HEADER HYDROLASE/HYDROLASE INHIBITOR 12-JUL-11 3SV2
TITLE HUMAN THROMBIN IN COMPLEX WITH UBTHR105
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THROMBIN LIGHT CHAIN;
COMPND 3 CHAIN: L;
COMPND 4 EC: 3.4.21.5;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: THROMBIN HEAVY CHAIN;
COMPND 7 CHAIN: H;
COMPND 8 EC: 3.4.21.5;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: HIRUDIN VARIANT-2;
COMPND 11 CHAIN: I;
COMPND 12 FRAGMENT: RESIDUES IN UNP 60-72;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 7 ORGANISM_COMMON: HUMAN;
SOURCE 8 ORGANISM_TAXID: 9606;
SOURCE 9 MOL_ID: 3;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 ORGANISM_SCIENTIFIC: HIRUDO MEDICINALIS;
SOURCE 12 ORGANISM_COMMON: MEDICINAL LEECH;
SOURCE 13 ORGANISM_TAXID: 6421;
SOURCE 14 OTHER_DETAILS: SYNTHETIC FRAGMENT OF HIRUDIN FROM HIRUDO MEDICINALIS
KEYWDS SERINE PROTEASE, KRINGLE, HYDROLASE, BLOOD COAGULATION, BLOOD
KEYWDS 2 CLOTTING, CONVERTION OF FIBRINOGEN TO FIBRIN, CLEAVAGE ON PAIRS OF
KEYWDS 3 BASIC RESIDUES, HIRUDIN, GLYCOSYLATION, BLOOD, HYDROLASE-HYDROLASE
KEYWDS 4 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.BIELA,A.HEINE,G.KLEBE
REVDAT 4 06-DEC-23 3SV2 1 REMARK
REVDAT 3 01-NOV-23 3SV2 1 HETSYN
REVDAT 2 29-JUL-20 3SV2 1 COMPND REMARK HETNAM LINK
REVDAT 2 2 1 SITE
REVDAT 1 20-JUN-12 3SV2 0
JRNL AUTH A.BIELA,M.KHAYAT,H.TAN,J.KONG,A.HEINE,D.HANGAUER,G.KLEBE
JRNL TITL IMPACT OF LIGAND AND PROTEIN DESOLVATION ON LIGAND BINDING
JRNL TITL 2 TO THE S1 POCKET OF THROMBIN
JRNL REF J.MOL.BIOL. V. 418 350 2012
JRNL REFN ISSN 0022-2836
JRNL PMID 22366545
JRNL DOI 10.1016/J.JMB.2012.01.054
REMARK 2
REMARK 2 RESOLUTION. 1.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7_650)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.68
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.4
REMARK 3 NUMBER OF REFLECTIONS : 80045
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.142
REMARK 3 R VALUE (WORKING SET) : 0.140
REMARK 3 FREE R VALUE : 0.165
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 4025
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 35.6979 - 3.9923 0.98 2808 169 0.1646 0.1850
REMARK 3 2 3.9923 - 3.1694 0.97 2718 149 0.1423 0.1592
REMARK 3 3 3.1694 - 2.7689 0.97 2716 153 0.1462 0.1491
REMARK 3 4 2.7689 - 2.5158 0.96 2730 134 0.1392 0.1758
REMARK 3 5 2.5158 - 2.3356 0.96 2713 142 0.1288 0.1604
REMARK 3 6 2.3356 - 2.1979 0.95 2687 156 0.1254 0.1516
REMARK 3 7 2.1979 - 2.0878 0.96 2682 141 0.1227 0.1604
REMARK 3 8 2.0878 - 1.9969 0.96 2683 137 0.1189 0.1542
REMARK 3 9 1.9969 - 1.9201 0.95 2637 141 0.1133 0.1199
REMARK 3 10 1.9201 - 1.8538 0.95 2676 137 0.1111 0.1343
REMARK 3 11 1.8538 - 1.7959 0.95 2674 141 0.1040 0.1406
REMARK 3 12 1.7959 - 1.7445 0.95 2684 135 0.0999 0.1324
REMARK 3 13 1.7445 - 1.6986 0.94 2631 144 0.1015 0.1434
REMARK 3 14 1.6986 - 1.6572 0.94 2621 126 0.1035 0.1423
REMARK 3 15 1.6572 - 1.6195 0.94 2638 139 0.1042 0.1368
REMARK 3 16 1.6195 - 1.5850 0.94 2628 135 0.1058 0.1497
REMARK 3 17 1.5850 - 1.5533 0.91 2547 146 0.1190 0.1351
REMARK 3 18 1.5533 - 1.5240 0.92 2566 140 0.1180 0.1680
REMARK 3 19 1.5240 - 1.4968 0.92 2592 134 0.1326 0.1473
REMARK 3 20 1.4968 - 1.4714 0.93 2592 141 0.1440 0.1636
REMARK 3 21 1.4714 - 1.4477 0.92 2596 137 0.1502 0.1710
REMARK 3 22 1.4477 - 1.4254 0.92 2547 135 0.1775 0.2097
REMARK 3 23 1.4254 - 1.4044 0.92 2622 136 0.1954 0.2314
REMARK 3 24 1.4044 - 1.3847 0.92 2591 113 0.2091 0.2822
REMARK 3 25 1.3847 - 1.3659 0.92 2599 135 0.2251 0.2620
REMARK 3 26 1.3659 - 1.3482 0.91 2539 133 0.2416 0.2554
REMARK 3 27 1.3482 - 1.3314 0.87 2432 147 0.2693 0.2774
REMARK 3 28 1.3314 - 1.3153 0.90 2483 119 0.2824 0.3341
REMARK 3 29 1.3153 - 1.3000 0.85 2388 130 0.3118 0.3268
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.89
REMARK 3 K_SOL : 0.40
REMARK 3 B_SOL : 35.30
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 14.130
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.59
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.87
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.02460
REMARK 3 B22 (A**2) : 0.91570
REMARK 3 B33 (A**2) : -0.94030
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.00190
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.012 2536
REMARK 3 ANGLE : 1.307 3432
REMARK 3 CHIRALITY : 0.080 356
REMARK 3 PLANARITY : 0.007 435
REMARK 3 DIHEDRAL : 16.468 1006
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3SV2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-JUL-11.
REMARK 100 THE DEPOSITION ID IS D_1000066687.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-JUN-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9686
REMARK 200 MONOCHROMATOR : SILICON MONOCHROMATOR
REMARK 200 OPTICS : COLLIMATING MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 85743
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.6
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.02700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.49200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1H8D
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG8000, 20MM SODIUM PHOSPHATE,
REMARK 280 175MM SODIUM CHLORIDE, PH 7.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 34.99400
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.68450
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 34.99400
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 35.68450
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4640 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, I
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH H1115 LIES ON A SPECIAL POSITION.
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 L 1H
REMARK 465 PHE L 1G
REMARK 465 GLY L 1F
REMARK 465 SER L 1E
REMARK 465 GLY L 1D
REMARK 465 ASP L 14L
REMARK 465 GLY L 14M
REMARK 465 ARG L 15
REMARK 465 TRP H 148
REMARK 465 THR H 149
REMARK 465 ALA H 149A
REMARK 465 ASN H 149B
REMARK 465 VAL H 149C
REMARK 465 GLY H 149D
REMARK 465 LYS H 149E
REMARK 465 GLU H 247
REMARK 465 ASN I 53
REMARK 465 GLY I 54
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 GLU L 1C CG CD OE1 OE2
REMARK 470 SER H 36A OG
REMARK 470 ASP H 186A CG OD1 OD2
REMARK 470 LYS H 236 CG CD CE NZ
REMARK 470 GLU I 58 CG CD OE1 OE2
REMARK 470 GLU I 61 CG CD OE1 OE2
REMARK 470 GLN I 65 CG CD OE1 NE2
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 O HOH H 1059 O HOH H 1231 2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PHE L 7 -88.59 -130.56
REMARK 500 TYR H 60A 86.22 -154.04
REMARK 500 ASN H 60G 83.53 -155.94
REMARK 500 HIS H 71 -63.18 -131.94
REMARK 500 ILE H 79 -62.07 -127.05
REMARK 500 GLU H 97A -70.80 -116.93
REMARK 500
REMARK 500 REMARK: NULL
REMARK 630
REMARK 630 MOLECULE TYPE: PEPTIDE-LIKE THROMBIN INHIBITOR
REMARK 630 MOLECULE NAME: D-PHENYLALANYL-N-(PYRIDIN-4-YLMETHYL)-L-PROLINAMIDE
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 630 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 630
REMARK 630 M RES C SSSEQI
REMARK 630 P05 H 1
REMARK 630 SOURCE: NULL
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP: DPN PRO NNW
REMARK 630 DETAILS: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3P17 RELATED DB: PDB
REMARK 900 RELATED ID: 3QTO RELATED DB: PDB
REMARK 900 RELATED ID: 3QTV RELATED DB: PDB
REMARK 900 RELATED ID: 3QWC RELATED DB: PDB
REMARK 900 RELATED ID: 3QX5 RELATED DB: PDB
REMARK 900 RELATED ID: 3SHA RELATED DB: PDB
DBREF 3SV2 L 1H 15 UNP P00734 THRB_HUMAN 328 363
DBREF 3SV2 H 16 247 UNP P00734 THRB_HUMAN 364 622
DBREF 3SV2 I 53 65 UNP P09945 HIRV2_HIRME 60 72
SEQRES 1 L 36 THR PHE GLY SER GLY GLU ALA ASP CYS GLY LEU ARG PRO
SEQRES 2 L 36 LEU PHE GLU LYS LYS SER LEU GLU ASP LYS THR GLU ARG
SEQRES 3 L 36 GLU LEU LEU GLU SER TYR ILE ASP GLY ARG
SEQRES 1 H 259 ILE VAL GLU GLY SER ASP ALA GLU ILE GLY MET SER PRO
SEQRES 2 H 259 TRP GLN VAL MET LEU PHE ARG LYS SER PRO GLN GLU LEU
SEQRES 3 H 259 LEU CYS GLY ALA SER LEU ILE SER ASP ARG TRP VAL LEU
SEQRES 4 H 259 THR ALA ALA HIS CYS LEU LEU TYR PRO PRO TRP ASP LYS
SEQRES 5 H 259 ASN PHE THR GLU ASN ASP LEU LEU VAL ARG ILE GLY LYS
SEQRES 6 H 259 HIS SER ARG THR ARG TYR GLU ARG ASN ILE GLU LYS ILE
SEQRES 7 H 259 SER MET LEU GLU LYS ILE TYR ILE HIS PRO ARG TYR ASN
SEQRES 8 H 259 TRP ARG GLU ASN LEU ASP ARG ASP ILE ALA LEU MET LYS
SEQRES 9 H 259 LEU LYS LYS PRO VAL ALA PHE SER ASP TYR ILE HIS PRO
SEQRES 10 H 259 VAL CYS LEU PRO ASP ARG GLU THR ALA ALA SER LEU LEU
SEQRES 11 H 259 GLN ALA GLY TYR LYS GLY ARG VAL THR GLY TRP GLY ASN
SEQRES 12 H 259 LEU LYS GLU THR TRP THR ALA ASN VAL GLY LYS GLY GLN
SEQRES 13 H 259 PRO SER VAL LEU GLN VAL VAL ASN LEU PRO ILE VAL GLU
SEQRES 14 H 259 ARG PRO VAL CYS LYS ASP SER THR ARG ILE ARG ILE THR
SEQRES 15 H 259 ASP ASN MET PHE CYS ALA GLY TYR LYS PRO ASP GLU GLY
SEQRES 16 H 259 LYS ARG GLY ASP ALA CYS GLU GLY ASP SER GLY GLY PRO
SEQRES 17 H 259 PHE VAL MET LYS SER PRO PHE ASN ASN ARG TRP TYR GLN
SEQRES 18 H 259 MET GLY ILE VAL SER TRP GLY GLU GLY CYS ASP ARG ASP
SEQRES 19 H 259 GLY LYS TYR GLY PHE TYR THR HIS VAL PHE ARG LEU LYS
SEQRES 20 H 259 LYS TRP ILE GLN LYS VAL ILE ASP GLN PHE GLY GLU
SEQRES 1 I 13 ASN GLY ASP PHE GLU GLU ILE PRO GLU GLU TYS LEU GLN
MODRES 3SV2 ASN H 60G ASN GLYCOSYLATION SITE
MODRES 3SV2 TYS I 63 TYR O-SULFO-L-TYROSINE
HET TYS I 63 16
HET NAG H 260G 14
HET P05 H 1 26
HET PO4 H 2 5
HET GOL H 3 6
HET GOL H 4 6
HET GOL H 5 6
HET NA H 6 1
HET NA H 7 1
HETNAM TYS O-SULFO-L-TYROSINE
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM P05 D-PHENYLALANYL-N-(PYRIDIN-4-YLMETHYL)-L-PROLINAMIDE
HETNAM PO4 PHOSPHATE ION
HETNAM GOL GLYCEROL
HETNAM NA SODIUM 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 GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 TYS C9 H11 N O6 S
FORMUL 4 NAG C8 H15 N O6
FORMUL 5 P05 C20 H24 N4 O2
FORMUL 6 PO4 O4 P 3-
FORMUL 7 GOL 3(C3 H8 O3)
FORMUL 10 NA 2(NA 1+)
FORMUL 12 HOH *327(H2 O)
HELIX 1 1 PHE L 7 SER L 11 5 5
HELIX 2 2 THR L 14B TYR L 14J 1 9
HELIX 3 3 ALA H 55 CYS H 58 5 4
HELIX 4 4 PRO H 60B ASP H 60E 5 4
HELIX 5 5 THR H 60I ASN H 62 5 3
HELIX 6 6 ASP H 125 LEU H 130 1 9
HELIX 7 7 GLU H 164 SER H 171 1 8
HELIX 8 8 LYS H 185 GLY H 186C 5 5
HELIX 9 9 LEU H 234 GLY H 246 1 13
HELIX 10 10 PRO I 60 LEU I 64 5 5
SHEET 1 A 7 SER H 20 ASP H 21 0
SHEET 2 A 7 GLN H 156 PRO H 161 -1 O VAL H 157 N SER H 20
SHEET 3 A 7 LYS H 135 GLY H 140 -1 N VAL H 138 O VAL H 158
SHEET 4 A 7 PRO H 198 LYS H 202 -1 O VAL H 200 N ARG H 137
SHEET 5 A 7 TRP H 207 TRP H 215 -1 O TYR H 208 N MET H 201
SHEET 6 A 7 GLY H 226 HIS H 230 -1 O PHE H 227 N TRP H 215
SHEET 7 A 7 MET H 180 ALA H 183 -1 N PHE H 181 O TYR H 228
SHEET 1 B 7 GLN H 30 ARG H 35 0
SHEET 2 B 7 GLU H 39 LEU H 46 -1 O LEU H 41 N LEU H 33
SHEET 3 B 7 TRP H 51 THR H 54 -1 O LEU H 53 N SER H 45
SHEET 4 B 7 ALA H 104 LEU H 108 -1 O ALA H 104 N THR H 54
SHEET 5 B 7 LYS H 81 ILE H 90 -1 N GLU H 86 O LYS H 107
SHEET 6 B 7 LEU H 64 ILE H 68 -1 N ILE H 68 O LYS H 81
SHEET 7 B 7 GLN H 30 ARG H 35 -1 N PHE H 34 O LEU H 65
SHEET 1 C 2 LEU H 60 TYR H 60A 0
SHEET 2 C 2 LYS H 60F ASN H 60G-1 O LYS H 60F N TYR H 60A
SSBOND 1 CYS L 1 CYS H 122 1555 1555 2.05
SSBOND 2 CYS H 42 CYS H 58 1555 1555 2.05
SSBOND 3 CYS H 168 CYS H 182 1555 1555 2.05
SSBOND 4 CYS H 191 CYS H 220 1555 1555 2.07
LINK ND2 ASN H 60G C1 NAG H 260G 1555 1555 1.42
LINK C GLU I 62 N TYS I 63 1555 1555 1.33
LINK C TYS I 63 N LEU I 64 1555 1555 1.33
CISPEP 1 SER H 36A PRO H 37 0 -4.99
CRYST1 69.988 71.369 72.199 90.00 100.29 90.00 C 1 2 1 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 0.014288 0.000000 0.002594 0.00000
SCALE2 0.000000 0.014012 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014077 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
