HEADER TRANSFERASE/TRANSFERASE INHIBITOR 25-FEB-11 3QV7
TITLE CRYSTAL STRUCTURE OF LEISHMANIA MEXICANA PYRUVATE KINASE(LMPYK)IN
TITLE 2 COMPLEX WITH PONCEAU S AND ACID BLUE 25.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PYRUVATE KINASE;
COMPND 3 CHAIN: D, A, B, C;
COMPND 4 SYNONYM: PK;
COMPND 5 EC: 2.7.1.40;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LEISHMANIA MEXICANA;
SOURCE 3 ORGANISM_TAXID: 5665;
SOURCE 4 STRAIN: BEL46;
SOURCE 5 GENE: PKY;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA 2 PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET3A
KEYWDS PYRUVATE KINASE, GLYCOLYSIS, TIM BARREL, SUGAR KINASE, ADP/ATP
KEYWDS 2 BINDING, CYTOSOL, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.P.MORGAN,D.S.AULD,I.W.MCNAE,M.W.NOWICKI,P.A.M.MICHELS,
AUTHOR 2 L.A.FOTHERGILL-GILMORE,M.D.WALKINSHAW
REVDAT 6 13-SEP-23 3QV7 1 REMARK LINK
REVDAT 5 29-JAN-20 3QV7 1 REMARK
REVDAT 4 21-SEP-11 3QV7 1 JRNL
REVDAT 3 17-AUG-11 3QV7 1 AUTHOR
REVDAT 2 03-AUG-11 3QV7 1 JRNL
REVDAT 1 29-JUN-11 3QV7 0
JRNL AUTH H.P.MORGAN,I.W.MCNAE,M.W.NOWICKI,W.ZHONG,P.A.MICHELS,
JRNL AUTH 2 D.S.AULD,L.A.FOTHERGILL-GILMORE,M.D.WALKINSHAW
JRNL TITL THE TRYPANOCIDAL DRUG SURAMIN AND OTHER TRYPAN BLUE MIMETICS
JRNL TITL 2 ARE INHIBITORS OF PYRUVATE KINASES AND BIND TO THE ADENOSINE
JRNL TITL 3 SITE.
JRNL REF J.BIOL.CHEM. V. 286 31232 2011
JRNL REFN ISSN 0021-9258
JRNL PMID 21733839
JRNL DOI 10.1074/JBC.M110.212613
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 21.14
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 84872
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 + TEST SET) : 0.217
REMARK 3 R VALUE (WORKING SET) : 0.215
REMARK 3 FREE R VALUE : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4480
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.77
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6079
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.84
REMARK 3 BIN R VALUE (WORKING SET) : 0.3170
REMARK 3 BIN FREE R VALUE SET COUNT : 337
REMARK 3 BIN FREE R VALUE : 0.3370
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 13572
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 270
REMARK 3 SOLVENT ATOMS : 505
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 56.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.25
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.39000
REMARK 3 B22 (A**2) : -0.23000
REMARK 3 B33 (A**2) : 0.22000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.44000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.277
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.206
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.317
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.923
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.903
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 14138 ; 0.006 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 19205 ; 0.859 ; 1.974
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1798 ; 4.233 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 615 ;36.249 ;24.732
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2413 ;14.122 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 86 ;14.023 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2205 ; 0.055 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10616 ; 0.003 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 8881 ; 0.232 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 14347 ; 0.428 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5257 ; 0.400 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4847 ; 0.749 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3QV7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-MAR-11.
REMARK 100 THE DEPOSITION ID IS D_1000064144.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 89354
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 21.140
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.700
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.12300
REMARK 200 R SYM (I) : 0.14400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.54200
REMARK 200 R SYM FOR SHELL (I) : 0.64000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 1PKL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 7-16% PEG 8,000, 20 MM TEA BUFFER (PH
REMARK 280 7.2), 50 MM MGCL2, 100 MM KCL AND 10-25% GLYCEROL, VAPOR
REMARK 280 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 91.05450
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 82.39900
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 91.05450
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 82.39900
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, A, B, C
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 MET D 0
REMARK 465 HIS D 483
REMARK 465 LYS D 484
REMARK 465 VAL D 485
REMARK 465 LYS D 486
REMARK 465 MET A 0
REMARK 465 ASP A 482
REMARK 465 HIS A 483
REMARK 465 LYS A 484
REMARK 465 VAL A 485
REMARK 465 LYS A 486
REMARK 465 MET B 0
REMARK 465 GLU B 88
REMARK 465 ILE B 89
REMARK 465 ARG B 90
REMARK 465 THR B 91
REMARK 465 GLY B 92
REMARK 465 GLN B 93
REMARK 465 PHE B 94
REMARK 465 VAL B 95
REMARK 465 GLY B 96
REMARK 465 GLY B 97
REMARK 465 ASP B 98
REMARK 465 ALA B 99
REMARK 465 VAL B 100
REMARK 465 MET B 101
REMARK 465 GLU B 102
REMARK 465 ARG B 103
REMARK 465 GLY B 104
REMARK 465 ALA B 105
REMARK 465 THR B 106
REMARK 465 CYS B 107
REMARK 465 TYR B 108
REMARK 465 VAL B 109
REMARK 465 THR B 110
REMARK 465 THR B 111
REMARK 465 ASP B 112
REMARK 465 PRO B 113
REMARK 465 ALA B 114
REMARK 465 PHE B 115
REMARK 465 ALA B 116
REMARK 465 ASP B 117
REMARK 465 LYS B 118
REMARK 465 GLY B 119
REMARK 465 THR B 120
REMARK 465 LYS B 121
REMARK 465 ASP B 122
REMARK 465 LYS B 123
REMARK 465 PHE B 124
REMARK 465 TYR B 125
REMARK 465 ILE B 126
REMARK 465 ASP B 127
REMARK 465 TYR B 128
REMARK 465 GLN B 129
REMARK 465 ASN B 130
REMARK 465 LEU B 131
REMARK 465 SER B 132
REMARK 465 LYS B 133
REMARK 465 VAL B 134
REMARK 465 VAL B 135
REMARK 465 ARG B 136
REMARK 465 PRO B 137
REMARK 465 GLY B 138
REMARK 465 ASN B 139
REMARK 465 TYR B 140
REMARK 465 ILE B 141
REMARK 465 TYR B 142
REMARK 465 ILE B 143
REMARK 465 ASP B 144
REMARK 465 ASP B 145
REMARK 465 GLY B 146
REMARK 465 ILE B 147
REMARK 465 LEU B 148
REMARK 465 ILE B 149
REMARK 465 LEU B 150
REMARK 465 GLN B 151
REMARK 465 VAL B 152
REMARK 465 GLN B 153
REMARK 465 SER B 154
REMARK 465 HIS B 155
REMARK 465 GLU B 156
REMARK 465 ASP B 157
REMARK 465 GLU B 158
REMARK 465 GLN B 159
REMARK 465 THR B 160
REMARK 465 LEU B 161
REMARK 465 GLU B 162
REMARK 465 CYS B 163
REMARK 465 THR B 164
REMARK 465 VAL B 165
REMARK 465 THR B 166
REMARK 465 ASN B 167
REMARK 465 SER B 168
REMARK 465 HIS B 169
REMARK 465 THR B 170
REMARK 465 ILE B 171
REMARK 465 SER B 172
REMARK 465 ASP B 173
REMARK 465 ARG B 174
REMARK 465 ARG B 175
REMARK 465 GLY B 176
REMARK 465 VAL B 177
REMARK 465 ASN B 178
REMARK 465 LEU B 179
REMARK 465 PRO B 180
REMARK 465 GLY B 181
REMARK 465 CYS B 182
REMARK 465 ASP B 183
REMARK 465 VAL B 184
REMARK 465 ASP B 185
REMARK 465 MET C 0
REMARK 465 GLU C 88
REMARK 465 ILE C 89
REMARK 465 ARG C 90
REMARK 465 THR C 91
REMARK 465 GLY C 92
REMARK 465 GLN C 93
REMARK 465 PHE C 94
REMARK 465 VAL C 95
REMARK 465 GLY C 96
REMARK 465 GLY C 97
REMARK 465 ASP C 98
REMARK 465 ALA C 99
REMARK 465 VAL C 100
REMARK 465 MET C 101
REMARK 465 GLU C 102
REMARK 465 ARG C 103
REMARK 465 GLY C 104
REMARK 465 ALA C 105
REMARK 465 THR C 106
REMARK 465 CYS C 107
REMARK 465 TYR C 108
REMARK 465 VAL C 109
REMARK 465 THR C 110
REMARK 465 THR C 111
REMARK 465 ASP C 112
REMARK 465 PRO C 113
REMARK 465 ALA C 114
REMARK 465 PHE C 115
REMARK 465 ALA C 116
REMARK 465 ASP C 117
REMARK 465 LYS C 118
REMARK 465 GLY C 119
REMARK 465 THR C 120
REMARK 465 LYS C 121
REMARK 465 ASP C 122
REMARK 465 LYS C 123
REMARK 465 PHE C 124
REMARK 465 TYR C 125
REMARK 465 ILE C 126
REMARK 465 ASP C 127
REMARK 465 TYR C 128
REMARK 465 GLN C 129
REMARK 465 ASN C 130
REMARK 465 LEU C 131
REMARK 465 SER C 132
REMARK 465 LYS C 133
REMARK 465 VAL C 134
REMARK 465 VAL C 135
REMARK 465 ARG C 136
REMARK 465 PRO C 137
REMARK 465 GLY C 138
REMARK 465 ASN C 139
REMARK 465 TYR C 140
REMARK 465 ILE C 141
REMARK 465 TYR C 142
REMARK 465 ILE C 143
REMARK 465 ASP C 144
REMARK 465 ASP C 145
REMARK 465 GLY C 146
REMARK 465 ILE C 147
REMARK 465 LEU C 148
REMARK 465 ILE C 149
REMARK 465 LEU C 150
REMARK 465 GLN C 151
REMARK 465 VAL C 152
REMARK 465 GLN C 153
REMARK 465 SER C 154
REMARK 465 HIS C 155
REMARK 465 GLU C 156
REMARK 465 ASP C 157
REMARK 465 GLU C 158
REMARK 465 GLN C 159
REMARK 465 THR C 160
REMARK 465 LEU C 161
REMARK 465 GLU C 162
REMARK 465 CYS C 163
REMARK 465 THR C 164
REMARK 465 VAL C 165
REMARK 465 THR C 166
REMARK 465 ASN C 167
REMARK 465 SER C 168
REMARK 465 HIS C 169
REMARK 465 THR C 170
REMARK 465 ILE C 171
REMARK 465 SER C 172
REMARK 465 ASP C 173
REMARK 465 ARG C 174
REMARK 465 ARG C 175
REMARK 465 GLY C 176
REMARK 465 VAL C 177
REMARK 465 ASN C 178
REMARK 465 LEU C 179
REMARK 465 PRO C 180
REMARK 465 GLY C 181
REMARK 465 CYS C 182
REMARK 465 ASP C 183
REMARK 465 HIS C 483
REMARK 465 LYS C 484
REMARK 465 VAL C 485
REMARK 465 LYS C 486
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 LYS D 118 37.78 -143.70
REMARK 500 ASP D 144 74.60 64.01
REMARK 500 ASP D 157 -153.17 -149.87
REMARK 500 THR D 296 141.89 63.55
REMARK 500 MET D 298 -60.26 -99.52
REMARK 500 SER D 330 -96.40 -96.39
REMARK 500 ARG D 413 73.28 54.14
REMARK 500 LYS D 453 -8.89 78.38
REMARK 500 TYR D 488 84.71 60.91
REMARK 500 ASP A 144 69.90 64.59
REMARK 500 ASP A 157 -151.08 -154.94
REMARK 500 LEU A 179 79.79 -118.28
REMARK 500 THR A 296 136.39 68.84
REMARK 500 SER A 330 -102.77 -108.88
REMARK 500 ARG A 413 74.46 50.97
REMARK 500 LYS A 453 -3.30 74.33
REMARK 500 ALA B 188 -75.86 -59.12
REMARK 500 THR B 296 147.69 67.36
REMARK 500 MET B 298 -78.24 -80.44
REMARK 500 LEU B 299 54.10 -118.27
REMARK 500 SER B 330 -100.39 -105.21
REMARK 500 ARG B 413 74.57 51.80
REMARK 500 ASN B 415 35.74 -89.04
REMARK 500 LYS B 453 -5.20 76.79
REMARK 500 LEU C 186 145.11 -38.95
REMARK 500 ALA C 188 -71.90 -61.58
REMARK 500 THR C 296 142.36 66.17
REMARK 500 SER C 330 -103.14 -93.58
REMARK 500 ARG C 413 76.59 55.81
REMARK 500 TYR C 488 90.38 62.09
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 K D 501 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN D 51 OD1
REMARK 620 2 SER D 53 OG 60.9
REMARK 620 3 THR D 84 O 102.5 88.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 501 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 240 OE1
REMARK 620 2 HOH A 595 O 81.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 502 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 354 O
REMARK 620 2 LEU A 357 O 71.2
REMARK 620 3 GLU A 359 OE2 109.1 68.2
REMARK 620 4 GLU A 359 OE1 80.4 81.1 38.4
REMARK 620 5 HOH A 663 O 77.6 125.2 81.7 49.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B 503 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN B 354 O
REMARK 620 2 LEU B 357 O 67.8
REMARK 620 3 GLU B 359 OE2 111.1 74.5
REMARK 620 4 GLU B 359 OE1 73.8 68.7 38.8
REMARK 620 5 HOH B 575 O 103.6 90.1 132.3 158.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K C 500 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN C 51 OD1
REMARK 620 2 SER C 53 OG 61.0
REMARK 620 3 ASP C 83 OD1 86.9 128.8
REMARK 620 4 THR C 84 O 93.7 82.0 59.8
REMARK 620 5 HOH C 656 O 173.6 113.2 99.2 88.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K C 501 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN C 354 O
REMARK 620 2 LEU C 357 O 64.4
REMARK 620 3 GLU C 359 OE1 79.5 75.5
REMARK 620 4 GLU C 359 OE2 111.3 70.3 40.2
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 499
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K D 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE QV7 D 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE QV7 A 499
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE QV7 B 499
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE QV8 B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE QV7 B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE QV7 B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 499
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PKL RELATED DB: PDB
REMARK 900 APO STRUCTURE
REMARK 900 RELATED ID: 3QV6 RELATED DB: PDB
REMARK 900 RELATED ID: 3QV8 RELATED DB: PDB
REMARK 900 RELATED ID: 3QV9 RELATED DB: PDB
DBREF 3QV7 D 0 498 UNP Q27686 KPYK_LEIME 1 499
DBREF 3QV7 A 0 498 UNP Q27686 KPYK_LEIME 1 499
DBREF 3QV7 B 0 498 UNP Q27686 KPYK_LEIME 1 499
DBREF 3QV7 C 0 498 UNP Q27686 KPYK_LEIME 1 499
SEQRES 1 D 499 MET SER GLN LEU ALA HIS ASN LEU THR LEU SER ILE PHE
SEQRES 2 D 499 ASP PRO VAL ALA ASN TYR ARG ALA ALA ARG ILE ILE CYS
SEQRES 3 D 499 THR ILE GLY PRO SER THR GLN SER VAL GLU ALA LEU LYS
SEQRES 4 D 499 GLY LEU ILE GLN SER GLY MET SER VAL ALA ARG MET ASN
SEQRES 5 D 499 PHE SER HIS GLY SER HIS GLU TYR HIS GLN THR THR ILE
SEQRES 6 D 499 ASN ASN VAL ARG GLN ALA ALA ALA GLU LEU GLY VAL ASN
SEQRES 7 D 499 ILE ALA ILE ALA LEU ASP THR LYS GLY PRO GLU ILE ARG
SEQRES 8 D 499 THR GLY GLN PHE VAL GLY GLY ASP ALA VAL MET GLU ARG
SEQRES 9 D 499 GLY ALA THR CYS TYR VAL THR THR ASP PRO ALA PHE ALA
SEQRES 10 D 499 ASP LYS GLY THR LYS ASP LYS PHE TYR ILE ASP TYR GLN
SEQRES 11 D 499 ASN LEU SER LYS VAL VAL ARG PRO GLY ASN TYR ILE TYR
SEQRES 12 D 499 ILE ASP ASP GLY ILE LEU ILE LEU GLN VAL GLN SER HIS
SEQRES 13 D 499 GLU ASP GLU GLN THR LEU GLU CYS THR VAL THR ASN SER
SEQRES 14 D 499 HIS THR ILE SER ASP ARG ARG GLY VAL ASN LEU PRO GLY
SEQRES 15 D 499 CYS ASP VAL ASP LEU PRO ALA VAL SER ALA LYS ASP ARG
SEQRES 16 D 499 VAL ASP LEU GLN PHE GLY VAL GLU GLN GLY VAL ASP MET
SEQRES 17 D 499 ILE PHE ALA SER PHE ILE ARG SER ALA GLU GLN VAL GLY
SEQRES 18 D 499 ASP VAL ARG LYS ALA LEU GLY PRO LYS GLY ARG ASP ILE
SEQRES 19 D 499 MET ILE ILE CYS LYS ILE GLU ASN HIS GLN GLY VAL GLN
SEQRES 20 D 499 ASN ILE ASP SER ILE ILE GLU GLU SER ASP GLY ILE MET
SEQRES 21 D 499 VAL ALA ARG GLY ASP LEU GLY VAL GLU ILE PRO ALA GLU
SEQRES 22 D 499 LYS VAL VAL VAL ALA GLN LYS ILE LEU ILE SER LYS CYS
SEQRES 23 D 499 ASN VAL ALA GLY LYS PRO VAL ILE CYS ALA THR GLN MET
SEQRES 24 D 499 LEU GLU SER MET THR TYR ASN PRO ARG PRO THR ARG ALA
SEQRES 25 D 499 GLU VAL SER ASP VAL ALA ASN ALA VAL PHE ASN GLY ALA
SEQRES 26 D 499 ASP CYS VAL MET LEU SER GLY GLU THR ALA LYS GLY LYS
SEQRES 27 D 499 TYR PRO ASN GLU VAL VAL GLN TYR MET ALA ARG ILE CYS
SEQRES 28 D 499 LEU GLU ALA GLN SER ALA LEU ASN GLU TYR VAL PHE PHE
SEQRES 29 D 499 ASN SER ILE LYS LYS LEU GLN HIS ILE PRO MET SER ALA
SEQRES 30 D 499 ASP GLU ALA VAL CYS SER SER ALA VAL ASN SER VAL TYR
SEQRES 31 D 499 GLU THR LYS ALA LYS ALA MET VAL VAL LEU SER ASN THR
SEQRES 32 D 499 GLY ARG SER ALA ARG LEU VAL ALA LYS TYR ARG PRO ASN
SEQRES 33 D 499 CYS PRO ILE VAL CYS VAL THR THR ARG LEU GLN THR CYS
SEQRES 34 D 499 ARG GLN LEU ASN ILE THR GLN GLY VAL GLU SER VAL PHE
SEQRES 35 D 499 PHE ASP ALA ASP LYS LEU GLY HIS ASP GLU GLY LYS GLU
SEQRES 36 D 499 HIS ARG VAL ALA ALA GLY VAL GLU PHE ALA LYS SER LYS
SEQRES 37 D 499 GLY TYR VAL GLN THR GLY ASP TYR CYS VAL VAL ILE HIS
SEQRES 38 D 499 ALA ASP HIS LYS VAL LYS GLY TYR ALA ASN GLN THR ARG
SEQRES 39 D 499 ILE LEU LEU VAL GLU
SEQRES 1 A 499 MET SER GLN LEU ALA HIS ASN LEU THR LEU SER ILE PHE
SEQRES 2 A 499 ASP PRO VAL ALA ASN TYR ARG ALA ALA ARG ILE ILE CYS
SEQRES 3 A 499 THR ILE GLY PRO SER THR GLN SER VAL GLU ALA LEU LYS
SEQRES 4 A 499 GLY LEU ILE GLN SER GLY MET SER VAL ALA ARG MET ASN
SEQRES 5 A 499 PHE SER HIS GLY SER HIS GLU TYR HIS GLN THR THR ILE
SEQRES 6 A 499 ASN ASN VAL ARG GLN ALA ALA ALA GLU LEU GLY VAL ASN
SEQRES 7 A 499 ILE ALA ILE ALA LEU ASP THR LYS GLY PRO GLU ILE ARG
SEQRES 8 A 499 THR GLY GLN PHE VAL GLY GLY ASP ALA VAL MET GLU ARG
SEQRES 9 A 499 GLY ALA THR CYS TYR VAL THR THR ASP PRO ALA PHE ALA
SEQRES 10 A 499 ASP LYS GLY THR LYS ASP LYS PHE TYR ILE ASP TYR GLN
SEQRES 11 A 499 ASN LEU SER LYS VAL VAL ARG PRO GLY ASN TYR ILE TYR
SEQRES 12 A 499 ILE ASP ASP GLY ILE LEU ILE LEU GLN VAL GLN SER HIS
SEQRES 13 A 499 GLU ASP GLU GLN THR LEU GLU CYS THR VAL THR ASN SER
SEQRES 14 A 499 HIS THR ILE SER ASP ARG ARG GLY VAL ASN LEU PRO GLY
SEQRES 15 A 499 CYS ASP VAL ASP LEU PRO ALA VAL SER ALA LYS ASP ARG
SEQRES 16 A 499 VAL ASP LEU GLN PHE GLY VAL GLU GLN GLY VAL ASP MET
SEQRES 17 A 499 ILE PHE ALA SER PHE ILE ARG SER ALA GLU GLN VAL GLY
SEQRES 18 A 499 ASP VAL ARG LYS ALA LEU GLY PRO LYS GLY ARG ASP ILE
SEQRES 19 A 499 MET ILE ILE CYS LYS ILE GLU ASN HIS GLN GLY VAL GLN
SEQRES 20 A 499 ASN ILE ASP SER ILE ILE GLU GLU SER ASP GLY ILE MET
SEQRES 21 A 499 VAL ALA ARG GLY ASP LEU GLY VAL GLU ILE PRO ALA GLU
SEQRES 22 A 499 LYS VAL VAL VAL ALA GLN LYS ILE LEU ILE SER LYS CYS
SEQRES 23 A 499 ASN VAL ALA GLY LYS PRO VAL ILE CYS ALA THR GLN MET
SEQRES 24 A 499 LEU GLU SER MET THR TYR ASN PRO ARG PRO THR ARG ALA
SEQRES 25 A 499 GLU VAL SER ASP VAL ALA ASN ALA VAL PHE ASN GLY ALA
SEQRES 26 A 499 ASP CYS VAL MET LEU SER GLY GLU THR ALA LYS GLY LYS
SEQRES 27 A 499 TYR PRO ASN GLU VAL VAL GLN TYR MET ALA ARG ILE CYS
SEQRES 28 A 499 LEU GLU ALA GLN SER ALA LEU ASN GLU TYR VAL PHE PHE
SEQRES 29 A 499 ASN SER ILE LYS LYS LEU GLN HIS ILE PRO MET SER ALA
SEQRES 30 A 499 ASP GLU ALA VAL CYS SER SER ALA VAL ASN SER VAL TYR
SEQRES 31 A 499 GLU THR LYS ALA LYS ALA MET VAL VAL LEU SER ASN THR
SEQRES 32 A 499 GLY ARG SER ALA ARG LEU VAL ALA LYS TYR ARG PRO ASN
SEQRES 33 A 499 CYS PRO ILE VAL CYS VAL THR THR ARG LEU GLN THR CYS
SEQRES 34 A 499 ARG GLN LEU ASN ILE THR GLN GLY VAL GLU SER VAL PHE
SEQRES 35 A 499 PHE ASP ALA ASP LYS LEU GLY HIS ASP GLU GLY LYS GLU
SEQRES 36 A 499 HIS ARG VAL ALA ALA GLY VAL GLU PHE ALA LYS SER LYS
SEQRES 37 A 499 GLY TYR VAL GLN THR GLY ASP TYR CYS VAL VAL ILE HIS
SEQRES 38 A 499 ALA ASP HIS LYS VAL LYS GLY TYR ALA ASN GLN THR ARG
SEQRES 39 A 499 ILE LEU LEU VAL GLU
SEQRES 1 B 499 MET SER GLN LEU ALA HIS ASN LEU THR LEU SER ILE PHE
SEQRES 2 B 499 ASP PRO VAL ALA ASN TYR ARG ALA ALA ARG ILE ILE CYS
SEQRES 3 B 499 THR ILE GLY PRO SER THR GLN SER VAL GLU ALA LEU LYS
SEQRES 4 B 499 GLY LEU ILE GLN SER GLY MET SER VAL ALA ARG MET ASN
SEQRES 5 B 499 PHE SER HIS GLY SER HIS GLU TYR HIS GLN THR THR ILE
SEQRES 6 B 499 ASN ASN VAL ARG GLN ALA ALA ALA GLU LEU GLY VAL ASN
SEQRES 7 B 499 ILE ALA ILE ALA LEU ASP THR LYS GLY PRO GLU ILE ARG
SEQRES 8 B 499 THR GLY GLN PHE VAL GLY GLY ASP ALA VAL MET GLU ARG
SEQRES 9 B 499 GLY ALA THR CYS TYR VAL THR THR ASP PRO ALA PHE ALA
SEQRES 10 B 499 ASP LYS GLY THR LYS ASP LYS PHE TYR ILE ASP TYR GLN
SEQRES 11 B 499 ASN LEU SER LYS VAL VAL ARG PRO GLY ASN TYR ILE TYR
SEQRES 12 B 499 ILE ASP ASP GLY ILE LEU ILE LEU GLN VAL GLN SER HIS
SEQRES 13 B 499 GLU ASP GLU GLN THR LEU GLU CYS THR VAL THR ASN SER
SEQRES 14 B 499 HIS THR ILE SER ASP ARG ARG GLY VAL ASN LEU PRO GLY
SEQRES 15 B 499 CYS ASP VAL ASP LEU PRO ALA VAL SER ALA LYS ASP ARG
SEQRES 16 B 499 VAL ASP LEU GLN PHE GLY VAL GLU GLN GLY VAL ASP MET
SEQRES 17 B 499 ILE PHE ALA SER PHE ILE ARG SER ALA GLU GLN VAL GLY
SEQRES 18 B 499 ASP VAL ARG LYS ALA LEU GLY PRO LYS GLY ARG ASP ILE
SEQRES 19 B 499 MET ILE ILE CYS LYS ILE GLU ASN HIS GLN GLY VAL GLN
SEQRES 20 B 499 ASN ILE ASP SER ILE ILE GLU GLU SER ASP GLY ILE MET
SEQRES 21 B 499 VAL ALA ARG GLY ASP LEU GLY VAL GLU ILE PRO ALA GLU
SEQRES 22 B 499 LYS VAL VAL VAL ALA GLN LYS ILE LEU ILE SER LYS CYS
SEQRES 23 B 499 ASN VAL ALA GLY LYS PRO VAL ILE CYS ALA THR GLN MET
SEQRES 24 B 499 LEU GLU SER MET THR TYR ASN PRO ARG PRO THR ARG ALA
SEQRES 25 B 499 GLU VAL SER ASP VAL ALA ASN ALA VAL PHE ASN GLY ALA
SEQRES 26 B 499 ASP CYS VAL MET LEU SER GLY GLU THR ALA LYS GLY LYS
SEQRES 27 B 499 TYR PRO ASN GLU VAL VAL GLN TYR MET ALA ARG ILE CYS
SEQRES 28 B 499 LEU GLU ALA GLN SER ALA LEU ASN GLU TYR VAL PHE PHE
SEQRES 29 B 499 ASN SER ILE LYS LYS LEU GLN HIS ILE PRO MET SER ALA
SEQRES 30 B 499 ASP GLU ALA VAL CYS SER SER ALA VAL ASN SER VAL TYR
SEQRES 31 B 499 GLU THR LYS ALA LYS ALA MET VAL VAL LEU SER ASN THR
SEQRES 32 B 499 GLY ARG SER ALA ARG LEU VAL ALA LYS TYR ARG PRO ASN
SEQRES 33 B 499 CYS PRO ILE VAL CYS VAL THR THR ARG LEU GLN THR CYS
SEQRES 34 B 499 ARG GLN LEU ASN ILE THR GLN GLY VAL GLU SER VAL PHE
SEQRES 35 B 499 PHE ASP ALA ASP LYS LEU GLY HIS ASP GLU GLY LYS GLU
SEQRES 36 B 499 HIS ARG VAL ALA ALA GLY VAL GLU PHE ALA LYS SER LYS
SEQRES 37 B 499 GLY TYR VAL GLN THR GLY ASP TYR CYS VAL VAL ILE HIS
SEQRES 38 B 499 ALA ASP HIS LYS VAL LYS GLY TYR ALA ASN GLN THR ARG
SEQRES 39 B 499 ILE LEU LEU VAL GLU
SEQRES 1 C 499 MET SER GLN LEU ALA HIS ASN LEU THR LEU SER ILE PHE
SEQRES 2 C 499 ASP PRO VAL ALA ASN TYR ARG ALA ALA ARG ILE ILE CYS
SEQRES 3 C 499 THR ILE GLY PRO SER THR GLN SER VAL GLU ALA LEU LYS
SEQRES 4 C 499 GLY LEU ILE GLN SER GLY MET SER VAL ALA ARG MET ASN
SEQRES 5 C 499 PHE SER HIS GLY SER HIS GLU TYR HIS GLN THR THR ILE
SEQRES 6 C 499 ASN ASN VAL ARG GLN ALA ALA ALA GLU LEU GLY VAL ASN
SEQRES 7 C 499 ILE ALA ILE ALA LEU ASP THR LYS GLY PRO GLU ILE ARG
SEQRES 8 C 499 THR GLY GLN PHE VAL GLY GLY ASP ALA VAL MET GLU ARG
SEQRES 9 C 499 GLY ALA THR CYS TYR VAL THR THR ASP PRO ALA PHE ALA
SEQRES 10 C 499 ASP LYS GLY THR LYS ASP LYS PHE TYR ILE ASP TYR GLN
SEQRES 11 C 499 ASN LEU SER LYS VAL VAL ARG PRO GLY ASN TYR ILE TYR
SEQRES 12 C 499 ILE ASP ASP GLY ILE LEU ILE LEU GLN VAL GLN SER HIS
SEQRES 13 C 499 GLU ASP GLU GLN THR LEU GLU CYS THR VAL THR ASN SER
SEQRES 14 C 499 HIS THR ILE SER ASP ARG ARG GLY VAL ASN LEU PRO GLY
SEQRES 15 C 499 CYS ASP VAL ASP LEU PRO ALA VAL SER ALA LYS ASP ARG
SEQRES 16 C 499 VAL ASP LEU GLN PHE GLY VAL GLU GLN GLY VAL ASP MET
SEQRES 17 C 499 ILE PHE ALA SER PHE ILE ARG SER ALA GLU GLN VAL GLY
SEQRES 18 C 499 ASP VAL ARG LYS ALA LEU GLY PRO LYS GLY ARG ASP ILE
SEQRES 19 C 499 MET ILE ILE CYS LYS ILE GLU ASN HIS GLN GLY VAL GLN
SEQRES 20 C 499 ASN ILE ASP SER ILE ILE GLU GLU SER ASP GLY ILE MET
SEQRES 21 C 499 VAL ALA ARG GLY ASP LEU GLY VAL GLU ILE PRO ALA GLU
SEQRES 22 C 499 LYS VAL VAL VAL ALA GLN LYS ILE LEU ILE SER LYS CYS
SEQRES 23 C 499 ASN VAL ALA GLY LYS PRO VAL ILE CYS ALA THR GLN MET
SEQRES 24 C 499 LEU GLU SER MET THR TYR ASN PRO ARG PRO THR ARG ALA
SEQRES 25 C 499 GLU VAL SER ASP VAL ALA ASN ALA VAL PHE ASN GLY ALA
SEQRES 26 C 499 ASP CYS VAL MET LEU SER GLY GLU THR ALA LYS GLY LYS
SEQRES 27 C 499 TYR PRO ASN GLU VAL VAL GLN TYR MET ALA ARG ILE CYS
SEQRES 28 C 499 LEU GLU ALA GLN SER ALA LEU ASN GLU TYR VAL PHE PHE
SEQRES 29 C 499 ASN SER ILE LYS LYS LEU GLN HIS ILE PRO MET SER ALA
SEQRES 30 C 499 ASP GLU ALA VAL CYS SER SER ALA VAL ASN SER VAL TYR
SEQRES 31 C 499 GLU THR LYS ALA LYS ALA MET VAL VAL LEU SER ASN THR
SEQRES 32 C 499 GLY ARG SER ALA ARG LEU VAL ALA LYS TYR ARG PRO ASN
SEQRES 33 C 499 CYS PRO ILE VAL CYS VAL THR THR ARG LEU GLN THR CYS
SEQRES 34 C 499 ARG GLN LEU ASN ILE THR GLN GLY VAL GLU SER VAL PHE
SEQRES 35 C 499 PHE ASP ALA ASP LYS LEU GLY HIS ASP GLU GLY LYS GLU
SEQRES 36 C 499 HIS ARG VAL ALA ALA GLY VAL GLU PHE ALA LYS SER LYS
SEQRES 37 C 499 GLY TYR VAL GLN THR GLY ASP TYR CYS VAL VAL ILE HIS
SEQRES 38 C 499 ALA ASP HIS LYS VAL LYS GLY TYR ALA ASN GLN THR ARG
SEQRES 39 C 499 ILE LEU LEU VAL GLU
HET SO4 D 499 5
HET SO4 D 500 5
HET K D 501 1
HET K D 502 1
HET QV7 D 503 43
HET QV7 A 499 43
HET SO4 A 500 5
HET K A 501 1
HET K A 502 1
HET QV7 B 499 43
HET QV8 B 500 27
HET QV7 B 501 43
HET K B 502 1
HET K B 503 1
HET QV7 B 504 43
HET SO4 C 499 5
HET K C 500 1
HET K C 501 1
HETNAM SO4 SULFATE ION
HETNAM K POTASSIUM ION
HETNAM QV7 3-HYDROXY-4-[(E)-{2-SULFO-4-[(E)-(4-SULFOPHENYL)
HETNAM 2 QV7 DIAZENYL]PHENYL}DIAZENYL]NAPHTHALENE-2,7-DISULFONIC
HETNAM 3 QV7 ACID
HETNAM QV8 9,10-DIOXO-4-(PHENYLAMINO)-9,10-DIHYDROANTHRACENE-2-
HETNAM 2 QV8 SULFONIC ACID
HETSYN QV7 PONCEAU S
HETSYN QV8 ACID BLUE 25
FORMUL 5 SO4 4(O4 S 2-)
FORMUL 7 K 8(K 1+)
FORMUL 9 QV7 5(C22 H16 N4 O13 S4)
FORMUL 15 QV8 C20 H13 N O5 S
FORMUL 23 HOH *505(H2 O)
HELIX 1 1 SER D 1 THR D 8 1 8
HELIX 2 2 SER D 33 GLY D 44 1 12
HELIX 3 3 GLU D 58 GLY D 75 1 18
HELIX 4 4 PHE D 94 GLY D 96 5 3
HELIX 5 5 ASP D 112 LYS D 118 5 7
HELIX 6 6 ASN D 130 VAL D 135 1 6
HELIX 7 7 SER D 190 GLY D 204 1 15
HELIX 8 8 SER D 215 GLY D 227 1 13
HELIX 9 9 PRO D 228 ARG D 231 5 4
HELIX 10 10 ASN D 241 ASN D 247 1 7
HELIX 11 11 ASN D 247 SER D 255 1 9
HELIX 12 12 ARG D 262 VAL D 267 1 6
HELIX 13 13 PRO D 270 GLY D 289 1 20
HELIX 14 14 LEU D 299 TYR D 304 5 6
HELIX 15 15 THR D 309 GLY D 323 1 15
HELIX 16 16 SER D 330 LYS D 335 1 6
HELIX 17 17 TYR D 338 LEU D 357 1 20
HELIX 18 18 ASN D 358 LEU D 369 1 12
HELIX 19 19 SER D 375 LYS D 392 1 18
HELIX 20 20 GLY D 403 TYR D 412 1 10
HELIX 21 21 ARG D 424 LEU D 431 1 8
HELIX 22 22 ASN D 432 THR D 434 5 3
HELIX 23 23 ASP D 443 GLY D 448 1 6
HELIX 24 24 LYS D 453 LYS D 467 1 15
HELIX 25 25 SER A 1 LEU A 9 1 9
HELIX 26 26 SER A 33 GLY A 44 1 12
HELIX 27 27 SER A 56 GLY A 75 1 20
HELIX 28 28 ASP A 112 ALA A 116 5 5
HELIX 29 29 ASN A 130 VAL A 135 1 6
HELIX 30 30 SER A 190 GLN A 203 1 14
HELIX 31 31 SER A 215 GLY A 227 1 13
HELIX 32 32 ASN A 241 ASN A 247 1 7
HELIX 33 33 ASN A 247 SER A 255 1 9
HELIX 34 34 ARG A 262 ILE A 269 1 8
HELIX 35 35 PRO A 270 GLY A 289 1 20
HELIX 36 36 LEU A 299 TYR A 304 5 6
HELIX 37 37 THR A 309 GLY A 323 1 15
HELIX 38 38 SER A 330 LYS A 335 1 6
HELIX 39 39 TYR A 338 LEU A 357 1 20
HELIX 40 40 ASN A 358 LEU A 369 1 12
HELIX 41 41 SER A 375 LYS A 392 1 18
HELIX 42 42 GLY A 403 TYR A 412 1 10
HELIX 43 43 ARG A 424 LEU A 431 1 8
HELIX 44 44 ASN A 432 THR A 434 5 3
HELIX 45 45 ASP A 443 GLY A 448 1 6
HELIX 46 46 LYS A 453 LYS A 467 1 15
HELIX 47 47 SER B 1 THR B 8 1 8
HELIX 48 48 SER B 33 GLY B 44 1 12
HELIX 49 49 SER B 56 GLY B 75 1 20
HELIX 50 50 SER B 190 GLY B 204 1 15
HELIX 51 51 ALA B 216 GLY B 227 1 12
HELIX 52 52 PRO B 228 ARG B 231 5 4
HELIX 53 53 ASN B 241 ASN B 247 1 7
HELIX 54 54 ASN B 247 SER B 255 1 9
HELIX 55 55 ARG B 262 VAL B 267 1 6
HELIX 56 56 PRO B 270 GLY B 289 1 20
HELIX 57 57 LEU B 299 TYR B 304 5 6
HELIX 58 58 THR B 309 GLY B 323 1 15
HELIX 59 59 SER B 330 LYS B 335 1 6
HELIX 60 60 TYR B 338 LEU B 357 1 20
HELIX 61 61 ASN B 358 LEU B 369 1 12
HELIX 62 62 SER B 375 LYS B 392 1 18
HELIX 63 63 GLY B 403 TYR B 412 1 10
HELIX 64 64 ARG B 424 LEU B 431 1 8
HELIX 65 65 ASN B 432 THR B 434 5 3
HELIX 66 66 ASP B 443 GLY B 448 1 6
HELIX 67 67 LYS B 453 LYS B 467 1 15
HELIX 68 68 HIS B 483 GLY B 487 5 5
HELIX 69 69 SER C 1 THR C 8 1 8
HELIX 70 70 SER C 33 GLY C 44 1 12
HELIX 71 71 SER C 56 GLY C 75 1 20
HELIX 72 72 SER C 190 GLN C 203 1 14
HELIX 73 73 ALA C 216 GLY C 227 1 12
HELIX 74 74 PRO C 228 ARG C 231 5 4
HELIX 75 75 ASN C 241 ASN C 247 1 7
HELIX 76 76 ASN C 247 SER C 255 1 9
HELIX 77 77 ARG C 262 ILE C 269 1 8
HELIX 78 78 PRO C 270 GLY C 289 1 20
HELIX 79 79 LEU C 299 THR C 303 5 5
HELIX 80 80 THR C 309 GLY C 323 1 15
HELIX 81 81 SER C 330 LYS C 335 1 6
HELIX 82 82 TYR C 338 LEU C 357 1 20
HELIX 83 83 ASN C 358 LEU C 369 1 12
HELIX 84 84 SER C 375 LYS C 392 1 18
HELIX 85 85 GLY C 403 TYR C 412 1 10
HELIX 86 86 ARG C 424 LEU C 431 1 8
HELIX 87 87 ASN C 432 THR C 434 5 3
HELIX 88 88 ASP C 443 GLY C 448 1 6
HELIX 89 89 LYS C 453 LYS C 467 1 15
SHEET 1 A 9 ARG D 22 THR D 26 0
SHEET 2 A 9 MET D 45 ASN D 51 1 O ARG D 49 N CYS D 25
SHEET 3 A 9 ALA D 79 ASP D 83 1 O ALA D 79 N ALA D 48
SHEET 4 A 9 MET D 207 ALA D 210 1 O PHE D 209 N LEU D 82
SHEET 5 A 9 MET D 234 ILE D 239 1 O ILE D 236 N ILE D 208
SHEET 6 A 9 GLY D 257 ALA D 261 1 O MET D 259 N CYS D 237
SHEET 7 A 9 VAL D 292 ALA D 295 1 O ILE D 293 N VAL D 260
SHEET 8 A 9 CYS D 326 LEU D 329 1 O CYS D 326 N CYS D 294
SHEET 9 A 9 ARG D 22 THR D 26 1 N ILE D 24 O VAL D 327
SHEET 1 B 2 ASP D 98 MET D 101 0
SHEET 2 B 2 HIS D 169 SER D 172 -1 O HIS D 169 N MET D 101
SHEET 1 C 6 LYS D 123 TYR D 125 0
SHEET 2 C 6 THR D 106 THR D 110 1 N THR D 110 O PHE D 124
SHEET 3 C 6 THR D 160 VAL D 165 -1 O CYS D 163 N CYS D 107
SHEET 4 C 6 LEU D 148 HIS D 155 -1 N GLN D 153 O GLU D 162
SHEET 5 C 6 TYR D 140 ILE D 143 -1 N ILE D 141 O LEU D 150
SHEET 6 C 6 VAL D 177 ASN D 178 -1 O ASN D 178 N TYR D 142
SHEET 1 D 5 VAL D 437 PHE D 441 0
SHEET 2 D 5 ILE D 418 THR D 422 1 N CYS D 420 O VAL D 440
SHEET 3 D 5 ALA D 395 LEU D 399 1 N VAL D 398 O VAL D 421
SHEET 4 D 5 TYR D 475 ALA D 481 1 O VAL D 477 N VAL D 397
SHEET 5 D 5 ASN D 490 LEU D 496 -1 O ARG D 493 N VAL D 478
SHEET 1 E 9 ARG A 22 THR A 26 0
SHEET 2 E 9 MET A 45 ASN A 51 1 O ARG A 49 N CYS A 25
SHEET 3 E 9 ALA A 79 ASP A 83 1 O ALA A 79 N ALA A 48
SHEET 4 E 9 MET A 207 ALA A 210 1 O PHE A 209 N LEU A 82
SHEET 5 E 9 MET A 234 ILE A 239 1 O ILE A 236 N ILE A 208
SHEET 6 E 9 GLY A 257 ALA A 261 1 O MET A 259 N CYS A 237
SHEET 7 E 9 VAL A 292 ALA A 295 1 O ILE A 293 N VAL A 260
SHEET 8 E 9 CYS A 326 LEU A 329 1 O CYS A 326 N CYS A 294
SHEET 9 E 9 ARG A 22 THR A 26 1 N ILE A 24 O LEU A 329
SHEET 1 F 2 ASP A 98 MET A 101 0
SHEET 2 F 2 HIS A 169 SER A 172 -1 O ILE A 171 N ALA A 99
SHEET 1 G 6 LYS A 123 TYR A 125 0
SHEET 2 G 6 THR A 106 THR A 110 1 N THR A 110 O PHE A 124
SHEET 3 G 6 THR A 160 VAL A 165 -1 O CYS A 163 N CYS A 107
SHEET 4 G 6 LEU A 148 HIS A 155 -1 N GLN A 153 O GLU A 162
SHEET 5 G 6 TYR A 140 ILE A 143 -1 N ILE A 141 O LEU A 150
SHEET 6 G 6 VAL A 177 ASN A 178 -1 O ASN A 178 N TYR A 142
SHEET 1 H 5 VAL A 437 PHE A 441 0
SHEET 2 H 5 ILE A 418 THR A 422 1 N CYS A 420 O VAL A 440
SHEET 3 H 5 ALA A 395 LEU A 399 1 N MET A 396 O VAL A 419
SHEET 4 H 5 TYR A 475 HIS A 480 1 O ILE A 479 N VAL A 397
SHEET 5 H 5 GLN A 491 LEU A 496 -1 O ARG A 493 N VAL A 478
SHEET 1 I 9 ARG B 22 THR B 26 0
SHEET 2 I 9 MET B 45 ASN B 51 1 O ARG B 49 N CYS B 25
SHEET 3 I 9 ALA B 79 ASP B 83 1 O ALA B 79 N ALA B 48
SHEET 4 I 9 MET B 207 ALA B 210 1 O PHE B 209 N LEU B 82
SHEET 5 I 9 MET B 234 ILE B 239 1 O ILE B 236 N ILE B 208
SHEET 6 I 9 ILE B 258 ALA B 261 1 O MET B 259 N CYS B 237
SHEET 7 I 9 VAL B 292 ALA B 295 1 O ILE B 293 N VAL B 260
SHEET 8 I 9 CYS B 326 LEU B 329 1 O CYS B 326 N CYS B 294
SHEET 9 I 9 ARG B 22 THR B 26 1 N ILE B 24 O LEU B 329
SHEET 1 J 5 VAL B 437 PHE B 441 0
SHEET 2 J 5 ILE B 418 THR B 422 1 N CYS B 420 O VAL B 440
SHEET 3 J 5 ALA B 395 LEU B 399 1 N VAL B 398 O VAL B 421
SHEET 4 J 5 TYR B 475 ALA B 481 1 O ILE B 479 N VAL B 397
SHEET 5 J 5 ASN B 490 LEU B 496 -1 O LEU B 495 N CYS B 476
SHEET 1 K 9 ARG C 22 THR C 26 0
SHEET 2 K 9 MET C 45 ASN C 51 1 O ARG C 49 N CYS C 25
SHEET 3 K 9 ALA C 79 ASP C 83 1 O ASP C 83 N MET C 50
SHEET 4 K 9 MET C 207 ALA C 210 1 O PHE C 209 N LEU C 82
SHEET 5 K 9 MET C 234 ILE C 239 1 O ILE C 236 N ILE C 208
SHEET 6 K 9 GLY C 257 ALA C 261 1 O MET C 259 N CYS C 237
SHEET 7 K 9 VAL C 292 ALA C 295 1 O ILE C 293 N VAL C 260
SHEET 8 K 9 CYS C 326 LEU C 329 1 O CYS C 326 N CYS C 294
SHEET 9 K 9 ARG C 22 THR C 26 1 N ILE C 24 O LEU C 329
SHEET 1 L 5 VAL C 437 PHE C 441 0
SHEET 2 L 5 ILE C 418 THR C 422 1 N CYS C 420 O VAL C 440
SHEET 3 L 5 ALA C 395 LEU C 399 1 N VAL C 398 O VAL C 421
SHEET 4 L 5 TYR C 475 ALA C 481 1 O ILE C 479 N VAL C 397
SHEET 5 L 5 ASN C 490 LEU C 496 -1 O ARG C 493 N VAL C 478
LINK OD1 ASN D 51 K K D 501 1555 1555 3.36
LINK OG SER D 53 K K D 501 1555 1555 3.19
LINK O THR D 84 K K D 501 1555 1555 3.39
LINK OD1 ASP D 264 K K D 502 1555 1555 3.35
LINK OE1 GLU A 240 K K A 501 1555 1555 3.44
LINK O GLN A 354 K K A 502 1555 1555 3.21
LINK O LEU A 357 K K A 502 1555 1555 2.89
LINK OE2 GLU A 359 K K A 502 1555 1555 3.26
LINK OE1 GLU A 359 K K A 502 1555 1555 3.40
LINK K K A 501 O HOH A 595 1555 1555 3.48
LINK K K A 502 O HOH A 663 1555 1555 3.37
LINK O GLN B 354 K K B 503 1555 1555 3.10
LINK O LEU B 357 K K B 503 1555 1555 3.12
LINK OE2 GLU B 359 K K B 503 1555 1555 3.26
LINK OE1 GLU B 359 K K B 503 1555 1555 3.34
LINK K K B 503 O HOH B 575 1555 1555 2.77
LINK OD1 ASN C 51 K K C 500 1555 1555 3.25
LINK OG SER C 53 K K C 500 1555 1555 3.24
LINK OD1 ASP C 83 K K C 500 1555 1555 3.21
LINK O THR C 84 K K C 500 1555 1555 3.17
LINK O GLN C 354 K K C 501 1555 1555 3.09
LINK O LEU C 357 K K C 501 1555 1555 3.07
LINK OE1 GLU C 359 K K C 501 1555 1555 3.14
LINK OE2 GLU C 359 K K C 501 1555 1555 3.24
LINK K K C 500 O HOH C 656 1555 1555 2.94
CISPEP 1 ILE D 372 PRO D 373 0 5.45
CISPEP 2 ILE A 372 PRO A 373 0 3.53
CISPEP 3 GLY A 487 TYR A 488 0 -1.36
CISPEP 4 ILE B 372 PRO B 373 0 4.31
CISPEP 5 ILE C 372 PRO C 373 0 2.56
SITE 1 AC1 6 PRO D 87 GLU D 88 ILE D 89 VAL D 177
SITE 2 AC1 6 ASN D 178 PHE D 212
SITE 1 AC2 7 SER D 400 ASN D 401 THR D 402 ARG D 404
SITE 2 AC2 7 SER D 405 ALA D 481 ASP D 482
SITE 1 AC3 4 ASN D 51 SER D 53 THR D 84 LYS D 238
SITE 1 AC4 1 ASP D 264
SITE 1 AC5 5 HIS D 54 GLY D 55 SER D 56 TYR D 59
SITE 2 AC5 5 LYS D 335
SITE 1 AC6 10 SER A 53 HIS A 54 GLY A 55 LYS A 335
SITE 2 AC6 10 HOH A 655 ARG B 231 ARG B 404 ARG B 407
SITE 3 AC6 10 QV7 B 499 QV8 B 500
SITE 1 AC7 6 SER A 400 ASN A 401 THR A 402 GLY A 403
SITE 2 AC7 6 ARG A 404 SER A 405
SITE 1 AC8 2 GLU A 240 ASP A 264
SITE 1 AC9 3 GLN A 354 LEU A 357 GLU A 359
SITE 1 BC1 16 THR A 26 PRO A 29 ASN A 51 HIS A 54
SITE 2 BC1 16 GLY A 55 SER A 56 TYR A 59 ALA A 334
SITE 3 BC1 16 LYS A 335 QV7 A 499 THR B 402 ARG B 404
SITE 4 BC1 16 ASP B 482 HIS B 483 LYS B 486 HOH B 514
SITE 1 BC2 5 QV7 A 499 ARG B 231 ASP B 232 THR B 402
SITE 2 BC2 5 ARG B 424
SITE 1 BC3 9 SER A 1 SER B 1 TYR B 360 VAL B 361
SITE 2 BC3 9 ASN B 364 QV7 B 504 ASN D 364 LYS D 368
SITE 3 BC3 9 HOH D 507
SITE 1 BC4 4 GLN B 354 LEU B 357 GLU B 359 HOH B 575
SITE 1 BC5 9 SER A 1 TYR A 360 VAL A 361 ASN A 364
SITE 2 BC5 9 SER B 1 QV7 B 501 SER C 1 VAL C 361
SITE 3 BC5 9 LYS C 368
SITE 1 BC6 7 SER C 400 ASN C 401 THR C 402 ARG C 404
SITE 2 BC6 7 SER C 405 ALA C 481 ASP C 482
SITE 1 BC7 6 ASN C 51 SER C 53 ASP C 83 THR C 84
SITE 2 BC7 6 LYS C 238 HOH C 656
SITE 1 BC8 3 GLN C 354 LEU C 357 GLU C 359
CRYST1 182.109 164.798 123.348 90.00 115.80 90.00 C 1 2 1 16
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 0.005491 0.000000 0.002655 0.00000
SCALE2 0.000000 0.006068 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009005 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
