HEADER BLOOD CLOTTING, HYDROLASE 09-SEP-03 1O5D
TITLE DISSECTING AND DESIGNING INHIBITOR SELECTIVITY DETERMINANTS AT THE S1
TITLE 2 SITE USING AN ARTIFICIAL ALA190 PROTEASE (ALA190 UPA)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COAGULATION FACTOR VII;
COMPND 3 CHAIN: L;
COMPND 4 FRAGMENT: LIGHT CHAIN;
COMPND 5 SYNONYM: SERUM PROTHROMBIN CONVERSION ACCELERATOR, EPTACOG ALFA;
COMPND 6 EC: 3.4.21.21;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: COAGULATION FACTOR VII;
COMPND 10 CHAIN: H;
COMPND 11 FRAGMENT: HEAVY CHAIN (CATALYTIC DOMAIN);
COMPND 12 SYNONYM: SERUM PROTHROMBIN CONVERSION ACCELERATOR, EPTACOG ALFA;
COMPND 13 EC: 3.4.21.21;
COMPND 14 ENGINEERED: YES;
COMPND 15 MOL_ID: 3;
COMPND 16 MOLECULE: TISSUE FACTOR;
COMPND 17 CHAIN: T;
COMPND 18 SYNONYM: TF, COAGULATION FACTOR III, THROMBOPLASTIN, CD142 ANTIGEN;
COMPND 19 ENGINEERED: YES;
COMPND 20 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: F7;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: 293;
SOURCE 10 EXPRESSION_SYSTEM_ORGAN: EMBRYONIC KIDNEY;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PCI-NEO(PROMEGA);
SOURCE 13 MOL_ID: 2;
SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 15 ORGANISM_COMMON: HUMAN;
SOURCE 16 ORGANISM_TAXID: 9606;
SOURCE 17 GENE: F7;
SOURCE 18 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 19 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 20 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 21 EXPRESSION_SYSTEM_CELL_LINE: 293;
SOURCE 22 EXPRESSION_SYSTEM_ORGAN: EMBRYONIC KIDNEY;
SOURCE 23 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 24 EXPRESSION_SYSTEM_PLASMID: PCI-NEO(PROMEGA);
SOURCE 25 MOL_ID: 3;
SOURCE 26 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 27 ORGANISM_COMMON: HUMAN;
SOURCE 28 ORGANISM_TAXID: 9606;
SOURCE 29 GENE: F3;
SOURCE 30 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 31 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 32 EXPRESSION_SYSTEM_STRAIN: BL21-DES3;
SOURCE 33 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 34 EXPRESSION_SYSTEM_PLASMID: PET-21A(+);
SOURCE 35 OTHER_DETAILS: ESCHERICHIA COLI
KEYWDS ALA190 UPA, S1 SITE, SELECTIVITY, CONSERVED WATER DISPLACEMENT
KEYWDS 2 HYDROGEN BOND DEFICIT, TRYPSIN, THROMBIN, HEPSIN, FACTOR VIIA, BLOOD
KEYWDS 3 CLOTTING, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.A.KATZ,C.LUONG,J.D.HO,J.R.SOMOZA,E.GJERSTAD,J.TANG,S.R.WILLIAMS,
AUTHOR 2 E.VERNER,R.L.MACKMAN,W.B.YOUNG,P.A.SPRENGELER,H.CHAN,K.MORTARA,
AUTHOR 3 J.W.JANC,M.E.MCGRATH
REVDAT 5 27-DEC-23 1O5D 1 REMARK
REVDAT 4 04-OCT-17 1O5D 1 REMARK
REVDAT 3 24-FEB-09 1O5D 1 VERSN
REVDAT 2 17-MAY-05 1O5D 1 JRNL
REVDAT 1 21-SEP-04 1O5D 0
JRNL AUTH B.A.KATZ,C.LUONG,J.D.HO,J.R.SOMOZA,E.GJERSTAD,J.TANG,
JRNL AUTH 2 S.R.WILLIAMS,E.VERNER,R.L.MACKMAN,W.B.YOUNG,P.A.SPRENGELER,
JRNL AUTH 3 H.CHAN,K.MORTARA,J.W.JANC,M.E.MCGRATH
JRNL TITL DISSECTING AND DESIGNING INHIBITOR SELECTIVITY DETERMINANTS
JRNL TITL 2 AT THE S1 SITE USING AN ARTIFICIAL ALA190 PROTEASE (ALA190
JRNL TITL 3 UPA).
JRNL REF J.MOL.BIOL. V. 344 527 2004
JRNL REFN ISSN 0022-2836
JRNL PMID 15522303
JRNL DOI 10.1016/J.JMB.2004.09.032
REMARK 2
REMARK 2 RESOLUTION. 2.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 7.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.400
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 77.3
REMARK 3 NUMBER OF REFLECTIONS : 40130
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.226
REMARK 3 FREE R VALUE : 0.262
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4073
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3910
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 588
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.019
REMARK 3 BOND ANGLES (DEGREES) : 3.900
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
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:
REMARK 3 THE GLA DOMAIN OF THE LIGHT CHAIN (RESIDUE ALA L1 THROUGH ASP L46)
REMARK 3 IS NOT VISIBLE (DISORDERED).
REMARK 3
REMARK 3 SOME OF THE SOLUBLE TISSUE FACTOR IS NOT VISIBLE (DISORDERED):
REMARK 3 GLY_T2 THROUGH ASN_T5;GLN T110 THROUGH GLU T128;
REMARK 3 TRP T158 THROUGH PHE T187; PRO T206 THROUGH MET T210.
REMARK 3
REMARK 3 MANY OF THE WATERS MAY CORRESPOND TO SPORADIC DENSITY IN THE
REMARK 3 REGIONS OF
REMARK 3 DIORDERED PROTEIN.
REMARK 3
REMARK 3 RESIDUES SIMULTANEOUSLY REFINED IN TWO OR MORE CONFORMATIONS ARE:
REMARK 3 LEU_L121, LYS_L137, VAL_H138, LYS_H188, SER_H190, SER_T42
REMARK 3
REMARK 3 DISCRETELY DISORDERED WATERS ARE:
REMARK 3 HOH_94;
REMARK 3 A_HOH_578 IS CLOSE TO B_HOH578 WHICH IS CLOSE TO
REMARK 3 A_HOH_581 WHICH IS CLOSE TO B_HOH_581.
REMARK 3 HOH_858;
REMARK 3
REMARK 3
REMARK 3 HIS_H57 IS DOUBLY PROTONATED.
REMARK 3 HIS_H91 IS MONOPROTONATED ON THE EPSILON NITROGEN
REMARK 3
REMARK 3 NO ENERGY TERMS ARE INCLUDED OG_SER_H195, AND O6' AND HN3 OF THE
REMARK 3 INHIBITOR. THESE ATOMS FORM A SHORT HYDROGEN-BONDING NETWORK.
REMARK 4
REMARK 4 1O5D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-SEP-03.
REMARK 100 THE DEPOSITION ID IS D_1000001823.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-MAR-03
REMARK 200 TEMPERATURE (KELVIN) : 113
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO 1.97.2
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50184
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : 0.05100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.14
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.28800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: QUANTA
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M CITRATE, 16-18% PEG 5K MME, PH
REMARK 280 7.2, VAPOR DIFFUSION AT 290 K
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 34.51500
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 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: 5560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, T
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 ALA L 1
REMARK 465 ASN L 2
REMARK 465 ALA L 3
REMARK 465 PHE L 4
REMARK 465 LEU L 5
REMARK 465 GLU L 6
REMARK 465 GLU L 7
REMARK 465 LEU L 8
REMARK 465 ARG L 9
REMARK 465 PRO L 10
REMARK 465 GLY L 11
REMARK 465 SER L 12
REMARK 465 LEU L 13
REMARK 465 GLU L 14
REMARK 465 ARG L 15
REMARK 465 GLU L 16
REMARK 465 CYS L 17
REMARK 465 LYS L 18
REMARK 465 GLU L 19
REMARK 465 GLU L 20
REMARK 465 GLN L 21
REMARK 465 CYS L 22
REMARK 465 SER L 23
REMARK 465 PHE L 24
REMARK 465 GLU L 25
REMARK 465 GLU L 26
REMARK 465 ALA L 27
REMARK 465 ARG L 28
REMARK 465 GLU L 29
REMARK 465 ILE L 30
REMARK 465 PHE L 31
REMARK 465 LYS L 32
REMARK 465 ASP L 33
REMARK 465 ALA L 34
REMARK 465 GLU L 35
REMARK 465 ARG L 36
REMARK 465 THR L 37
REMARK 465 LYS L 38
REMARK 465 LEU L 39
REMARK 465 PHE L 40
REMARK 465 TRP L 41
REMARK 465 ILE L 42
REMARK 465 SER L 43
REMARK 465 TYR L 44
REMARK 465 SER L 45
REMARK 465 ASP L 46
REMARK 465 LYS L 143
REMARK 465 ARG L 144
REMARK 465 ASN L 145
REMARK 465 ALA L 146
REMARK 465 SER L 147
REMARK 465 LYS L 148
REMARK 465 PRO L 149
REMARK 465 GLN L 150
REMARK 465 GLY L 151
REMARK 465 ARG L 152
REMARK 465 GLY T 2
REMARK 465 THR T 3
REMARK 465 THR T 4
REMARK 465 ASN T 5
REMARK 465 GLN T 110
REMARK 465 PRO T 111
REMARK 465 THR T 112
REMARK 465 ILE T 113
REMARK 465 GLN T 114
REMARK 465 SER T 115
REMARK 465 PHE T 116
REMARK 465 GLU T 117
REMARK 465 GLN T 118
REMARK 465 VAL T 119
REMARK 465 GLY T 120
REMARK 465 THR T 121
REMARK 465 LYS T 122
REMARK 465 VAL T 123
REMARK 465 ASN T 124
REMARK 465 VAL T 125
REMARK 465 THR T 126
REMARK 465 VAL T 127
REMARK 465 GLU T 128
REMARK 465 TRP T 158
REMARK 465 LYS T 159
REMARK 465 SER T 160
REMARK 465 SER T 161
REMARK 465 SER T 162
REMARK 465 SER T 163
REMARK 465 GLY T 164
REMARK 465 LYS T 165
REMARK 465 LYS T 166
REMARK 465 THR T 167
REMARK 465 ALA T 168
REMARK 465 LYS T 169
REMARK 465 THR T 170
REMARK 465 ASN T 171
REMARK 465 THR T 172
REMARK 465 ASN T 173
REMARK 465 GLU T 174
REMARK 465 PHE T 175
REMARK 465 LEU T 176
REMARK 465 ILE T 177
REMARK 465 ASP T 178
REMARK 465 VAL T 179
REMARK 465 ASP T 180
REMARK 465 LYS T 181
REMARK 465 GLY T 182
REMARK 465 GLU T 183
REMARK 465 ASN T 184
REMARK 465 TYR T 185
REMARK 465 CYS T 186
REMARK 465 PHE T 187
REMARK 465 PRO T 206
REMARK 465 VAL T 207
REMARK 465 GLU T 208
REMARK 465 CYS T 209
REMARK 465 MET T 210
REMARK 465 GLY T 211
REMARK 465 GLN T 212
REMARK 465 GLU T 213
REMARK 465 LYS T 214
REMARK 465 GLY T 215
REMARK 465 GLU T 216
REMARK 465 PHE T 217
REMARK 465 ARG T 218
REMARK 465 GLU T 219
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 HH22 ARG H 230 H1 HOH H 398 1.22
REMARK 500 O LEU H 144 H2 HOH H 303 1.40
REMARK 500 OG1 THR T 101 H2 HOH T 240 1.46
REMARK 500 O VAL H 21 H2 HOH H 404 1.46
REMARK 500 OG SER H 82 H1 HOH H 485 1.47
REMARK 500 OG SER L 60 H2 HOH L 215 1.50
REMARK 500 OG1 THR H 98 H2 HOH H 422 1.51
REMARK 500 O GLU H 75 H2 HOH H 279 1.51
REMARK 500 OG SER L 103 H1 HOH L 199 1.52
REMARK 500 O SER H 139 H2 HOH H 299 1.52
REMARK 500 O LYS T 28 H2 HOH T 364 1.52
REMARK 500 O THR H 99 H2 HOH H 306 1.53
REMARK 500 O ALA T 89 H1 HOH T 269 1.53
REMARK 500 OG1 THR H 206 H2 HOH H 305 1.54
REMARK 500 OG SER T 42 H2 HOH T 405 1.54
REMARK 500 O GLY L 97 H1 HOH L 227 1.54
REMARK 500 O PRO L 54 H2 HOH L 164 1.54
REMARK 500 OG SER H 185 H1 HOH H 361 1.55
REMARK 500 O PHE H 135 H1 HOH H 402 1.55
REMARK 500 OG1 THR H 127 H2 HOH H 294 1.55
REMARK 500 O GLU H 26 H2 HOH H 316 1.55
REMARK 500 OG1 THR H 49 H1 HOH H 349 1.55
REMARK 500 OG SER H 232 H2 HOH H 265 1.56
REMARK 500 O PHE H 225 H2 HOH H 296 1.56
REMARK 500 OD1 ASN L 95 H1 HOH L 188 1.56
REMARK 500 O ASN H 175 H2 HOH H 440 1.56
REMARK 500 O PRO T 29 H2 HOH T 346 1.56
REMARK 500 O GLU T 99 H2 HOH T 387 1.57
REMARK 500 O LEU H 163 H1 HOH H 363 1.57
REMARK 500 O ASP T 61 H1 HOH T 253 1.57
REMARK 500 O GLY H 69 H1 HOH H 330 1.57
REMARK 500 OE1 GLN H 143 H1 HOH H 424 1.58
REMARK 500 OG SER T 77 H1 HOH T 260 1.58
REMARK 500 O SER T 47 H2 HOH T 294 1.58
REMARK 500 O ARG H 204 H1 HOH H 391 1.59
REMARK 500 O PRO T 92 H2 HOH T 292 1.59
REMARK 500 O ILE H 16 H1 HOH H 346 1.59
REMARK 500 OG1 THR H 129C H1 HOH H 417 1.59
REMARK 500 O LEU H 169 H2 HOH H 369 1.59
REMARK 500 O VAL H 129G H1 HOH H 320 1.59
REMARK 500 OD1 ASN L 93 H1 HOH T 294 1.60
REMARK 500 O ASN T 138 H2 HOH T 287 1.60
REMARK 500 O CYS L 102 H2 HOH L 198 1.60
REMARK 500 OG SER H 195 O6' CR9 H 258 2.07
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O TYR L 118 H1 HOH T 303 2646 1.53
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 HIS H 71 NE2 HIS H 71 CD2 -0.080
REMARK 500
REMARK 500 REMARK: NULL
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 L 102 CA - CB - SG ANGL. DEV. = 8.3 DEGREES
REMARK 500 ASP L 104 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ASP L 123 CB - CG - OD2 ANGL. DEV. = -7.8 DEGREES
REMARK 500 TRP H 29 CG - CD1 - NE1 ANGL. DEV. = -8.1 DEGREES
REMARK 500 TRP H 29 CD1 - NE1 - CE2 ANGL. DEV. = 9.5 DEGREES
REMARK 500 TRP H 29 NE1 - CE2 - CZ2 ANGL. DEV. = 9.7 DEGREES
REMARK 500 TRP H 29 NE1 - CE2 - CD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 TRP H 51 CG - CD1 - NE1 ANGL. DEV. = -7.0 DEGREES
REMARK 500 TRP H 51 CD1 - NE1 - CE2 ANGL. DEV. = 8.4 DEGREES
REMARK 500 TRP H 61 CG - CD1 - NE1 ANGL. DEV. = -8.0 DEGREES
REMARK 500 TRP H 61 CD1 - NE1 - CE2 ANGL. DEV. = 9.2 DEGREES
REMARK 500 TRP H 61 NE1 - CE2 - CZ2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 TRP H 61 NE1 - CE2 - CD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 VAL H 129G N - CA - C ANGL. DEV. = -19.6 DEGREES
REMARK 500 ARG H 134 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 TRP H 141 CG - CD1 - NE1 ANGL. DEV. = -6.7 DEGREES
REMARK 500 TRP H 141 CD1 - NE1 - CE2 ANGL. DEV. = 7.9 DEGREES
REMARK 500 TRP H 141 NE1 - CE2 - CZ2 ANGL. DEV. = 8.2 DEGREES
REMARK 500 TRP H 141 NE1 - CE2 - CD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ARG H 147 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 HIS H 199 N - CA - C ANGL. DEV. = -20.9 DEGREES
REMARK 500 TRP H 207 CG - CD1 - NE1 ANGL. DEV. = -7.5 DEGREES
REMARK 500 TRP H 207 CD1 - NE1 - CE2 ANGL. DEV. = 8.7 DEGREES
REMARK 500 TRP H 207 NE1 - CE2 - CZ2 ANGL. DEV. = 9.4 DEGREES
REMARK 500 TRP H 207 NE1 - CE2 - CD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 TRP H 215 CG - CD1 - NE1 ANGL. DEV. = -7.1 DEGREES
REMARK 500 TRP H 215 CD1 - NE1 - CE2 ANGL. DEV. = 8.5 DEGREES
REMARK 500 TRP H 215 NE1 - CE2 - CZ2 ANGL. DEV. = 7.1 DEGREES
REMARK 500 TRP H 215 NE1 - CE2 - CD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 TRP H 237 CG - CD1 - NE1 ANGL. DEV. = -7.2 DEGREES
REMARK 500 TRP H 237 CD1 - NE1 - CE2 ANGL. DEV. = 8.2 DEGREES
REMARK 500 TRP H 237 NE1 - CE2 - CZ2 ANGL. DEV. = 9.1 DEGREES
REMARK 500 TRP H 237 NE1 - CE2 - CD2 ANGL. DEV. = -6.6 DEGREES
REMARK 500 ARG H 243 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG H 253 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 TRP T 14 CG - CD1 - NE1 ANGL. DEV. = -6.8 DEGREES
REMARK 500 TRP T 14 CD1 - NE1 - CE2 ANGL. DEV. = 8.1 DEGREES
REMARK 500 TRP T 14 NE1 - CE2 - CZ2 ANGL. DEV. = 8.2 DEGREES
REMARK 500 TRP T 25 CG - CD1 - NE1 ANGL. DEV. = -7.5 DEGREES
REMARK 500 TRP T 25 CD1 - NE1 - CE2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 TRP T 25 NE1 - CE2 - CZ2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 THR T 40 N - CA - C ANGL. DEV. = -17.5 DEGREES
REMARK 500 TRP T 45 CG - CD1 - NE1 ANGL. DEV. = -7.2 DEGREES
REMARK 500 TRP T 45 CD1 - NE1 - CE2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 TRP T 45 NE1 - CE2 - CZ2 ANGL. DEV. = 8.2 DEGREES
REMARK 500 ARG T 74 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 TYR T 157 N - CA - C ANGL. DEV. = -18.9 DEGREES
REMARK 500 ARG T 196 NE - CZ - NH2 ANGL. DEV. = -3.0 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 CYS L 50 -58.99 -0.94
REMARK 500 SER L 52 53.37 -106.75
REMARK 500 SER L 53 62.33 14.14
REMARK 500 ASN L 57 33.54 34.09
REMARK 500 GLN L 64 -152.24 -125.73
REMARK 500 GLN L 66 -55.31 89.31
REMARK 500 SER L 67 175.62 -59.96
REMARK 500 PRO L 74 -34.52 -33.74
REMARK 500 CYS L 81 44.11 32.93
REMARK 500 GLN L 100 -85.07 -123.93
REMARK 500 LYS L 109 156.02 -48.53
REMARK 500 TYR L 133 78.03 -114.28
REMARK 500 LEU H 41 -80.02 -111.58
REMARK 500 THR H 49 -25.93 -34.08
REMARK 500 LYS H 60A 65.14 -117.76
REMARK 500 ASN H 60D 53.87 -114.97
REMARK 500 HIS H 71 -59.51 -138.57
REMARK 500 ASP H 77 -169.94 -125.54
REMARK 500 ASP H 79 -10.94 -31.83
REMARK 500 ARG H 147 24.39 49.34
REMARK 500 LYS H 170D -62.90 -25.56
REMARK 500 VAL H 170E -167.64 -121.49
REMARK 500 PRO H 170I -169.36 -56.93
REMARK 500 ASP H 189 175.92 172.35
REMARK 500 ASP H 189 176.70 172.35
REMARK 500 SER H 195 140.50 -36.14
REMARK 500 ARG H 204 53.41 36.71
REMARK 500 MET H 242 0.90 -66.14
REMARK 500 PRO H 248 53.07 -95.92
REMARK 500 PRO H 255 123.81 -30.16
REMARK 500 PHE T 19 -4.92 80.48
REMARK 500 CYS T 49 65.10 33.49
REMARK 500 TYR T 51 56.36 26.62
REMARK 500 SER T 88 -32.26 -20.96
REMARK 500 ASN T 137 62.20 21.84
REMARK 500 ASN T 138 6.38 55.82
REMARK 500 TYR T 156 -49.65 175.14
REMARK 500 ASN T 199 50.55 31.15
REMARK 500 SER T 202 -144.40 -104.34
REMARK 500 THR T 203 -162.24 -116.07
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 CR9 H 258
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DAN RELATED DB: PDB
REMARK 900 STRUCTURE SOLVED BY MOLECULAR REPLACEMENT WITH 1DAN
DBREF 1O5D L 1 152 UNP P08709 FA7_HUMAN 61 212
DBREF 1O5D H 16 257 UNP P08709 FA7_HUMAN 213 466
DBREF 1O5D T 2 219 UNP P13726 TF_HUMAN 34 251
SEQRES 1 L 152 ALA ASN ALA PHE LEU GLU GLU LEU ARG PRO GLY SER LEU
SEQRES 2 L 152 GLU ARG GLU CYS LYS GLU GLU GLN CYS SER PHE GLU GLU
SEQRES 3 L 152 ALA ARG GLU ILE PHE LYS ASP ALA GLU ARG THR LYS LEU
SEQRES 4 L 152 PHE TRP ILE SER TYR SER ASP GLY ASP GLN CYS ALA SER
SEQRES 5 L 152 SER PRO CYS GLN ASN GLY GLY SER CYS LYS ASP GLN LEU
SEQRES 6 L 152 GLN SER TYR ILE CYS PHE CYS LEU PRO ALA PHE GLU GLY
SEQRES 7 L 152 ARG ASN CYS GLU THR HIS LYS ASP ASP GLN LEU ILE CYS
SEQRES 8 L 152 VAL ASN GLU ASN GLY GLY CYS GLU GLN TYR CYS SER ASP
SEQRES 9 L 152 HIS THR GLY THR LYS ARG SER CYS ARG CYS HIS GLU GLY
SEQRES 10 L 152 TYR SER LEU LEU ALA ASP GLY VAL SER CYS THR PRO THR
SEQRES 11 L 152 VAL GLU TYR PRO CYS GLY LYS ILE PRO ILE LEU GLU LYS
SEQRES 12 L 152 ARG ASN ALA SER LYS PRO GLN GLY ARG
SEQRES 1 H 254 ILE VAL GLY GLY LYS VAL CYS PRO LYS GLY GLU CYS PRO
SEQRES 2 H 254 TRP GLN VAL LEU LEU LEU VAL ASN GLY ALA GLN LEU CYS
SEQRES 3 H 254 GLY GLY THR LEU ILE ASN THR ILE TRP VAL VAL SER ALA
SEQRES 4 H 254 ALA HIS CYS PHE ASP LYS ILE LYS ASN TRP ARG ASN LEU
SEQRES 5 H 254 ILE ALA VAL LEU GLY GLU HIS ASP LEU SER GLU HIS ASP
SEQRES 6 H 254 GLY ASP GLU GLN SER ARG ARG VAL ALA GLN VAL ILE ILE
SEQRES 7 H 254 PRO SER THR TYR VAL PRO GLY THR THR ASN HIS ASP ILE
SEQRES 8 H 254 ALA LEU LEU ARG LEU HIS GLN PRO VAL VAL LEU THR ASP
SEQRES 9 H 254 HIS VAL VAL PRO LEU CYS LEU PRO GLU ARG THR PHE SER
SEQRES 10 H 254 GLU ARG THR LEU ALA PHE VAL ARG PHE SER LEU VAL SER
SEQRES 11 H 254 GLY TRP GLY GLN LEU LEU ASP ARG GLY ALA THR ALA LEU
SEQRES 12 H 254 GLU LEU MET VAL LEU ASN VAL PRO ARG LEU MET THR GLN
SEQRES 13 H 254 ASP CYS LEU GLN GLN SER ARG LYS VAL GLY ASP SER PRO
SEQRES 14 H 254 ASN ILE THR GLU TYR MET PHE CYS ALA GLY TYR SER ASP
SEQRES 15 H 254 GLY SER LYS ASP SER CYS LYS GLY ASP SER GLY GLY PRO
SEQRES 16 H 254 HIS ALA THR HIS TYR ARG GLY THR TRP TYR LEU THR GLY
SEQRES 17 H 254 ILE VAL SER TRP GLY GLN GLY CYS ALA THR VAL GLY HIS
SEQRES 18 H 254 PHE GLY VAL TYR THR ARG VAL SER GLN TYR ILE GLU TRP
SEQRES 19 H 254 LEU GLN LYS LEU MET ARG SER GLU PRO ARG PRO GLY VAL
SEQRES 20 H 254 LEU LEU ARG ALA PRO PHE PRO
SEQRES 1 T 218 GLY THR THR ASN THR VAL ALA ALA TYR ASN LEU THR TRP
SEQRES 2 T 218 LYS SER THR ASN PHE LYS THR ILE LEU GLU TRP GLU PRO
SEQRES 3 T 218 LYS PRO VAL ASN GLN VAL TYR THR VAL GLN ILE SER THR
SEQRES 4 T 218 LYS SER GLY ASP TRP LYS SER LYS CYS PHE TYR THR THR
SEQRES 5 T 218 ASP THR GLU CYS ASP LEU THR ASP GLU ILE VAL LYS ASP
SEQRES 6 T 218 VAL LYS GLN THR TYR LEU ALA ARG VAL PHE SER TYR PRO
SEQRES 7 T 218 ALA GLY ASN VAL GLU SER THR GLY SER ALA GLY GLU PRO
SEQRES 8 T 218 LEU TYR GLU ASN SER PRO GLU PHE THR PRO TYR LEU GLU
SEQRES 9 T 218 THR ASN LEU GLY GLN PRO THR ILE GLN SER PHE GLU GLN
SEQRES 10 T 218 VAL GLY THR LYS VAL ASN VAL THR VAL GLU ASP GLU ARG
SEQRES 11 T 218 THR LEU VAL ARG ARG ASN ASN THR PHE LEU SER LEU ARG
SEQRES 12 T 218 ASP VAL PHE GLY LYS ASP LEU ILE TYR THR LEU TYR TYR
SEQRES 13 T 218 TRP LYS SER SER SER SER GLY LYS LYS THR ALA LYS THR
SEQRES 14 T 218 ASN THR ASN GLU PHE LEU ILE ASP VAL ASP LYS GLY GLU
SEQRES 15 T 218 ASN TYR CYS PHE SER VAL GLN ALA VAL ILE PRO SER ARG
SEQRES 16 T 218 THR VAL ASN ARG LYS SER THR ASP SER PRO VAL GLU CYS
SEQRES 17 T 218 MET GLY GLN GLU LYS GLY GLU PHE ARG GLU
HET CR9 H 258 51
HETNAM CR9 2-{5-[AMINO(IMINIO)METHYL]-6-FLUORO-1H-BENZIMIDAZOL-2-
HETNAM 2 CR9 YL}-6-[(2-METHYLCYCLOHEXYL)OXY]BENZENOLATE
HETSYN CR9 CRA_11092
FORMUL 4 CR9 C21 H23 F N4 O2
FORMUL 5 HOH *588(H2 O)
HELIX 1 1 GLN L 49 SER L 53 5 5
HELIX 2 2 ASP L 86 GLN L 88 5 3
HELIX 3 3 ASN L 93 CYS L 98 5 6
HELIX 4 4 ILE L 138 GLU L 142 5 5
HELIX 5 5 ALA H 55 ASP H 60 5 6
HELIX 6 6 ASN H 60D ARG H 62 5 3
HELIX 7 7 GLU H 125 THR H 129C 1 8
HELIX 8 8 LEU H 129D VAL H 129G 5 4
HELIX 9 9 MET H 164 SER H 170B 1 9
HELIX 10 10 TYR H 234 MET H 242 1 9
HELIX 11 11 LEU T 59 VAL T 64 1 6
HELIX 12 12 THR T 101 THR T 106 1 6
HELIX 13 13 LEU T 143 GLY T 148 1 6
SHEET 1 A 2 SER L 60 ASP L 63 0
SHEET 2 A 2 TYR L 68 PHE L 71 -1 O PHE L 71 N SER L 60
SHEET 1 B 2 PHE L 76 GLU L 77 0
SHEET 2 B 2 THR L 83 HIS L 84 -1 O THR L 83 N GLU L 77
SHEET 1 C 2 TYR L 101 HIS L 105 0
SHEET 2 C 2 THR L 108 ARG L 113 -1 O ARG L 113 N TYR L 101
SHEET 1 D 2 TYR L 118 LEU L 120 0
SHEET 2 D 2 CYS L 127 PRO L 129 -1 O THR L 128 N SER L 119
SHEET 1 E 8 LYS H 20 VAL H 21 0
SHEET 2 E 8 MET H 156 LEU H 163 -1 O VAL H 157 N LYS H 20
SHEET 3 E 8 MET H 180 ALA H 183 -1 O CYS H 182 N LEU H 163
SHEET 4 E 8 GLY H 226 ARG H 230 -1 O TYR H 228 N PHE H 181
SHEET 5 E 8 THR H 206 TRP H 215 -1 N TRP H 215 O VAL H 227
SHEET 6 E 8 PRO H 198 TYR H 203 -1 N TYR H 203 O THR H 206
SHEET 7 E 8 PHE H 135 GLY H 140 -1 N LEU H 137 O ALA H 200
SHEET 8 E 8 MET H 156 LEU H 163 -1 O MET H 156 N GLY H 140
SHEET 1 F 8 LEU H 251 ALA H 254 0
SHEET 2 F 8 GLN H 81 PRO H 91 1 N VAL H 88 O LEU H 252
SHEET 3 F 8 ALA H 104 LEU H 108 -1 O LEU H 105 N ILE H 89
SHEET 4 F 8 TRP H 51 SER H 54 -1 N VAL H 52 O LEU H 106
SHEET 5 F 8 ALA H 39 ASN H 48 -1 N THR H 45 O VAL H 53
SHEET 6 F 8 GLN H 30 VAL H 35 -1 N VAL H 35 O ALA H 39
SHEET 7 F 8 LEU H 64 LEU H 68 -1 O ILE H 65 N LEU H 34
SHEET 8 F 8 GLN H 81 PRO H 91 -1 O GLN H 81 N LEU H 68
SHEET 1 G 3 TYR T 10 THR T 17 0
SHEET 2 G 3 LYS T 20 GLU T 26 -1 O ILE T 22 N LYS T 15
SHEET 3 G 3 GLU T 56 ASP T 58 -1 O CYS T 57 N LEU T 23
SHEET 1 H 4 LYS T 46 THR T 52 0
SHEET 2 H 4 GLN T 32 THR T 40 -1 N VAL T 36 O LYS T 48
SHEET 3 H 4 TYR T 71 PRO T 79 -1 O PHE T 76 N THR T 35
SHEET 4 H 4 LEU T 93 ASN T 96 -1 O GLU T 95 N VAL T 75
SHEET 1 I 2 ARG T 131 ARG T 136 0
SHEET 2 I 2 THR T 139 SER T 142 -1 O THR T 139 N ARG T 136
SHEET 1 J 2 ILE T 152 THR T 154 0
SHEET 2 J 2 GLN T 190 VAL T 192 -1 O VAL T 192 N ILE T 152
SSBOND 1 CYS L 50 CYS L 61 1555 1555 2.02
SSBOND 2 CYS L 55 CYS L 70 1555 1555 2.02
SSBOND 3 CYS L 72 CYS L 81 1555 1555 2.04
SSBOND 4 CYS L 91 CYS L 102 1555 1555 2.02
SSBOND 5 CYS L 98 CYS L 112 1555 1555 2.02
SSBOND 6 CYS L 114 CYS L 127 1555 1555 2.03
SSBOND 7 CYS L 135 CYS H 122 1555 1555 2.04
SSBOND 8 CYS H 22 CYS H 27 1555 1555 2.03
SSBOND 9 CYS H 42 CYS H 58 1555 1555 2.02
SSBOND 10 CYS H 168 CYS H 182 1555 1555 2.04
SSBOND 11 CYS H 191 CYS H 220 1555 1555 2.04
SSBOND 12 CYS T 49 CYS T 57 1555 1555 2.05
CISPEP 1 PHE H 256 PRO H 257 0 1.83
CISPEP 2 GLU T 26 PRO T 27 0 -12.23
SITE 1 AC1 14 CYS H 42 HIS H 57 ASP H 189 SER H 190
SITE 2 AC1 14 LYS H 192 SER H 195 VAL H 213 SER H 214
SITE 3 AC1 14 TRP H 215 GLY H 219 CYS H 220 GLY H 226
SITE 4 AC1 14 HOH H 271 HOH H 289
CRYST1 78.540 69.030 79.120 90.00 89.99 90.00 P 1 21 1 2
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 0.012732 0.000000 -0.000002 0.00000
SCALE2 0.000000 0.014486 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012639 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
