HEADER HORMONE 06-JUL-07 2QJ2
TITLE A MECHANISTIC BASIS FOR CONVERTING A RECEPTOR TYROSINE KINASE AGONIST
TITLE 2 TO AN ANTAGONIST
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEPATOCYTE GROWTH FACTOR;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 28-209;
COMPND 5 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: HGF, HPTA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ORIGAMI(DE);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-DUET1
KEYWDS HGF/SF, HORMONE/GROWTH FACTOR, HORMONE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.D.TOLBERT,J.DAUGHERTY,C.-F.GAO,Q.XE,C.MIRANTI,E.GHERARDI,G.VANDE
AUTHOR 2 WOUDE,H.E.XU
REVDAT 3 30-AUG-23 2QJ2 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2QJ2 1 VERSN
REVDAT 1 18-SEP-07 2QJ2 0
JRNL AUTH W.D.TOLBERT,J.DAUGHERTY,C.GAO,Q.XIE,C.MIRANTI,E.GHERARDI,
JRNL AUTH 2 G.VANDE WOUDE,H.E.XU
JRNL TITL A MECHANISTIC BASIS FOR CONVERTING A RECEPTOR TYROSINE
JRNL TITL 2 KINASE AGONIST TO AN ANTAGONIST
JRNL REF PROC.NATL.ACAD.SCI.USA V. 104 14592 2007
JRNL REFN ISSN 0027-8424
JRNL PMID 17804794
JRNL DOI 10.1073/PNAS.0704290104
REMARK 2
REMARK 2 RESOLUTION. 1.81 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.81
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 22.29
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 256166.760
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 82.4
REMARK 3 NUMBER OF REFLECTIONS : 26701
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) : 0.201
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2647
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
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) : 1.81
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.91
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 28.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1429
REMARK 3 BIN R VALUE (WORKING SET) : 0.3180
REMARK 3 BIN FREE R VALUE : 0.3230
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 146
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.027
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2815
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 330
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.93000
REMARK 3 B22 (A**2) : -1.52000
REMARK 3 B33 (A**2) : -1.41000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 2.41000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.22
REMARK 3 ESD FROM SIGMAA (A) : 0.24
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) : 0.27
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.21
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.850
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.460 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.320 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.040 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.070 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.45
REMARK 3 BSOL : 70.89
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER_REP.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINED TO A MAXIMUM LIKELIHOOD TARGET
REMARK 3 USING AMPLITUDES.
REMARK 4
REMARK 4 2QJ2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JUL-07.
REMARK 100 THE DEPOSITION ID IS D_1000043660.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-DEC-04
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 5ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.99998
REMARK 200 MONOCHROMATOR : SI 1 1 1
REMARK 200 OPTICS : MONOCHROMATOR SI 1 1 1
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 : 28061
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 22.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 86.8
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : 0.08000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 31.3
REMARK 200 DATA REDUNDANCY IN SHELL : 1.70
REMARK 200 R MERGE FOR SHELL (I) : 0.37000
REMARK 200 R SYM FOR SHELL (I) : 0.37000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1NK1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM AMMONIUM SULFATE, 26-29% PEG
REMARK 280 4000 (W/W), 100 MM TRIS-HCL PH 8.0, 0.5 MM BETA-OCTYL GLUCOSIDE,
REMARK 280 AND 5% ETHYLENE GLYCOL , VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 25.90250
REMARK 290 SMTRY3 2 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 BIOLOGICAL ASSEMBLY IS THE DIMER IN THE ASYMMETRIC UNIT.
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3220 ANGSTROM**2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 GLY A 26
REMARK 465 SER A 27
REMARK 465 TYR A 28
REMARK 465 ALA A 29
REMARK 465 GLU A 30
REMARK 465 GLY A 31
REMARK 465 GLN A 32
REMARK 465 ARG A 33
REMARK 465 LYS A 34
REMARK 465 ARG A 35
REMARK 465 GLY B 1026
REMARK 465 SER B 1027
REMARK 465 TYR B 1028
REMARK 465 ALA B 1029
REMARK 465 GLU B 1030
REMARK 465 GLY B 1031
REMARK 465 GLN B 1032
REMARK 465 ARG B 1033
REMARK 465 LYS B 1034
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 CYS A 96 CA - CB - SG ANGL. DEV. = 6.8 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 GLU A 174 -132.44 45.84
REMARK 500 GLU A 184 -68.92 -16.27
REMARK 500 ASP A 202 65.17 -108.54
REMARK 500 ILE B1053 -71.26 -72.64
REMARK 500 ASP B1054 96.34 -33.23
REMARK 500 PRO B1081 34.87 -72.94
REMARK 500 LYS B1094 64.88 39.65
REMARK 500 GLU B1174 -126.29 41.81
REMARK 500 ARG B1181 17.38 54.53
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 3001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 3002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 3003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 3004
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1NK1 RELATED DB: PDB
REMARK 900 NK1 STRUCTURE
REMARK 900 RELATED ID: 1GP9 RELATED DB: PDB
REMARK 900 NK1 STRUCTURE
REMARK 900 RELATED ID: 1GMN RELATED DB: PDB
REMARK 900 NK1-HEPARIN COMPLEXES
REMARK 900 RELATED ID: 1GMO RELATED DB: PDB
REMARK 900 NK1-HEPARIN COMPLEXES
REMARK 900 RELATED ID: 1BHT RELATED DB: PDB
REMARK 900 NK1 STRUCTURE
REMARK 900 RELATED ID: 2HGF RELATED DB: PDB
REMARK 900 NMR N-TERMINAL DOMAIN STRUCTURE
REMARK 900 RELATED ID: 2QJ4 RELATED DB: PDB
DBREF 2QJ2 A 28 209 UNP P14210 HGF_HUMAN 28 209
DBREF 2QJ2 B 1028 1209 UNP P14210 HGF_HUMAN 28 209
SEQADV 2QJ2 GLY A 26 UNP P14210 EXPRESSION TAG
SEQADV 2QJ2 SER A 27 UNP P14210 EXPRESSION TAG
SEQADV 2QJ2 GLY B 1026 UNP P14210 EXPRESSION TAG
SEQADV 2QJ2 SER B 1027 UNP P14210 EXPRESSION TAG
SEQRES 1 A 184 GLY SER TYR ALA GLU GLY GLN ARG LYS ARG ARG ASN THR
SEQRES 2 A 184 ILE HIS GLU PHE LYS LYS SER ALA LYS THR THR LEU ILE
SEQRES 3 A 184 LYS ILE ASP PRO ALA LEU LYS ILE LYS THR LYS LYS VAL
SEQRES 4 A 184 ASN THR ALA ASP GLN CYS ALA ASN ARG CYS THR ARG ASN
SEQRES 5 A 184 LYS GLY LEU PRO PHE THR CYS LYS ALA PHE VAL PHE ASP
SEQRES 6 A 184 LYS ALA ARG LYS GLN CYS LEU TRP PHE PRO PHE ASN SER
SEQRES 7 A 184 MET SER SER GLY VAL LYS LYS GLU PHE GLY HIS GLU PHE
SEQRES 8 A 184 ASP LEU TYR GLU ASN LYS ASP TYR ILE ARG ASN CYS ILE
SEQRES 9 A 184 ILE GLY LYS GLY ARG SER TYR LYS GLY THR VAL SER ILE
SEQRES 10 A 184 THR LYS SER GLY ILE LYS CYS GLN PRO TRP SER SER MET
SEQRES 11 A 184 ILE PRO HIS GLU HIS SER PHE LEU PRO SER SER TYR ARG
SEQRES 12 A 184 GLY LYS ASP LEU GLN GLU ASN TYR CYS ARG ASN PRO ARG
SEQRES 13 A 184 GLY GLU GLU GLY GLY PRO TRP CYS PHE THR SER ASN PRO
SEQRES 14 A 184 GLU VAL ARG TYR GLU VAL CYS ASP ILE PRO GLN CYS SER
SEQRES 15 A 184 GLU VAL
SEQRES 1 B 184 GLY SER TYR ALA GLU GLY GLN ARG LYS ARG ARG ASN THR
SEQRES 2 B 184 ILE HIS GLU PHE LYS LYS SER ALA LYS THR THR LEU ILE
SEQRES 3 B 184 LYS ILE ASP PRO ALA LEU LYS ILE LYS THR LYS LYS VAL
SEQRES 4 B 184 ASN THR ALA ASP GLN CYS ALA ASN ARG CYS THR ARG ASN
SEQRES 5 B 184 LYS GLY LEU PRO PHE THR CYS LYS ALA PHE VAL PHE ASP
SEQRES 6 B 184 LYS ALA ARG LYS GLN CYS LEU TRP PHE PRO PHE ASN SER
SEQRES 7 B 184 MET SER SER GLY VAL LYS LYS GLU PHE GLY HIS GLU PHE
SEQRES 8 B 184 ASP LEU TYR GLU ASN LYS ASP TYR ILE ARG ASN CYS ILE
SEQRES 9 B 184 ILE GLY LYS GLY ARG SER TYR LYS GLY THR VAL SER ILE
SEQRES 10 B 184 THR LYS SER GLY ILE LYS CYS GLN PRO TRP SER SER MET
SEQRES 11 B 184 ILE PRO HIS GLU HIS SER PHE LEU PRO SER SER TYR ARG
SEQRES 12 B 184 GLY LYS ASP LEU GLN GLU ASN TYR CYS ARG ASN PRO ARG
SEQRES 13 B 184 GLY GLU GLU GLY GLY PRO TRP CYS PHE THR SER ASN PRO
SEQRES 14 B 184 GLU VAL ARG TYR GLU VAL CYS ASP ILE PRO GLN CYS SER
SEQRES 15 B 184 GLU VAL
HET SO4 A3001 5
HET SO4 A3002 5
HET SO4 A3004 5
HET SO4 B3003 5
HETNAM SO4 SULFATE ION
FORMUL 3 SO4 4(O4 S 2-)
FORMUL 7 HOH *330(H2 O)
HELIX 1 1 THR A 38 HIS A 40 5 3
HELIX 2 2 THR A 66 ARG A 76 1 11
HELIX 3 3 ASP A 123 ILE A 125 5 3
HELIX 4 4 LEU A 163 ARG A 168 5 6
HELIX 5 5 THR B 1038 HIS B 1040 5 3
HELIX 6 6 THR B 1066 ASN B 1077 1 12
HELIX 7 7 ASP B 1123 ILE B 1125 5 3
HELIX 8 8 ASN B 1179 GLU B 1183 5 5
SHEET 1 A 5 PHE A 42 SER A 45 0
SHEET 2 A 5 PHE A 116 ASN A 121 -1 O LEU A 118 N SER A 45
SHEET 3 A 5 ALA A 86 ASP A 90 -1 N PHE A 87 O TYR A 119
SHEET 4 A 5 GLN A 95 PHE A 99 -1 O PHE A 99 N ALA A 86
SHEET 5 A 5 LYS A 60 LYS A 63 -1 N LYS A 60 O TRP A 98
SHEET 1 B 2 THR A 48 LYS A 52 0
SHEET 2 B 2 VAL A 108 PHE A 112 -1 O LYS A 109 N ILE A 51
SHEET 1 C 2 TRP A 188 PHE A 190 0
SHEET 2 C 2 TYR A 198 VAL A 200 -1 O GLU A 199 N CYS A 189
SHEET 1 D 5 PHE B1042 LYS B1052 0
SHEET 2 D 5 VAL B1108 ASN B1121 -1 O LEU B1118 N SER B1045
SHEET 3 D 5 ALA B1086 ASP B1090 -1 N PHE B1087 O TYR B1119
SHEET 4 D 5 GLN B1095 PHE B1099 -1 O PHE B1099 N ALA B1086
SHEET 5 D 5 LYS B1060 LYS B1063 -1 N LYS B1060 O TRP B1098
SHEET 1 E 2 TRP B1188 PHE B1190 0
SHEET 2 E 2 TYR B1198 VAL B1200 -1 O GLU B1199 N CYS B1189
SSBOND 1 CYS A 70 CYS A 96 1555 1555 2.02
SSBOND 2 CYS A 74 CYS A 84 1555 1555 2.06
SSBOND 3 CYS A 128 CYS A 206 1555 1555 2.04
SSBOND 4 CYS A 149 CYS A 189 1555 1555 2.03
SSBOND 5 CYS A 177 CYS A 201 1555 1555 2.02
SSBOND 6 CYS B 1070 CYS B 1096 1555 1555 2.03
SSBOND 7 CYS B 1074 CYS B 1084 1555 1555 2.05
SSBOND 8 CYS B 1128 CYS B 1206 1555 1555 2.04
SSBOND 9 CYS B 1149 CYS B 1189 1555 1555 2.04
SSBOND 10 CYS B 1177 CYS B 1201 1555 1555 2.02
CISPEP 1 ILE A 156 PRO A 157 0 0.28
CISPEP 2 ILE B 1156 PRO B 1157 0 0.19
SITE 1 AC1 5 LYS A 60 LYS A 62 ARG A 73 TYR A 167
SITE 2 AC1 5 ARG A 181
SITE 1 AC2 8 ARG A 126 ILE A 130 GLY A 131 GLY A 133
SITE 2 AC2 8 ARG A 134 SER A 135 TYR A 136 HOH A2217
SITE 1 AC3 7 HIS B1160 SER B1161 PHE B1162 ARG B1168
SITE 2 AC3 7 ARG B1197 HOH B2228 HOH B2303
SITE 1 AC4 5 ARG A 168 GLY A 169 ASP A 171 HOH A2027
SITE 2 AC4 5 HOH A2278
CRYST1 49.401 51.805 73.167 90.00 107.87 90.00 P 1 21 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 0.020243 0.000000 0.006527 0.00000
SCALE2 0.000000 0.019303 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014360 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
