HEADER BLOOD CLOTTING/HYDROLASE INHIBITOR 04-JAN-08 2ZFF
TITLE EXPLORING THROMBIN S1-POCKET
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THROMBIN LIGHT CHAIN;
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: THROMBIN HEAVY CHAIN;
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-1;
COMPND 13 CHAIN: I;
COMPND 14 FRAGMENT: UNP RESIDUES 54-64;
COMPND 15 SYNONYM: LEPIRUDIN;
COMPND 16 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 TISSUE: BLOOD PLASMA;
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 PLASMA;
SOURCE 11 MOL_ID: 3;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 OTHER_DETAILS: SYNTHETIC FRAGMENT OF HIRUDIN FROM HIRUDO MEDICINALIS
KEYWDS BLOOD CLOTTING/HYDROLASE INHIBITORS, ACUTE PHASE, BLOOD COAGULATION,
KEYWDS 2 CLEAVAGE ON PAIR OF BASIC RESIDUES, DISEASE MUTATION, GAMMA-
KEYWDS 3 CARBOXYGLUTAMIC ACID, GLYCOPROTEIN, KRINGLE, PROTEASE, SECRETED,
KEYWDS 4 SERINE PROTEASE, ZYMOGEN, BLOOD CLOTTING-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR B.BAUM,A.HEINE,G.KLEBE
REVDAT 6 15-NOV-23 2ZFF 1 REMARK
REVDAT 5 01-NOV-23 2ZFF 1 REMARK LINK
REVDAT 4 11-OCT-17 2ZFF 1 REMARK
REVDAT 3 18-SEP-13 2ZFF 1 REMARK
REVDAT 2 13-JUL-11 2ZFF 1 VERSN
REVDAT 1 16-DEC-08 2ZFF 0
JRNL AUTH B.BAUM,D.HANGAUER,A.HEINE,G.KLEBE
JRNL TITL EXPLORING THROMBIN S1-POCKET
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.47 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.47
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.3
REMARK 3 CROSS-VALIDATION METHOD : FREE R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.208
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.156
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.260
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 2814
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 55657
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.199
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.149
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 2366
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 46899
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2340
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 159
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 2532.5
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 0.00
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 8
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 23114
REMARK 3 NUMBER OF RESTRAINTS : 28380
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 ANGLE DISTANCES (A) : 0.029
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.029
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.054
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.072
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.021
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.004
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.061
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.000
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: ANISOTROPIC SCALING APPLIED BY THE
REMARK 3 METHOD OF PARKIN, MOEZZI & HOPE, J.APPL.CRYST.28(1995)53-56
REMARK 3 ANISOTROPIC REFINEMENT REDUCED FREE R (NO CUTOFF)
REMARK 4
REMARK 4 2ZFF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-JAN-08.
REMARK 100 THE DEPOSITION ID IS D_1000027903.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-DEC-07
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 7.5
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) : 0.95373
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 58620
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.470
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 2.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.03600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 27.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.47
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.60
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.49900
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: AB INITIO PHASING
REMARK 200 SOFTWARE USED: SHELX
REMARK 200 STARTING MODEL: PDB ENTRY 1H8D
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PHOSPHATE BUFFER, SODIUM CHLORIDE, PEG
REMARK 280 8000, PH 7.5, VAPOR DIFFUSION, HANGING DROP, 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 35.05000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.75000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 35.05000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 35.75000
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: 3540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12730 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 HOH H3036 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 14N
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 LEU I 64
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 ARG H 75 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG L 14D NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG L 14D NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 LEU H 40 CA - CB - CG ANGL. DEV. = 14.4 DEGREES
REMARK 500 TYR H 60A CB - CG - CD1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG H 73 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG H 93 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG H 101 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 VAL H 157 CB - CA - C ANGL. DEV. = -14.3 DEGREES
REMARK 500 ARG H 165 CD - NE - CZ ANGL. DEV. = 9.0 DEGREES
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 -88.38 -131.07
REMARK 500 TYR H 60A 83.08 -154.30
REMARK 500 ASN H 60G 79.05 -158.55
REMARK 500 HIS H 71 -63.08 -131.50
REMARK 500 ILE H 79 -61.66 -126.69
REMARK 500 GLU H 97A -70.90 -119.97
REMARK 500 LYS H 186D 155.20 -49.03
REMARK 500 SER H 195 134.93 -36.53
REMARK 500
REMARK 500 REMARK: NULL
REMARK 630
REMARK 630 MOLECULE TYPE: PEPTIDE-LIKE THROMBIN INHIBITOR
REMARK 630 MOLECULE NAME: D-PHENYLALANYL-N-BENZYL-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 53U H 2001
REMARK 630 SOURCE: NULL
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP: DPN PRO ABN
REMARK 630 DETAILS: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA H 2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA H 2003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 53U H 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN I OF HIRUDIN VARIANT-1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1H8D RELATED DB: PDB
REMARK 900 RELATED ID: 1YPG RELATED DB: PDB
REMARK 900 RELATED ID: 2ZC9 RELATED DB: PDB
REMARK 900 RELATED ID: 2ZDA RELATED DB: PDB
REMARK 900 RELATED ID: 2ZDV RELATED DB: PDB
REMARK 900 RELATED ID: 2ZF0 RELATED DB: PDB
REMARK 900 RELATED ID: 2ZFP RELATED DB: PDB
DBREF 2ZFF L 1H 14N UNP P00734 THRB_HUMAN 328 363
DBREF 2ZFF H 16 247 UNP P00734 THRB_HUMAN 364 622
DBREF 2ZFF I 54 64 UNP P01050 ITH1_HIRME 54 64
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 11 GLY ASP PHE GLU GLU ILE PRO GLU GLU TYS LEU
MODRES 2ZFF TYS I 63 TYR O-SULFO-L-TYROSINE
HET TYS I 63 16
HET NA H2002 1
HET NA H2003 1
HET 53U H2001 26
HETNAM TYS O-SULFO-L-TYROSINE
HETNAM NA SODIUM ION
HETNAM 53U D-PHENYLALANYL-N-BENZYL-L-PROLINAMIDE
HETSYN 53U (2S)-1-((2R)-2-AMINO-3-PHENYL-PROPANOYL)-N-
HETSYN 2 53U (PHENYLMETHYL)PYRROLIDINE-2-CARBOXAMIDE
FORMUL 3 TYS C9 H11 N O6 S
FORMUL 4 NA 2(NA 1+)
FORMUL 6 53U C21 H25 N3 O2
FORMUL 7 HOH *159(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
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 GLU H 39 N ARG H 35
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 MET H 106 N VAL H 52
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 2.07
SSBOND 2 CYS H 42 CYS H 58 1555 1555 2.05
SSBOND 3 CYS H 168 CYS H 182 1555 1555 2.03
SSBOND 4 CYS H 191 CYS H 220 1555 1555 2.02
LINK C GLU I 62 N TYS I 63 1555 1555 1.33
CISPEP 1 SER H 36A PRO H 37 0 -6.96
SITE 1 AC1 6 ARG H 221A LYS H 224 HOH H3037 HOH H3057
SITE 2 AC1 6 HOH H3068 HOH H3143
SITE 1 AC2 6 LYS H 169 THR H 172 PHE H 204A HOH H3026
SITE 2 AC2 6 HOH H3035 HOH H3045
SITE 1 AC3 13 HIS H 57 TYR H 60A GLU H 97A ILE H 174
SITE 2 AC3 13 ALA H 190 SER H 195 VAL H 213 SER H 214
SITE 3 AC3 13 TRP H 215 GLY H 216 GLY H 219 HOH H3098
SITE 4 AC3 13 HOH H3160
SITE 1 AC4 17 PHE H 34 GLN H 38 LEU H 40 LEU H 65
SITE 2 AC4 17 ARG H 73 THR H 74 ARG H 75 TYR H 76
SITE 3 AC4 17 GLU H 80 LYS H 81 ILE H 82 GLN H 151
SITE 4 AC4 17 SER H 153 HOH H3050 HOH H3093 HOH I3130
SITE 5 AC4 17 HOH I3151
CRYST1 70.100 71.500 72.500 90.00 100.30 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 0.014259 0.000000 0.002602 0.00000
SCALE2 0.000000 0.013993 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014030 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
