HEADER HYDROLASE 19-APR-16 5JFD
TITLE THROMBIN IN COMPLEX WITH (S)-N-(2-(AMINOMETHYL)-5-CHLOROBENZYL)-1-
TITLE 2 ((BENZYLSULFONYL)-D-ARGINYL)PYRROLIDINE-2-CARBOXAMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTHROMBIN;
COMPND 3 CHAIN: L;
COMPND 4 SYNONYM: COAGULATION FACTOR II;
COMPND 5 EC: 3.4.21.5;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: PROTHROMBIN;
COMPND 8 CHAIN: H;
COMPND 9 SYNONYM: COAGULATION FACTOR II;
COMPND 10 EC: 3.4.21.5;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: HIRUDIN VARIANT-2;
COMPND 13 CHAIN: I;
COMPND 14 ENGINEERED: YES;
COMPND 15 OTHER_DETAILS: HTTP://SHOP.BACHEM.COM/H-7425.HTML CONTAINS SULFATED
COMPND 16 TYROSINE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 TISSUE: BLOOD;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 8 ORGANISM_COMMON: HUMAN;
SOURCE 9 ORGANISM_TAXID: 9606;
SOURCE 10 TISSUE: BLOOD;
SOURCE 11 MOL_ID: 3;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: HIRUDO MEDICINALIS;
SOURCE 14 ORGANISM_COMMON: MEDICINAL LEECH;
SOURCE 15 ORGANISM_TAXID: 6421
KEYWDS COAGULATION, BLOOD CLOTTING, CONVERTION OF FIBRINOGEN TO FIBRIN,
KEYWDS 2 BLOOD CLOTTING INHIBITOR, THROMBIN INHIBITOR, PREORGANIZATION,
KEYWDS 3 GLYCOSYLATION, BLOOD, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.SANDNER,A.HEINE,G.KLEBE
REVDAT 5 10-JAN-24 5JFD 1 HETSYN
REVDAT 4 29-JUL-20 5JFD 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE
REVDAT 3 27-NOV-19 5JFD 1 JRNL
REVDAT 2 20-JUN-18 5JFD 1 REMARK
REVDAT 1 24-MAY-17 5JFD 0
JRNL AUTH A.SANDNER,T.HUFNER-WULSDORF,A.HEINE,T.STEINMETZER,G.KLEBE
JRNL TITL STRATEGIES FOR LATE-STAGE OPTIMIZATION: PROFILING
JRNL TITL 2 THERMODYNAMICS BY PREORGANIZATION AND SALT BRIDGE SHIELDING.
JRNL REF J.MED.CHEM. V. 62 9753 2019
JRNL REFN ISSN 0022-2623
JRNL PMID 31633354
JRNL DOI 10.1021/ACS.JMEDCHEM.9B01196
REMARK 2
REMARK 2 RESOLUTION. 1.46 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.10.1_2155
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.46
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.13
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 58835
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.132
REMARK 3 R VALUE (WORKING SET) : 0.130
REMARK 3 FREE R VALUE : 0.163
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2941
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 1.4823 - 1.4600 0.92 2493 131 0.2424 0.2932
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.140
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.290
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 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 2589
REMARK 3 ANGLE : 1.217 3518
REMARK 3 CHIRALITY : 0.095 366
REMARK 3 PLANARITY : 0.008 468
REMARK 3 DIHEDRAL : 21.041 1004
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: PHENIX REFINEMENT
REMARK 4
REMARK 4 5JFD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-APR-16.
REMARK 100 THE DEPOSITION ID IS D_1000220158.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-OCT-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91841
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : SAGITALLY BENDED SI111-CRYSTAL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 58841
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.460
REMARK 200 RESOLUTION RANGE LOW (A) : 43.130
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.03900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.46
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.55
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 0.47000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
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 (%): 51.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 MM SODIUM DIHYDROGEN PHOSPHATE PH
REMARK 280 7.5, 350 MM NACL, 27% PEG 8000,, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
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 34.68350
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.74500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 34.68350
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 35.74500
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: 4590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 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 CZ ARG H 75 LIES ON A SPECIAL POSITION.
REMARK 375 HOH H 416 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 -4
REMARK 465 PHE L -3
REMARK 465 GLY L -2
REMARK 465 SER L -1
REMARK 465 GLY L 0
REMARK 465 THR H 148A
REMARK 465 ALA H 148B
REMARK 465 ASN H 148C
REMARK 465 VAL H 148D
REMARK 465 GLY H 148E
REMARK 465 LYS H 148F
REMARK 465 GLU H 247
REMARK 465 GLY I 554
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 LYS L 9 NZ
REMARK 470 LYS L 14A NZ
REMARK 470 ASP L 15 CG OD1 OD2
REMARK 470 MET H 84 CE
REMARK 470 LYS H 87 CE NZ
REMARK 470 LYS H 107 NZ
REMARK 470 LYS H 110 CD CE NZ
REMARK 470 ASP H 186A CG OD1 OD2
REMARK 470 LYS H 186D CE NZ
REMARK 470 LYS H 236 CD CE NZ
REMARK 470 GLN H 239 CG CD OE1 NE2
REMARK 470 LYS H 240 CD CE NZ
REMARK 470 ASP I 555 CG OD1 OD2
REMARK 470 GLU I 558 CG CD OE1 OE2
REMARK 470 GLU I 561 CG CD OE1 OE2
REMARK 470 GLN I 565 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 ND2 ASN H 60G O5 NAG H 302 1.88
REMARK 500 O HOH L 212 O HOH L 221 2.05
REMARK 500 O HOH H 435 O HOH H 591 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 -88.95 -131.10
REMARK 500 CYS H 42 167.72 172.15
REMARK 500 TYR H 60A 84.23 -154.32
REMARK 500 ASN H 60G 81.03 -156.03
REMARK 500 HIS H 71 -62.14 -131.36
REMARK 500 ILE H 79 -62.34 -128.99
REMARK 500 GLU H 97A -66.66 -109.92
REMARK 500 SER H 195 133.44 -37.18
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 NA H 303 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS H 169 O
REMARK 620 2 THR H 172 O 81.4
REMARK 620 3 PHE H 204A O 18.1 90.2
REMARK 620 4 HOH H 477 O 70.5 81.6 55.9
REMARK 620 5 HOH H 514 O 172.7 94.1 157.9 103.3
REMARK 620 6 HOH H 559 O 83.3 164.7 75.5 94.3 101.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA H 304 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG H 221A O
REMARK 620 2 LYS H 224 O 93.6
REMARK 620 3 HOH H 469 O 106.7 158.3
REMARK 620 4 HOH H 496 O 159.9 69.3 89.3
REMARK 620 5 HOH H 525 O 87.6 89.1 84.3 81.9
REMARK 620 6 HOH H 587 O 98.1 82.6 101.4 90.2 170.2
REMARK 620 N 1 2 3 4 5
REMARK 630
REMARK 630 MOLECULE TYPE: PEPTIDE-LIKE THROMBIN INHIBITOR
REMARK 630 MOLECULE NAME: (2S)-N-[[2-(AMINOMETHYL)-5-CHLORO-PHENYL]METHYL]-1-
REMARK 630 [(2R)-5-CARBAMIMIDAMIDO-2-(PHENYLMETHYLSULFONYLAMINO)PENTANOYL]
REMARK 630 PYRROLIDINE-2-CARBOXAMIDE
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 2TS H 301
REMARK 630 SOURCE: NULL
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP: PMS DAR PRO 00T
REMARK 630 DETAILS: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3EQ0 RELATED DB: PDB
REMARK 900 GUANIDINE SIDECHAIN OF LIGAND HAD TWO DIFFERENT CONFORMATIONS.
REMARK 900 DESITY NOT CLEAR.
DBREF 5JFD L -4 17 UNP P00734 THRB_HUMAN 328 363
DBREF 5JFD H 16 247 UNP P00734 THRB_HUMAN 364 622
DBREF 5JFD I 554 565 UNP P09945 HIRV2_HIRME 61 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 12 GLY ASP PHE GLU GLU ILE PRO GLU GLU TYS LEU GLN
MODRES 5JFD TYS I 563 TYR MODIFIED RESIDUE
HET TYS I 563 24
HET 2TS H 301 39
HET NAG H 302 14
HET NA H 303 1
HET NA H 304 1
HET GOL H 305 6
HET DMS H 306 4
HET GOL H 307 6
HETNAM TYS O-SULFO-L-TYROSINE
HETNAM 2TS (2S)-N-[[2-(AMINOMETHYL)-5-CHLORO-PHENYL]METHYL]-1-
HETNAM 2 2TS [(2R)-5-CARBAMIMIDAMIDO-2-(PHENYLMETHYLSULFONYLAMINO)
HETNAM 3 2TS PENTANOYL]PYRROLIDINE-2-CARBOXAMIDE
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM NA SODIUM ION
HETNAM GOL GLYCEROL
HETNAM DMS DIMETHYL SULFOXIDE
HETSYN 2TS (S)-1-((R)-5-GUANIDINO-2-PHENYLMETHANESULFONYLAMINO-
HETSYN 2 2TS PENTANOYL)-PYRROLIDINE-2-CARBOXYLIC ACID 2AMINOMETHYL-
HETSYN 3 2TS 5-CHLORO-BENZYLAMIDE
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 2TS C26 H36 CL N7 O4 S
FORMUL 5 NAG C8 H15 N O6
FORMUL 6 NA 2(NA 1+)
FORMUL 8 GOL 2(C3 H8 O3)
FORMUL 9 DMS C2 H6 O S
FORMUL 11 HOH *264(H2 O)
HELIX 1 AA1 PHE L 7 SER L 11 5 5
HELIX 2 AA2 THR L 14B TYR L 14J 1 9
HELIX 3 AA3 ALA H 55 CYS H 58 5 4
HELIX 4 AA4 PRO H 60B ASP H 60E 5 4
HELIX 5 AA5 THR H 60I ASN H 62 5 3
HELIX 6 AA6 ASP H 125 LEU H 130 1 9
HELIX 7 AA7 GLU H 164 SER H 171 1 8
HELIX 8 AA8 LYS H 185 GLY H 186C 5 5
HELIX 9 AA9 LEU H 234 GLY H 246 1 13
HELIX 10 AB1 PRO I 560 GLN I 565 5 6
SHEET 1 AA1 7 SER H 20 ASP H 21 0
SHEET 2 AA1 7 GLN H 156 PRO H 161 -1 O VAL H 157 N SER H 20
SHEET 3 AA1 7 LYS H 135 GLY H 140 -1 N VAL H 138 O VAL H 158
SHEET 4 AA1 7 PRO H 198 LYS H 202 -1 O VAL H 200 N ARG H 137
SHEET 5 AA1 7 TRP H 207 TRP H 215 -1 O TYR H 208 N MET H 201
SHEET 6 AA1 7 GLY H 226 HIS H 230 -1 O PHE H 227 N TRP H 215
SHEET 7 AA1 7 MET H 180 ALA H 183 -1 N PHE H 181 O TYR H 228
SHEET 1 AA2 7 LYS H 81 SER H 83 0
SHEET 2 AA2 7 LEU H 64 ILE H 68 -1 N ILE H 68 O LYS H 81
SHEET 3 AA2 7 GLN H 30 ARG H 35 -1 N PHE H 34 O LEU H 65
SHEET 4 AA2 7 GLU H 39 LEU H 46 -1 O LEU H 41 N LEU H 33
SHEET 5 AA2 7 TRP H 51 THR H 54 -1 O LEU H 53 N SER H 45
SHEET 6 AA2 7 ALA H 104 LEU H 108 -1 O ALA H 104 N THR H 54
SHEET 7 AA2 7 LEU H 85 ILE H 90 -1 N TYR H 89 O LEU H 105
SHEET 1 AA3 2 LEU H 60 TYR H 60A 0
SHEET 2 AA3 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 2.04
SSBOND 2 CYS H 42 CYS H 58 1555 1555 2.04
SSBOND 3 CYS H 168 CYS H 182 1555 1555 2.05
SSBOND 4 CYS H 191 CYS H 220 1555 1555 2.05
LINK ND2 ASN H 60G C1 NAG H 302 1555 1555 1.37
LINK C GLU I 562 N TYS I 563 1555 1555 1.33
LINK C TYS I 563 N LEU I 564 1555 1555 1.33
LINK O LYS H 169 NA NA H 303 1555 1555 2.38
LINK O THR H 172 NA NA H 303 1555 1555 2.35
LINK O PHE H 204A NA NA H 303 1555 4556 2.32
LINK O ARG H 221A NA NA H 304 1555 1555 2.34
LINK O LYS H 224 NA NA H 304 1555 1555 2.45
LINK NA NA H 303 O HOH H 477 1555 1555 2.58
LINK NA NA H 303 O HOH H 514 1555 4546 2.41
LINK NA NA H 303 O HOH H 559 1555 1555 2.38
LINK NA NA H 304 O HOH H 469 1555 1555 2.34
LINK NA NA H 304 O HOH H 496 1555 1555 2.47
LINK NA NA H 304 O HOH H 525 1555 1555 2.63
LINK NA NA H 304 O HOH H 587 1555 1555 2.33
CISPEP 1 SER H 36A PRO H 37 0 -2.01
CRYST1 69.367 71.490 72.135 90.00 99.79 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 0.014416 0.000000 0.002488 0.00000
SCALE2 0.000000 0.013988 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014068 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
