HEADER MEMBRANE PROTEIN/HYDROLASE 07-MAY-03 1P8V
TITLE CRYSTAL STRUCTURE OF THE COMPLEX OF PLATELET RECEPTOR GPIB-ALPHA AND
TITLE 2 ALPHA-THROMBIN AT 2.6A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PLATELET GLYCOPROTEIN IB ALPHA CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: GLYCOPROTEIN 1B ALPHA;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: PROTHROMBIN;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: ALPHA THROMBIN, LIGHT CHAIN;
COMPND 11 SYNONYM: COAGULATION FACTOR II;
COMPND 12 EC: 3.4.21.5;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: PROTHROMBIN;
COMPND 15 CHAIN: C;
COMPND 16 FRAGMENT: ALPHA THROMBIN, HEAVY CHAIN;
COMPND 17 SYNONYM: COAGULATION FACTOR II;
COMPND 18 EC: 3.4.21.5
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: GP1BA;
SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 9 EXPRESSION_SYSTEM_ORGAN: 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 OTHER_DETAILS: ISOLATED FROM HUMAN PLASMA;
SOURCE 15 MOL_ID: 3;
SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 17 ORGANISM_COMMON: HUMAN;
SOURCE 18 ORGANISM_TAXID: 9606;
SOURCE 19 OTHER_DETAILS: ISOLATED FROM HUMAN PLASMA
KEYWDS PLATELET GLYCOPROTEIN RECEPTOR, LEUCINE RICH REPEAT DOMAIN, MEMBRANE
KEYWDS 2 PROTEIN-HYDROLASE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.J.DUMAS,R.KUMAR,J.SEEHRA,W.S.SOMERS,L.MOSYAK
REVDAT 3 13-JUL-11 1P8V 1 VERSN
REVDAT 2 24-FEB-09 1P8V 1 VERSN
REVDAT 1 22-JUL-03 1P8V 0
JRNL AUTH J.J.DUMAS,R.KUMAR,J.SEEHRA,W.S.SOMERS,L.MOSYAK
JRNL TITL CRYSTAL STRUCTURE OF THE GPIBALPHA-THROMBIN COMPLEX
JRNL TITL 2 ESSENTIAL FOR PLATELET AGGREGATION
JRNL REF SCIENCE V. 301 222 2003
JRNL REFN ISSN 0036-8075
JRNL PMID 12855811
JRNL DOI 10.1126/SCIENCE.1083917
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 27605
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 SET) : 0.207
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.400
REMARK 3 FREE R VALUE TEST SET COUNT : 1903
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.76
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1903
REMARK 3 BIN R VALUE (WORKING SET) : 0.2810
REMARK 3 BIN FREE R VALUE : 0.3070
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 6.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 284
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.018
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4449
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 36
REMARK 3 SOLVENT ATOMS : 217
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 41.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -10.09000
REMARK 3 B22 (A**2) : -0.51000
REMARK 3 B33 (A**2) : 10.59000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.30
REMARK 3 ESD FROM SIGMAA (A) : 0.36
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.35
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.37
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.40
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.90
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.437 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.351 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.349 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.522 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 37.85
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1P8V COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-MAY-03.
REMARK 100 THE RCSB ID CODE IS RCSB019153.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-DEC-02
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : SI(220)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28711
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.39200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
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 (%): 65.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 14% PEG 400, PH 6.0, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 291K, PH 6.00
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 23.54750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 88.12550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.88500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 88.12550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.54750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.88500
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 300 REMARK: THE SECOND PART OF THE BIOLOGICAL ASSEMBLY IS GENERATED BY
REMARK 300 THE CRYSTALLOGRAPHIC SYMMETRY OPERATION: -X, Y+0.5, -Z+0.5
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 -1.000000 0.000000 0.000000 47.09500
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 55.88500
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 88.12550
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 THR C 147
REMARK 465 TRP C 148
REMARK 465 THR C 149
REMARK 465 ALA C 150
REMARK 465 ASN C 151
REMARK 465 VAL C 152
REMARK 465 GLY C 153
REMARK 465 LYS C 154
REMARK 465 GLU C 259
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 ASP A 272 CG OD1 OD2
REMARK 470 LYS C 145 CG CD CE NZ
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 ALA A 10 -131.58 68.01
REMARK 500 LYS A 19 76.07 31.86
REMARK 500 LEU A 42 62.09 -107.39
REMARK 500 LEU A 43 75.62 -102.09
REMARK 500 TYR A 54 75.86 -107.57
REMARK 500 ASN A 110 -144.97 -126.83
REMARK 500 LEU A 123 49.30 -92.33
REMARK 500 ASN A 134 -163.44 -109.96
REMARK 500 ASN A 158 -152.70 -119.20
REMARK 500 ASN A 182 -156.51 -114.42
REMARK 500 PRO A 206 49.83 -77.99
REMARK 500 ASN A 242 94.97 -171.07
REMARK 500 ASP A 249 16.63 56.81
REMARK 500 ASP A 252 4.05 -59.75
REMARK 500 PRO A 265 -151.04 -53.50
REMARK 500 ASP A 269 145.89 137.88
REMARK 500 TYS A 276 -166.00 -105.63
REMARK 500 CYS B 4 154.53 -47.10
REMARK 500 PHE B 10 -89.26 -132.07
REMARK 500 LYS B 12 2.75 -60.66
REMARK 500 LYS B 13 28.13 -145.87
REMARK 500 SER C 12 59.80 -146.67
REMARK 500 TYR C 47 82.91 -163.50
REMARK 500 ASN C 53 79.18 -160.19
REMARK 500 HIS C 66 -58.51 -131.59
REMARK 500 GLU C 72 79.46 -66.68
REMARK 500 ILE C 75 -56.70 -121.76
REMARK 500 GLU C 94 -55.21 -121.26
REMARK 500 ASN C 95 22.64 -147.33
REMARK 500 SER C 112 -153.51 -148.31
REMARK 500 GLU C 202 113.01 -31.59
REMARK 500 SER C 226 -65.89 -106.74
REMARK 500 HIS C 242 98.71 -69.94
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 A 520 DISTANCE = 5.40 ANGSTROMS
REMARK 525 HOH C 568 DISTANCE = 5.34 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 C 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DFP C 500
DBREF 1P8V A 1 278 UNP P07359 GP1BA_HUMAN 17 294
DBREF 1P8V B 1 29 UNP P00734 THRB_HUMAN 333 361
DBREF 1P8V C 1 258 UNP P00734 THRB_HUMAN 364 621
SEQADV 1P8V ASP A 21 UNP P07359 ASN 37 ENGINEERED
SEQADV 1P8V TYS A 276 UNP P07359 TYR 292 MODIFIED RESIDUE
SEQADV 1P8V TYS A 279 UNP P07359 CLONING ARTIFACT
SEQADV 1P8V GLU C 259 UNP P00734 CLONING ARTIFACT
SEQRES 1 A 279 HIS PRO ILE CYS GLU VAL SER LYS VAL ALA SER HIS LEU
SEQRES 2 A 279 GLU VAL ASN CYS ASP LYS ARG ASP LEU THR ALA LEU PRO
SEQRES 3 A 279 PRO ASP LEU PRO LYS ASP THR THR ILE LEU HIS LEU SER
SEQRES 4 A 279 GLU ASN LEU LEU TYR THR PHE SER LEU ALA THR LEU MET
SEQRES 5 A 279 PRO TYR THR ARG LEU THR GLN LEU ASN LEU ASP ARG CYS
SEQRES 6 A 279 GLU LEU THR LYS LEU GLN VAL ASP GLY THR LEU PRO VAL
SEQRES 7 A 279 LEU GLY THR LEU ASP LEU SER HIS ASN GLN LEU GLN SER
SEQRES 8 A 279 LEU PRO LEU LEU GLY GLN THR LEU PRO ALA LEU THR VAL
SEQRES 9 A 279 LEU ASP VAL SER PHE ASN ARG LEU THR SER LEU PRO LEU
SEQRES 10 A 279 GLY ALA LEU ARG GLY LEU GLY GLU LEU GLN GLU LEU TYR
SEQRES 11 A 279 LEU LYS GLY ASN GLU LEU LYS THR LEU PRO PRO GLY LEU
SEQRES 12 A 279 LEU THR PRO THR PRO LYS LEU GLU LYS LEU SER LEU ALA
SEQRES 13 A 279 ASN ASN ASN LEU THR GLU LEU PRO ALA GLY LEU LEU ASN
SEQRES 14 A 279 GLY LEU GLU ASN LEU ASP THR LEU LEU LEU GLN GLU ASN
SEQRES 15 A 279 SER LEU TYR THR ILE PRO LYS GLY PHE PHE GLY SER HIS
SEQRES 16 A 279 LEU LEU PRO PHE ALA PHE LEU HIS GLY ASN PRO TRP LEU
SEQRES 17 A 279 CYS ASN CYS GLU ILE LEU TYR PHE ARG ARG TRP LEU GLN
SEQRES 18 A 279 ASP ASN ALA GLU ASN VAL TYR VAL TRP LYS GLN GLY VAL
SEQRES 19 A 279 ASP VAL LYS ALA MET THR SER ASN VAL ALA SER VAL GLN
SEQRES 20 A 279 CYS ASP ASN SER ASP LYS PHE PRO VAL TYR LYS TYR PRO
SEQRES 21 A 279 GLY LYS GLY CYS PRO THR LEU GLY ASP GLU GLY ASP THR
SEQRES 22 A 279 ASP LEU TYS ASP TYR TYS
SEQRES 1 B 29 GLU ALA ASP CYS GLY LEU ARG PRO LEU PHE GLU LYS LYS
SEQRES 2 B 29 SER LEU GLU ASP LYS THR GLU ARG GLU LEU LEU GLU SER
SEQRES 3 B 29 TYR ILE ASP
SEQRES 1 C 259 ILE VAL GLU GLY SER ASP ALA GLU ILE GLY MET SER PRO
SEQRES 2 C 259 TRP GLN VAL MET LEU PHE ARG LYS SER PRO GLN GLU LEU
SEQRES 3 C 259 LEU CYS GLY ALA SER LEU ILE SER ASP ARG TRP VAL LEU
SEQRES 4 C 259 THR ALA ALA HIS CYS LEU LEU TYR PRO PRO TRP ASP LYS
SEQRES 5 C 259 ASN PHE THR GLU ASN ASP LEU LEU VAL ARG ILE GLY LYS
SEQRES 6 C 259 HIS SER ARG THR ARG TYR GLU ARG ASN ILE GLU LYS ILE
SEQRES 7 C 259 SER MET LEU GLU LYS ILE TYR ILE HIS PRO ARG TYR ASN
SEQRES 8 C 259 TRP ARG GLU ASN LEU ASP ARG ASP ILE ALA LEU MET LYS
SEQRES 9 C 259 LEU LYS LYS PRO VAL ALA PHE SER ASP TYR ILE HIS PRO
SEQRES 10 C 259 VAL CYS LEU PRO ASP ARG GLU THR ALA ALA SER LEU LEU
SEQRES 11 C 259 GLN ALA GLY TYR LYS GLY ARG VAL THR GLY TRP GLY ASN
SEQRES 12 C 259 LEU LYS GLU THR TRP THR ALA ASN VAL GLY LYS GLY GLN
SEQRES 13 C 259 PRO SER VAL LEU GLN VAL VAL ASN LEU PRO ILE VAL GLU
SEQRES 14 C 259 ARG PRO VAL CYS LYS ASP SER THR ARG ILE ARG ILE THR
SEQRES 15 C 259 ASP ASN MET PHE CYS ALA GLY TYR LYS PRO ASP GLU GLY
SEQRES 16 C 259 LYS ARG GLY ASP ALA CYS GLU GLY ASP SER GLY GLY PRO
SEQRES 17 C 259 PHE VAL MET LYS SER PRO PHE ASN ASN ARG TRP TYR GLN
SEQRES 18 C 259 MET GLY ILE VAL SER TRP GLY GLU GLY CYS ASP ARG ASP
SEQRES 19 C 259 GLY LYS TYR GLY PHE TYR THR HIS VAL PHE ARG LEU LYS
SEQRES 20 C 259 LYS TRP ILE GLN LYS VAL ILE ASP GLN PHE GLY GLU
MODRES 1P8V ASN C 53 ASN GLYCOSYLATION SITE
MODRES 1P8V TYS A 276 TYR O-SULFO-L-TYROSINE
MODRES 1P8V TYS A 279 TYR O-SULFO-L-TYROSINE
HET TYS A 276 16
HET TYS A 279 17
HET NAG C 300 14
HET MES A 400 12
HET DFP C 500 10
HETNAM TYS O-SULFO-L-TYROSINE
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETNAM DFP DIISOPROPYL PHOSPHONATE
FORMUL 1 TYS 2(C9 H11 N O6 S)
FORMUL 4 NAG C8 H15 N O6
FORMUL 5 MES C6 H13 N O4 S
FORMUL 6 DFP C6 H15 O3 P
FORMUL 7 HOH *217(H2 O)
HELIX 1 1 ALA A 49 MET A 52 5 4
HELIX 2 2 ASN A 210 GLU A 212 5 3
HELIX 3 3 ILE A 213 ASN A 223 1 11
HELIX 4 4 ALA A 224 VAL A 227 5 4
HELIX 5 5 ASP A 235 MET A 239 5 5
HELIX 6 6 ASN A 242 VAL A 246 5 5
HELIX 7 7 GLN A 247 SER A 251 5 5
HELIX 8 8 PRO A 255 TYR A 259 5 5
HELIX 9 9 PHE B 10 SER B 14 5 5
HELIX 10 10 THR B 19 GLU B 25 1 7
HELIX 11 11 SER B 26 ILE B 28 5 3
HELIX 12 12 ALA C 41 CYS C 44 5 4
HELIX 13 13 PRO C 48 ASP C 51 5 4
HELIX 14 14 THR C 55 ASN C 57 5 3
HELIX 15 15 ASP C 122 LEU C 130 1 9
HELIX 16 16 GLU C 169 ASP C 175 1 7
HELIX 17 17 LYS C 191 GLY C 195 5 5
HELIX 18 18 LEU C 246 GLY C 258 1 13
SHEET 1 A10 GLU A 5 VAL A 9 0
SHEET 2 A10 HIS A 12 ASN A 16 -1 O ASN A 16 N GLU A 5
SHEET 3 A10 ILE A 35 HIS A 37 1 O ILE A 35 N VAL A 15
SHEET 4 A10 GLN A 59 ASN A 61 1 O GLN A 59 N LEU A 36
SHEET 5 A10 THR A 81 ASP A 83 1 O THR A 81 N LEU A 60
SHEET 6 A10 VAL A 104 ASP A 106 1 O ASP A 106 N LEU A 82
SHEET 7 A10 GLU A 128 TYR A 130 1 O GLU A 128 N LEU A 105
SHEET 8 A10 LYS A 152 SER A 154 1 O SER A 154 N LEU A 129
SHEET 9 A10 THR A 176 LEU A 178 1 O LEU A 178 N LEU A 153
SHEET 10 A10 PHE A 199 PHE A 201 1 O PHE A 199 N LEU A 177
SHEET 1 B 2 THR A 45 SER A 47 0
SHEET 2 B 2 LYS A 69 GLN A 71 1 O GLN A 71 N PHE A 46
SHEET 1 C 8 SER C 5 ASP C 6 0
SHEET 2 C 8 GLN C 161 VAL C 168 -1 O VAL C 162 N SER C 5
SHEET 3 C 8 MET C 185 ALA C 188 -1 O CYS C 187 N VAL C 168
SHEET 4 C 8 GLY C 238 HIS C 242 -1 O TYR C 240 N PHE C 186
SHEET 5 C 8 TRP C 219 TRP C 227 -1 N TRP C 227 O PHE C 239
SHEET 6 C 8 PRO C 208 LYS C 212 -1 N MET C 211 O TYR C 220
SHEET 7 C 8 LYS C 135 GLY C 140 -1 N ARG C 137 O VAL C 210
SHEET 8 C 8 GLN C 161 VAL C 168 -1 O VAL C 163 N VAL C 138
SHEET 1 D 7 LYS C 77 SER C 79 0
SHEET 2 D 7 LEU C 59 ILE C 63 -1 N ILE C 63 O LYS C 77
SHEET 3 D 7 GLN C 15 ARG C 20 -1 N PHE C 19 O LEU C 60
SHEET 4 D 7 GLU C 25 LEU C 32 -1 O GLU C 25 N ARG C 20
SHEET 5 D 7 TRP C 37 THR C 40 -1 O LEU C 39 N SER C 31
SHEET 6 D 7 ALA C 101 LEU C 105 -1 O MET C 103 N VAL C 38
SHEET 7 D 7 LEU C 81 ILE C 86 -1 N TYR C 85 O LEU C 102
SHEET 1 E 2 LEU C 46 TYR C 47 0
SHEET 2 E 2 LYS C 52 ASN C 53 -1 O LYS C 52 N TYR C 47
SSBOND 1 CYS A 4 CYS A 17 1555 1555 2.03
SSBOND 2 CYS A 209 CYS A 248 1555 1555 2.04
SSBOND 3 CYS A 211 CYS A 264 1555 1555 2.04
SSBOND 4 CYS B 4 CYS C 119 1555 1555 2.01
SSBOND 5 CYS C 28 CYS C 44 1555 1555 2.03
SSBOND 6 CYS C 173 CYS C 187 1555 1555 2.04
SSBOND 7 CYS C 201 CYS C 231 1555 1555 2.04
LINK ND2 ASN C 53 C1 NAG C 300 1555 1555 1.71
LINK OG SER C 205 P DFP C 500 1555 1555 1.49
LINK OG SER C 205 O3P DFP C 500 1555 1555 2.05
LINK C LEU A 275 N TYS A 276 1555 1555 1.33
LINK C TYS A 276 N ASP A 277 1555 1555 1.33
LINK C TYR A 278 N TYS A 279 1555 1555 1.33
CISPEP 1 SER C 22 PRO C 23 0 0.94
SITE 1 AC1 1 ASN C 53
SITE 1 AC2 11 ALA A 165 GLY A 166 LEU A 168 ASN A 169
SITE 2 AC2 11 GLY A 190 PHE A 191 PHE A 192 GLY A 193
SITE 3 AC2 11 THR A 273 ASP A 274 HOH A 535
SITE 1 AC3 10 CYS C 28 HIS C 43 LYS C 52 CYS C 201
SITE 2 AC3 10 GLU C 202 GLY C 203 SER C 205 SER C 226
SITE 3 AC3 10 TRP C 227 HOH C 567
CRYST1 47.095 111.770 176.251 90.00 90.00 90.00 P 21 21 21 4
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 0.021234 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008947 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005674 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
