLN LYS GLN LEU GLU GLN VAL ILE ALA
SEQRES 6 A 66 LYS
SEQRES 1 B 313 HIS GLN LEU TYR ILE ASP GLU THR VAL ASN SER ASN ILE
SEQRES 2 B 313 PRO THR ASN LEU ARG VAL LEU ARG SER ILE LEU GLU ASN
SEQRES 3 B 313 LEU ARG SER LYS ILE GLN LYS LEU GLU SER ASP VAL SER
SEQRES 4 B 313 ALA GLN MET GLU TYR CYS ARG THR PRO CYS THR VAL SER
SEQRES 5 B 313 CYS ASN ILE PRO VAL VAL SER GLY LYS GLU CYS GLU GLU
SEQRES 6 B 313 ILE ILE ARG LYS GLY GLY GLU THR SER GLU MET TYR LEU
SEQRES 7 B 313 ILE GLN PRO ASP SER SER VAL LYS PRO TYR ARG VAL TYR
SEQRES 8 B 313 CYS ASP MET ASN THR GLU ASN GLY GLY TRP THR VAL ILE
SEQRES 9 B 313 GLN ASN ARG GLN ASP GLY SER VAL ASP PHE GLY ARG LYS
SEQRES 10 B 313 TRP ASP PRO TYR LYS GLN GLY PHE GLY ASN VAL ALA THR
SEQRES 11 B 313 ASN THR ASP GLY LYS ASN TYR CYS GLY LEU PRO GLY GLU
SEQRES 12 B 313 TYR TRP LEU GLY ASN ASP LYS ILE SER GLN LEU THR ARG
SEQRES 13 B 313 MET GLY PRO THR GLU LEU LEU ILE GLU MET GLU ASP TRP
SEQRES 14 B 313 LYS GLY ASP LYS VAL LYS ALA HIS TYR GLY GLY PHE THR
SEQRES 15 B 313 VAL GLN ASN GLU ALA ASN LYS TYR GLN ILE SER VAL ASN
SEQRES 16 B 313 LYS TYR ARG GLY THR ALA GLY ASN ALA LEU MET ASP GLY
SEQRES 17 B 313 ALA SER GLN LEU MET GLY GLU ASN ARG THR MET THR ILE
SEQRES 18 B 313 HIS ASN GLY MET PHE PHE SER THR TYR ASP ARG ASP ASN
SEQRES 19 B 313 ASP GLY TRP LEU THR SER ASP PRO ARG LYS GLN CYS SER
SEQRES 20 B 313 LYS GLU ASP GLY GLY GLY TRP TRP TYR ASN ARG CYS HIS
SEQRES 21 B 313 ALA ALA ASN PRO ASN GLY ARG TYR TYR TRP GLY GLY GLN
SEQRES 22 B 313 TYR THR TRP ASP MET ALA LYS HIS GLY THR ASP ASP GLY
SEQRES 23 B 313 VAL VAL TRP MET ASN TRP LYS GLY SER TRP TYR SER MET
SEQRES 24 B 313 ARG LYS MET SER MET LYS ILE ARG PRO PHE PHE PRO GLN
SEQRES 25 B 313 GLN
SEQRES 1 C 311 TYR GLU ALA SER ILE LEU THR HIS ASP SER SER ILE ARG
SEQRES 2 C 311 TYR LEU GLN GLU ILE TYR ASN SER ASN ASN GLN LYS ILE
SEQRES 3 C 311 VAL ASN LEU LYS GLU LYS VAL ALA GLN LEU GLU ALA GLN
SEQRES 4 C 311 CYS GLN GLU PRO CYS LYS ASP THR VAL GLN ILE HIS ASP
SEQRES 5 C 311 ILE THR GLY LYS ASP CYS GLN ASP ILE ALA ASN LYS GLY
SEQRES 6 C 311 ALA LYS GLN SER GLY LEU TYR PHE ILE LYS PRO LEU LYS
SEQRES 7 C 311 ALA ASN GLN GLN PHE LEU VAL TYR CYS GLU ILE ASP GLY
SEQRES 8 C 311 SER GLY ASN GLY TRP THR VAL PHE GLN LYS ARG LEU ASP
SEQRES 9 C 311 GLY SER VAL ASP PHE LYS LYS ASN TRP ILE GLN TYR LYS
SEQRES 10 C 311 GLU GLY PHE GLY HIS LEU SER PRO THR GLY THR THR GLU
SEQRES 11 C 311 PHE TRP LEU GLY ASN GLU LYS ILE HIS LEU ILE SER THR
SEQRES 12 C 311 GLN SER ALA ILE PRO TYR ALA LEU ARG VAL GLU LEU GLU
SEQRES 13 C 311 ASP TRP ASN GLY ARG THR SER THR ALA ASP TYR ALA MET
SEQRES 14 C 311 PHE LYS VAL GLY PRO GLU ALA ASP LYS TYR ARG LEU THR
SEQRES 15 C 311 TYR ALA TYR PHE ALA GLY GLY ASP ALA GLY ASP ALA PHE
SEQRES 16 C 311 ASP GLY PHE ASP PHE GLY ASP ASP PRO SER ASP LYS PHE
SEQRES 17 C 311 PHE THR SER HIS ASN GLY MET GLN PHE SER THR TRP ASP
SEQRES 18 C 311 ASN ASP ASN ASP LYS PHE GLU GLY ASN CYS ALA GLU GLN
SEQRES 19 C 311 ASP GLY SER GLY TRP TRP MET ASN LYS CYS HIS ALA GLY
SEQRES 20 C 311 HIS LEU ASN GLY VAL TYR TYR GLN GLY GLY THR TYR SER
SEQRES 21 C 311 LYS ALA SER THR PRO ASN GLY TYR ASP ASN GLY ILE ILE
SEQRES 22 C 311 TRP ALA THR TRP LYS THR ARG TRP TYR SER MET LYS LYS
SEQRES 23 C 311 THR THR MET LYS ILE ILE PRO PHE ASN ARG LEU THR ILE
SEQRES 24 C 311 GLY GLU GLY GLN GLN HIS HIS LEU GLY GLY ALA LYS
SEQRES 1 D 66 VAL ILE GLU LYS VAL GLN HIS ILE GLN LEU LEU GLN LYS
SEQRES 2 D 66 ASN VAL ARG ALA GLN LEU VAL ASP MET LYS ARG LEU GLU
SEQRES 3 D 66 VAL ASP ILE ASP ILE LYS ILE ARG SER CYS ARG GLY SER
SEQRES 4 D 66 CYS SER ARG ALA LEU ALA ARG GLU VAL ASP LEU LYS ASP
SEQRES 5 D 66 TYR GLU ASP GLN GLN LYS GLN LEU GLU GLN VAL ILE ALA
SEQRES 6 D 66 LYS
SEQRES 1 E 313 HIS GLN LEU TYR ILE ASP GLU THR VAL ASN SER ASN ILE
SEQRES 2 E 313 PRO THR ASN LEU ARG VAL LEU ARG SER ILE LEU GLU ASN
SEQRES 3 E 313 LEU ARG SER LYS ILE GLN LYS LEU GLU SER ASP VAL SER
SEQRES 4 E 313 ALA GLN MET GLU TYR CYS ARG THR PRO CYS THR VAL SER
SEQRES 5 E 313 CYS ASN ILE PRO VAL VAL SER GLY LYS GLU CYS GLU GLU
SEQRES 6 E 313 ILE ILE ARG LYS GLY GLY GLU THR SER GLU MET TYR LEU
SEQRES 7 E 313 ILE GLN PRO ASP SER SER VAL LYS PRO TYR ARG VAL TYR
SEQRES 8 E 313 CYS ASP MET ASN THR GLU ASN GLY GLY TRP THR VAL ILE
SEQRES 9 E 313 GLN ASN ARG GLN ASP GLY SER VAL ASP PHE GLY ARG LYS
SEQRES 10 E 313 TRP ASP PRO TYR LYS GLN GLY PHE GLY ASN VAL ALA THR
SEQRES 11 E 313 ASN THR ASP GLY LYS ASN TYR CYS GLY LEU PRO GLY GLU
SEQRES 12 E 313 TYR TRP LEU GLY ASN ASP LYS ILE SER GLN LEU THR ARG
SEQRES 13 E 313 MET GLY PRO THR GLU LEU LEU ILE GLU MET GLU ASP TRP
SEQRES 14 E 313 LYS GLY ASP LYS VAL LYS ALA HIS TYR GLY GLY PHE THR
SEQRES 15 E 313 VAL GLN ASN GLU ALA ASN LYS TYR GLN ILE SER VAL ASN
SEQRES 16 E 313 LYS TYR ARG GLY THR ALA GLY ASN ALA LEU MET ASP GLY
SEQRES 17 E 313 ALA SER GLN LEU MET GLY GLU ASN ARG THR MET THR ILE
SEQRES 18 E 313 HIS ASN GLY MET PHE PHE SER THR TYR ASP ARG ASP ASN
SEQRES 19 E 313 ASP GLY TRP LEU THR SER ASP PRO ARG LYS GLN CYS SER
SEQRES 20 E 313 LYS GLU ASP GLY GLY GLY TRP TRP TYR ASN ARG CYS HIS
SEQRES 21 E 313 ALA ALA ASN PRO ASN GLY ARG TYR TYR TRP GLY GLY GLN
SEQRES 22 E 313 TYR THR TRP ASP MET ALA LYS HIS GLY THR ASP ASP GLY
SEQRES 23 E 313 VAL VAL TRP MET ASN TRP LYS GLY SER TRP TYR SER MET
SEQRES 24 E 313 ARG LYS MET SER MET LYS ILE ARG PRO PHE PHE PRO GLN
SEQRES 25 E 313 GLN
SEQRES 1 F 311 TYR GLU ALA SER ILE LEU THR HIS ASP SER SER ILE ARG
SEQRES 2 F 311 TYR LEU GLN GLU ILE TYR ASN SER ASN ASN GLN LYS ILE
SEQRES 3 F 311 VAL ASN LEU LYS GLU LYS VAL ALA GLN LEU GLU ALA GLN
SEQRES 4 F 311 CYS GLN GLU PRO CYS LYS ASP THR VAL GLN ILE HIS ASP
SEQRES 5 F 311 ILE THR GLY LYS ASP CYS GLN ASP ILE ALA ASN LYS GLY
SEQRES 6 F 311 ALA LYS GLN SER GLY LEU TYR PHE ILE LYS PRO LEU LYS
SEQRES 7 F 311 ALA ASN GLN GLN PHE LEU VAL TYR CYS GLU ILE ASP GLY
SEQRES 8 F 311 SER GLY ASN GLY TRP THR VAL PHE GLN LYS ARG LEU ASP
SEQRES 9 F 311 GLY SER VAL ASP PHE LYS LYS ASN TRP ILE GLN TYR LYS
SEQRES 10 F 311 GLU GLY PHE GLY HIS LEU SER PRO THR GLY THR THR GLU
SEQRES 11 F 311 PHE TRP LEU GLY ASN GLU LYS ILE HIS LEU ILE SER THR
SEQRES 12 F 311 GLN SER ALA ILE PRO TYR ALA LEU ARG VAL GLU LEU GLU
SEQRES 13 F 311 ASP TRP ASN GLY ARG THR SER THR ALA ASP TYR ALA MET
SEQRES 14 F 311 PHE LYS VAL GLY PRO GLU ALA ASP LYS TYR ARG LEU THR
SEQRES 15 F 311 TYR ALA TYR PHE ALA GLY GLY ASP ALA GLY ASP ALA PHE
SEQRES 16 F 311 ASP GLY PHE ASP PHE GLY ASP ASP PRO SER ASP LYS PHE
SEQRES 17 F 311 PHE THR SER HIS ASN GLY MET GLN PHE SER THR TRP ASP
SEQRES 18 F 311 ASN ASP ASN ASP LYS PHE GLU GLY ASN CYS ALA GLU GLN
SEQRES 19 F 311 ASP GLY SER GLY TRP TRP MET ASN LYS CYS HIS ALA GLY
SEQRES 20 F 311 HIS LEU ASN GLY VAL TYR TYR GLN GLY GLY THR TYR SER
SEQRES 21 F 311 LYS ALA SER THR PRO ASN GLY TYR ASP ASN GLY ILE ILE
SEQRES 22 F 311 TRP ALA THR TRP LYS THR ARG TRP TYR SER MET LYS LYS
SEQRES 23 F 311 THR THR MET LYS ILE ILE PRO PHE ASN ARG LEU THR ILE
SEQRES 24 F 311 GLY GLU GLY GLN GLN HIS HIS LEU GLY GLY ALA LYS
SEQRES 1 G 6 GLY PRO ARG VAL VAL GLU
SEQRES 1 H 6 GLY PRO ARG VAL VAL GLU
SEQRES 1 I 6 GLY PRO ARG VAL VAL GLU
SEQRES 1 J 6 GLY PRO ARG VAL VAL GLU
MODRES 2FFD ASN B 364 ASN GLYCOSYLATION SITE
MODRES 2FFD ASN E 364 ASN GLYCOSYLATION SITE
HET NAG K 1 14
HET NAG K 2 14
HET FUC K 3 10
HET NAG L 1 14
HET NAG L 2 14
HET FUC L 3 10
HET CA B 600 1
HET CA C 601 1
HET CA E 602 1
HET CA F 603 1
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM FUC ALPHA-L-FUCOPYRANOSE
HETNAM CA CALCIUM ION
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L-
HETSYN 2 FUC FUCOSE; FUCOSE
FORMUL 11 NAG 4(C8 H15 N O6)
FORMUL 11 FUC 2(C6 H12 O5)
FORMUL 13 CA 4(CA 2+)
FORMUL 17 HOH *231(H2 O)
HELIX 1 1 ILE A 127 SER A 160 1 34
HELIX 2 2 ASP A 174 ALA A 190 1 17
HELIX 3 3 SER B 159 CYS B 193 1 35
HELIX 4 4 GLU B 210 LYS B 217 1 8
HELIX 5 5 ASN B 243 GLY B 247 5 5
HELIX 6 6 LYS B 265 GLY B 272 1 8
HELIX 7 7 GLY B 295 ARG B 304 1 10
HELIX 8 8 ASN B 333 LYS B 337 5 5
HELIX 9 9 ASN B 351 GLY B 356 1 6
HELIX 10 10 GLY B 362 MET B 367 1 6
HELIX 11 11 GLN B 393 ASP B 398 1 6
HELIX 12 12 MET B 438 GLY B 442 1 5
HELIX 13 13 LEU C 101 ALA C 133 1 33
HELIX 14 14 ASP C 152 LYS C 159 1 8
HELIX 15 15 ASN C 207 GLY C 214 1 8
HELIX 16 16 GLY C 229 THR C 238 1 10
HELIX 17 17 SER C 300 THR C 305 1 6
HELIX 18 18 ASN C 325 ASP C 330 1 6
HELIX 19 19 SER C 355 THR C 359 5 5
HELIX 20 20 ASN C 390 LEU C 392 5 3
HELIX 21 21 ILE D 133 VAL D 140 1 8
HELIX 22 22 ARG D 141 SER D 160 1 20
HELIX 23 23 ASP D 174 GLN D 187 1 14
HELIX 24 24 LEU E 165 CYS E 193 1 29
HELIX 25 25 GLU E 210 ARG E 216 1 7
HELIX 26 26 ASN E 243 GLY E 247 5 5
HELIX 27 27 LYS E 265 GLY E 272 1 8
HELIX 28 28 GLY E 295 MET E 305 1 11
HELIX 29 29 ASN E 333 LYS E 337 5 5
HELIX 30 30 ASN E 351 GLY E 356 1 6
HELIX 31 31 MET E 361 MET E 367 1 7
HELIX 32 32 GLN E 393 ASP E 398 1 6
HELIX 33 33 MET E 438 GLY E 442 1 5
HELIX 34 34 LEU F 110 ALA F 133 1 24
HELIX 35 35 GLN F 134 GLN F 136 5 3
HELIX 36 36 ASP F 152 LYS F 159 1 8
HELIX 37 37 ASN F 207 GLY F 214 1 8
HELIX 38 38 GLY F 229 THR F 238 1 10
HELIX 39 39 PRO F 269 LYS F 273 5 5
HELIX 40 40 ASP F 288 GLY F 292 5 5
HELIX 41 41 SER F 300 THR F 305 1 6
HELIX 42 42 ASN F 325 GLY F 331 1 7
HELIX 43 43 SER F 355 THR F 359 5 5
HELIX 44 44 ASN F 390 LEU F 392 5 3
SHEET 1 A 2 THR B 198 VAL B 199 0
SHEET 2 A 2 LYS C 140 ASP C 141 1 O LYS C 140 N VAL B 199
SHEET 1 B 6 ILE B 203 PRO B 204 0
SHEET 2 B 6 PHE C 215 LEU C 218 -1 O LEU C 218 N ILE B 203
SHEET 3 B 6 PHE C 226 TRP C 227 -1 O TRP C 227 N PHE C 215
SHEET 4 B 6 GLY C 190 ARG C 197 -1 N LYS C 196 O PHE C 226
SHEET 5 B 6 PHE C 178 ILE C 184 -1 N GLU C 183 O TRP C 191
SHEET 6 B 6 GLY C 165 ILE C 169 -1 N ILE C 169 O PHE C 178
SHEET 1 C 8 ILE B 203 PRO B 204 0
SHEET 2 C 8 PHE C 215 LEU C 218 -1 O LEU C 218 N ILE B 203
SHEET 3 C 8 PHE C 226 TRP C 227 -1 O TRP C 227 N PHE C 215
SHEET 4 C 8 GLY C 190 ARG C 197 -1 N LYS C 196 O PHE C 226
SHEET 5 C 8 LYS C 381 PRO C 388 -1 O THR C 382 N ARG C 197
SHEET 6 C 8 TYR C 244 GLU C 251 -1 N ARG C 247 O LYS C 385
SHEET 7 C 8 THR C 257 ALA C 263 -1 O SER C 258 N LEU C 250
SHEET 8 C 8 TYR C 280 GLY C 283 -1 O ALA C 282 N ASP C 261
SHEET 1 D 5 MET B 224 ILE B 227 0
SHEET 2 D 5 TYR B 236 ASP B 241 -1 O VAL B 238 N TYR B 225
SHEET 3 D 5 TRP B 249 ARG B 255 -1 O TRP B 249 N ASP B 241
SHEET 4 D 5 TYR B 292 TRP B 293 -1 O TYR B 292 N ASN B 254
SHEET 5 D 5 PHE B 273 GLY B 274 -1 N PHE B 273 O TRP B 293
SHEET 1 E 7 MET B 224 ILE B 227 0
SHEET 2 E 7 TYR B 236 ASP B 241 -1 O VAL B 238 N TYR B 225
SHEET 3 E 7 TRP B 249 ARG B 255 -1 O TRP B 249 N ASP B 241
SHEET 4 E 7 LYS B 449 PRO B 456 -1 O ILE B 454 N THR B 250
SHEET 5 E 7 THR B 308 GLU B 315 -1 N LEU B 311 O LYS B 453
SHEET 6 E 7 LYS B 321 VAL B 331 -1 O TYR B 326 N LEU B 310
SHEET 7 E 7 ILE B 340 GLY B 347 -1 O LYS B 344 N GLY B 327
SHEET 1 F 2 ALA B 277 THR B 278 0
SHEET 2 F 2 LEU B 288 PRO B 289 -1 O LEU B 288 N THR B 278
SHEET 1 G 2 ALA B 410 ASN B 411 0
SHEET 2 G 2 VAL B 436 TRP B 437 -1 O VAL B 436 N ASN B 411
SHEET 1 H 2 LYS C 266 VAL C 267 0
SHEET 2 H 2 LEU C 276 THR C 277 -1 O THR C 277 N LYS C 266
SHEET 1 I 2 THR E 198 VAL E 199 0
SHEET 2 I 2 LYS F 140 ASP F 141 1 O LYS F 140 N VAL E 199
SHEET 1 J 8 ILE E 203 PRO E 204 0
SHEET 2 J 8 PHE F 215 LEU F 218 -1 O LEU F 218 N ILE E 203
SHEET 3 J 8 PHE F 226 TRP F 227 -1 O TRP F 227 N PHE F 215
SHEET 4 J 8 GLY F 190 ARG F 197 -1 N LYS F 196 O PHE F 226
SHEET 5 J 8 LYS F 381 PRO F 388 -1 O MET F 384 N PHE F 194
SHEET 6 J 8 TYR F 244 GLU F 251 -1 N ALA F 245 O ILE F 387
SHEET 7 J 8 THR F 257 VAL F 267 -1 O ALA F 260 N VAL F 248
SHEET 8 J 8 LEU F 276 THR F 277 -1 O THR F 277 N LYS F 266
SHEET 1 K 7 GLY F 165 ILE F 169 0
SHEET 2 K 7 PHE F 178 ILE F 184 -1 O VAL F 180 N TYR F 167
SHEET 3 K 7 GLY F 190 ARG F 197 -1 O TRP F 191 N GLU F 183
SHEET 4 K 7 LYS F 381 PRO F 388 -1 O MET F 384 N PHE F 194
SHEET 5 K 7 TYR F 244 GLU F 251 -1 N ALA F 245 O ILE F 387
SHEET 6 K 7 THR F 257 VAL F 267 -1 O ALA F 260 N VAL F 248
SHEET 7 K 7 TYR F 280 PHE F 281 -1 O TYR F 280 N ALA F 263
SHEET 1 L 5 GLU E 223 ILE E 227 0
SHEET 2 L 5 TYR E 236 ASP E 241 -1 O TYR E 236 N ILE E 227
SHEET 3 L 5 TRP E 249 ARG E 255 -1 O TRP E 249 N ASP E 241
SHEET 4 L 5 TYR E 292 TRP E 293 -1 O TYR E 292 N ASN E 254
SHEET 5 L 5 PHE E 273 GLY E 274 -1 N PHE E 273 O TRP E 293
SHEET 1 M 7 GLU E 223 ILE E 227 0
SHEET 2 M 7 TYR E 236 ASP E 241 -1 O TYR E 236 N ILE E 227
SHEET 3 M 7 TRP E 249 ARG E 255 -1 O TRP E 249 N ASP E 241
SHEET 4 M 7 LYS E 449 PRO E 456 -1 O ILE E 454 N THR E 250
SHEET 5 M 7 THR E 308 GLU E 315 -1 N LEU E 311 O LYS E 453
SHEET 6 M 7 LYS E 321 VAL E 331 -1 O ALA E 324 N ILE E 312
SHEET 7 M 7 ILE E 340 GLY E 347 -1 O SER E 341 N THR E 330
SHEET 1 N 2 ALA E 277 THR E 278 0
SHEET 2 N 2 LEU E 288 PRO E 289 -1 O LEU E 288 N THR E 278
SHEET 1 O 2 ALA E 410 ASN E 411 0
SHEET 2 O 2 VAL E 436 TRP E 437 -1 O VAL E 436 N ASN E 411
SHEET 1 P 2 GLY F 342 HIS F 343 0
SHEET 2 P 2 ILE F 368 TRP F 369 -1 O ILE F 368 N HIS F 343
SSBOND 1 CYS A 161 CYS C 135 1555 1555 2.03
SSBOND 2 CYS A 165 CYS B 193 1555 1555 2.04
SSBOND 3 CYS B 197 CYS C 139 1555 1555 2.04
SSBOND 4 CYS B 201 CYS B 286 1555 1555 2.03
SSBOND 5 CYS B 211 CYS B 240 1555 1555 2.03
SSBOND 6 CYS B 394 CYS B 407 1555 1555 2.03
SSBOND 7 CYS C 153 CYS C 182 1555 1555 2.02
SSBOND 8 CYS C 326 CYS C 339 1555 1555 2.04
SSBOND 9 CYS D 161 CYS F 135 1555 1555 2.02
SSBOND 10 CYS D 165 CYS E 193 1555 1555 2.03
SSBOND 11 CYS E 197 CYS F 139 1555 1555 2.03
SSBOND 12 CYS E 201 CYS E 286 1555 1555 2.04
SSBOND 13 CYS E 211 CYS E 240 1555 1555 2.03
SSBOND 14 CYS E 394 CYS E 407 1555 1555 2.06
SSBOND 15 CYS F 153 CYS F 182 1555 1555 2.01
SSBOND 16 CYS F 326 CYS F 339 1555 1555 2.04
LINK ND2 ASN B 364 C1 NAG K 1 1555 1555 1.42
LINK ND2 ASN E 364 C1 NAG L 1 1555 1555 1.46
LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.39
LINK O6 NAG K 1 C1 FUC K 3 1555 1555 1.40
LINK O4 NAG L 1 C1 NAG L 2 1555 1555 1.40
LINK O6 NAG L 1 C1 FUC L 3 1555 1555 1.42
LINK OD2 ASP B 381 CA CA B 600 1555 1555 2.47
LINK OD1 ASP B 381 CA CA B 600 1555 1555 2.61
LINK OD1 ASP B 383 CA CA B 600 1555 1555 2.34
LINK O TRP B 385 CA CA B 600 1555 1555 2.37
LINK OD1 ASP C 318 CA CA C 601 1555 1555 2.62
LINK OD2 ASP C 318 CA CA C 601 1555 1555 2.79
LINK OD1 ASP C 320 CA CA C 601 1555 1555 2.42
LINK O PHE C 322 CA CA C 601 1555 1555 2.33
LINK O GLY C 324 CA CA C 601 1555 1555 2.61
LINK OD1 ASP E 381 CA CA E 602 1555 1555 2.80
LINK OD2 ASP E 381 CA CA E 602 1555 1555 2.23
LINK OD1 ASP E 383 CA CA E 602 1555 1555 2.45
LINK O TRP E 385 CA CA E 602 1555 1555 2.36
LINK OD2 ASP F 318 CA CA F 603 1555 1555 2.80
LINK OD1 ASP F 318 CA CA F 603 1555 1555 2.53
LINK OD1 ASP F 320 CA CA F 603 1555 1555 2.41
LINK O PHE F 322 CA CA F 603 1555 1555 2.29
LINK O GLY F 324 CA CA F 603 1555 1555 2.17
LINK CA CA F 603 O HOH F 627 1555 1555 2.31
CISPEP 1 ARG B 406 CYS B 407 0 -2.90
CISPEP 2 LYS C 338 CYS C 339 0 -1.70
CISPEP 3 ARG E 406 CYS E 407 0 -3.21
CISPEP 4 LYS F 338 CYS F 339 0 -1.11
CRYST1 89.521 94.652 227.490 90.00 90.00 90.00 P 21 21 21 16
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 0.011170 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010560 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004400 0.00000
(ATOM LINES ARE NOT SHOWN.)
END