HEADER TRANSFERASE 29-JAN-09 3G15
TITLE CRYSTAL STRUCTURE OF HUMAN CHOLINE KINASE ALPHA IN COMPLEX WITH
TITLE 2 HEMICHOLINIUM-3 AND ADP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHOLINE KINASE ALPHA;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 75-457;
COMPND 5 SYNONYM: CK, CHETK-ALPHA;
COMPND 6 EC: 2.7.1.32;
COMPND 7 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: CHKA, CHK, CKI;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28ALIC
KEYWDS NON-PROTEIN KINASE, CHOLINE KINASE, STRUCTURAL GENOMICS CONSORTIUM,
KEYWDS 2 SGC, HEMICHOLINIUM-3, KINASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.S.HONG,W.TEMPEL,W.M.RABEH,F.MACKENZIE,C.H.ARROWSMITH,A.M.EDWARDS,
AUTHOR 2 C.BOUNTRA,J.WEIGELT,A.BOCHKAREV,H.W.PARK,STRUCTURAL GENOMICS
AUTHOR 3 CONSORTIUM (SGC)
REVDAT 5 06-SEP-23 3G15 1 REMARK
REVDAT 4 21-OCT-20 3G15 1 REMARK SEQADV LINK
REVDAT 3 01-NOV-17 3G15 1 REMARK
REVDAT 2 01-SEP-10 3G15 1 JRNL
REVDAT 1 10-FEB-09 3G15 0
SPRSDE 10-FEB-09 3G15 3F2S
JRNL AUTH B.S.HONG,A.ALLALI-HASSANI,W.TEMPEL,P.J.FINERTY,F.MACKENZIE,
JRNL AUTH 2 S.DIMOV,M.VEDADI,H.W.PARK
JRNL TITL CRYSTAL STRUCTURES OF HUMAN CHOLINE KINASE ISOFORMS IN
JRNL TITL 2 COMPLEX WITH HEMICHOLINIUM-3: SINGLE AMINO ACID NEAR THE
JRNL TITL 3 ACTIVE SITE INFLUENCES INHIBITOR SENSITIVITY.
JRNL REF J.BIOL.CHEM. V. 285 16330 2010
JRNL REFN ISSN 0021-9258
JRNL PMID 20299452
JRNL DOI 10.1074/JBC.M109.039024
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.4.0069
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 3 NUMBER OF REFLECTIONS : 93409
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : THIN SHELLS (SFTOOLS)
REMARK 3 R VALUE (WORKING + TEST SET) : 0.221
REMARK 3 R VALUE (WORKING SET) : 0.220
REMARK 3 FREE R VALUE : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.272
REMARK 3 FREE R VALUE TEST SET COUNT : 2122
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4998
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 70.89
REMARK 3 BIN R VALUE (WORKING SET) : 0.3370
REMARK 3 BIN FREE R VALUE SET COUNT : 0
REMARK 3 BIN FREE R VALUE : 0.2980
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5354
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 149
REMARK 3 SOLVENT ATOMS : 324
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.16
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.52200
REMARK 3 B22 (A**2) : 1.29200
REMARK 3 B33 (A**2) : -0.77000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.112
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.113
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.079
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.363
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.947
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.922
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5670 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 3911 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7696 ; 1.388 ; 1.992
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9476 ; 2.189 ; 3.007
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 669 ; 5.454 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 257 ;32.119 ;23.424
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 961 ;12.758 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 31 ;13.077 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 802 ; 0.083 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6164 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1241 ; 0.002 ; 0.020
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): 3322 ; 2.012 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1327 ; 0.586 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5332 ; 2.992 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2348 ; 2.410 ; 2.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2357 ; 3.479 ; 3.000
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 BULK SOLVENT
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. HEMICHOLINIUM-3 RESTRAINTS WERE PREPARED BY THE
REMARK 3 PRODRG SERVER.
REMARK 4
REMARK 4 3G15 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JAN-09.
REMARK 100 THE DEPOSITION ID IS D_1000051291.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-FEB-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.96863
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 300 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 93657
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.06900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 75.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.60
REMARK 200 R MERGE FOR SHELL (I) : 0.79700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2I7Q
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG-3350, 0.2M LITHIUM SULFATE,
REMARK 280 0.1M HEPES. CRYSTALLIZATION SAMPLE BUFFER: 0.01M TRIS PH 8.0,
REMARK 280 0.5M SODIUM CHLORIDE, 0.005M MAGNESIUM CHLORIDE, 0.01M DTT,
REMARK 280 0.003M HEMICHOLINIUM-3, 0.005M ADP., VAPOR DIFFUSION,
REMARK 280 TEMPERATURE 291K, PH 7.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 27.90100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 65.51950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 59.49300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 65.51950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.90100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 59.49300
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4630 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29920 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -109.0 KCAL/MOL
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 57
REMARK 465 SER A 58
REMARK 465 SER A 59
REMARK 465 HIS A 60
REMARK 465 HIS A 61
REMARK 465 HIS A 62
REMARK 465 HIS A 63
REMARK 465 HIS A 64
REMARK 465 HIS A 65
REMARK 465 SER A 66
REMARK 465 SER A 67
REMARK 465 GLY A 68
REMARK 465 LEU A 69
REMARK 465 VAL A 70
REMARK 465 PRO A 71
REMARK 465 ARG A 72
REMARK 465 GLY A 73
REMARK 465 SER A 74
REMARK 465 PRO A 75
REMARK 465 GLN A 76
REMARK 465 PRO A 77
REMARK 465 PRO A 78
REMARK 465 ALA A 79
REMARK 465 ASP A 80
REMARK 465 ILE A 151
REMARK 465 LEU A 152
REMARK 465 GLN A 153
REMARK 465 MET A 154
REMARK 465 ARG A 155
REMARK 465 SER A 156
REMARK 465 CYS A 157
REMARK 465 ASN A 158
REMARK 465 LYS A 159
REMARK 465 GLU A 160
REMARK 465 GLY A 161
REMARK 465 SER A 162
REMARK 465 GLU A 163
REMARK 465 GLN A 164
REMARK 465 ALA A 165
REMARK 465 GLN A 166
REMARK 465 LYS A 167
REMARK 465 GLU A 168
REMARK 465 ASN A 169
REMARK 465 GLU A 170
REMARK 465 PHE A 171
REMARK 465 GLN A 172
REMARK 465 GLY A 173
REMARK 465 GLY B 57
REMARK 465 SER B 58
REMARK 465 SER B 59
REMARK 465 HIS B 60
REMARK 465 HIS B 61
REMARK 465 HIS B 62
REMARK 465 HIS B 63
REMARK 465 HIS B 64
REMARK 465 HIS B 65
REMARK 465 SER B 66
REMARK 465 SER B 67
REMARK 465 GLY B 68
REMARK 465 LEU B 69
REMARK 465 VAL B 70
REMARK 465 PRO B 71
REMARK 465 ARG B 72
REMARK 465 GLY B 73
REMARK 465 SER B 74
REMARK 465 PRO B 75
REMARK 465 GLN B 76
REMARK 465 PRO B 77
REMARK 465 PRO B 78
REMARK 465 ALA B 79
REMARK 465 ASP B 80
REMARK 465 GLU B 81
REMARK 465 GLN B 82
REMARK 465 PRO B 83
REMARK 465 GLU B 84
REMARK 465 PRO B 85
REMARK 465 ARG B 86
REMARK 465 THR B 87
REMARK 465 GLY B 101
REMARK 465 ARG B 104
REMARK 465 GLY B 105
REMARK 465 LEU B 106
REMARK 465 ARG B 107
REMARK 465 GLU B 108
REMARK 465 ASP B 109
REMARK 465 GLU B 110
REMARK 465 PHE B 111
REMARK 465 HIS B 112
REMARK 465 ILE B 113
REMARK 465 SER B 114
REMARK 465 VAL B 115
REMARK 465 ILE B 116
REMARK 465 ARG B 117
REMARK 465 GLY B 118
REMARK 465 GLY B 119
REMARK 465 LEU B 120
REMARK 465 SER B 121
REMARK 465 ASN B 122
REMARK 465 SER B 128
REMARK 465 LEU B 129
REMARK 465 PRO B 130
REMARK 465 ASP B 131
REMARK 465 THR B 132
REMARK 465 THR B 133
REMARK 465 ALA B 134
REMARK 465 THR B 135
REMARK 465 LEU B 136
REMARK 465 GLY B 137
REMARK 465 ASP B 138
REMARK 465 GLU B 139
REMARK 465 PRO B 140
REMARK 465 ARG B 141
REMARK 465 LYS B 142
REMARK 465 TYR B 148
REMARK 465 GLY B 149
REMARK 465 ALA B 150
REMARK 465 ILE B 151
REMARK 465 LEU B 152
REMARK 465 GLN B 153
REMARK 465 MET B 154
REMARK 465 ARG B 155
REMARK 465 SER B 156
REMARK 465 CYS B 157
REMARK 465 ASN B 158
REMARK 465 LYS B 159
REMARK 465 GLU B 160
REMARK 465 GLY B 161
REMARK 465 SER B 162
REMARK 465 GLU B 163
REMARK 465 GLN B 164
REMARK 465 ALA B 165
REMARK 465 GLN B 166
REMARK 465 LYS B 167
REMARK 465 GLU B 168
REMARK 465 ASN B 169
REMARK 465 GLU B 170
REMARK 465 PHE B 171
REMARK 465 GLN B 172
REMARK 465 GLY B 173
REMARK 465 ALA B 174
REMARK 465 GLU B 175
REMARK 465 ALA B 176
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 A 81 CG CD OE1 OE2
REMARK 470 ARG A 89 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 90 NE CZ NH1 NH2
REMARK 470 LYS A 142 CG CD CE NZ
REMARK 470 GLU A 175 CG CD OE1 OE2
REMARK 470 LYS A 195 CD CE NZ
REMARK 470 ARG A 213 NE CZ NH1 NH2
REMARK 470 GLU A 217 CG CD OE1 OE2
REMARK 470 GLU A 230 CD OE1 OE2
REMARK 470 LYS A 239 CD CE NZ
REMARK 470 LYS A 255 CD CE NZ
REMARK 470 LYS A 258 CG CD CE NZ
REMARK 470 GLU A 259 CG CD OE1 OE2
REMARK 470 ARG A 262 NE CZ NH1 NH2
REMARK 470 LYS A 272 CG CD CE NZ
REMARK 470 GLU A 294 CG CD OE1 OE2
REMARK 470 ASN A 320 CG OD1 ND2
REMARK 470 GLU A 357 CD OE1 OE2
REMARK 470 LYS A 358 CG CD CE NZ
REMARK 470 ARG A 363 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 388 CG OD1 ND2
REMARK 470 GLU A 391 CG CD OE1 OE2
REMARK 470 GLU A 403 CG CD OE1 OE2
REMARK 470 ARG B 88 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 89 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 90 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 96 CG CD CE NZ
REMARK 470 LEU B 147 CG CD1 CD2
REMARK 470 GLU B 180 CD OE1 OE2
REMARK 470 LYS B 195 CE NZ
REMARK 470 ARG B 213 NE CZ NH1 NH2
REMARK 470 LYS B 264 CD CE NZ
REMARK 470 GLU B 268 CD OE1 OE2
REMARK 470 LYS B 272 CD CE NZ
REMARK 470 GLU B 322 CG CD OE1 OE2
REMARK 470 GLU B 357 CD OE1 OE2
REMARK 470 LYS B 358 CE NZ
REMARK 470 ARG B 367 NE CZ NH1 NH2
REMARK 470 LYS B 368 CD CE NZ
REMARK 470 LYS B 373 CE NZ
REMARK 470 ASN B 388 CG OD1 ND2
REMARK 470 GLU B 397 CG CD OE1 OE2
REMARK 470 LYS B 454 CE NZ
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 CD2 LEU B 192 CE MET B 238 1.98
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 SER A 211 170.31 178.24
REMARK 500 PRO A 241 44.17 -80.49
REMARK 500 ASN A 281 76.67 54.02
REMARK 500 ASN A 305 -1.50 79.18
REMARK 500 ASP A 306 47.74 -155.21
REMARK 500 ASP A 330 77.39 70.17
REMARK 500 SER B 211 173.38 179.30
REMARK 500 PRO B 241 45.35 -83.76
REMARK 500 ASP B 306 47.75 -157.91
REMARK 500 GLN B 324 57.92 -140.57
REMARK 500 ASP B 330 82.51 66.48
REMARK 500 PHE B 435 145.68 -172.43
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 MG A 605 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 39 O
REMARK 620 2 ASP A 330 OD1 68.7
REMARK 620 3 ASP A 330 OD2 66.4 52.5
REMARK 620 4 GLU A 332 OE2 105.1 152.0 99.7
REMARK 620 5 ADP A 601 O1B 149.5 84.9 85.7 91.0
REMARK 620 6 SO4 A 604 O4 88.5 92.7 141.9 114.8 108.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 602 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 49 O
REMARK 620 2 ASN A 311 OD1 84.7
REMARK 620 3 ASP A 330 OD1 173.3 88.6
REMARK 620 4 ADP A 601 O2B 89.6 174.3 97.1
REMARK 620 5 ADP A 601 O2A 89.0 89.7 90.9 89.9
REMARK 620 6 SO4 A 604 O2 91.8 88.7 88.1 91.8 178.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 605 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 1 O
REMARK 620 2 ASP B 330 OD2 76.8
REMARK 620 3 ASP B 330 OD1 69.6 55.2
REMARK 620 4 GLU B 332 OE2 100.4 163.9 108.8
REMARK 620 5 ADP B 601 O3B 158.3 84.0 91.1 95.2
REMARK 620 6 SO4 B 604 O3 87.0 91.1 141.9 104.7 103.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 602 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 2 O
REMARK 620 2 ASN B 311 OD1 87.1
REMARK 620 3 ASP B 330 OD2 174.8 87.9
REMARK 620 4 ADP B 601 O1B 91.0 173.3 94.1
REMARK 620 5 ADP B 601 O2A 88.5 89.4 92.7 84.1
REMARK 620 6 SO4 B 604 O2 87.6 93.5 91.5 92.8 174.9
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HC6 A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 12
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 13
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 14
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 16
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 17
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 19
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 20
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HC6 B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX B 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX B 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX B 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX B 7
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX B 8
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX B 9
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX B 10
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX B 15
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX B 18
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3F2S RELATED DB: PDB
REMARK 900 SUPERSEDES PDB ENTRY 3F2S.
DBREF 3G15 A 75 457 UNP P35790 CHKA_HUMAN 75 457
DBREF 3G15 B 75 457 UNP P35790 CHKA_HUMAN 75 457
SEQADV 3G15 GLY A 57 UNP P35790 EXPRESSION TAG
SEQADV 3G15 SER A 58 UNP P35790 EXPRESSION TAG
SEQADV 3G15 SER A 59 UNP P35790 EXPRESSION TAG
SEQADV 3G15 HIS A 60 UNP P35790 EXPRESSION TAG
SEQADV 3G15 HIS A 61 UNP P35790 EXPRESSION TAG
SEQADV 3G15 HIS A 62 UNP P35790 EXPRESSION TAG
SEQADV 3G15 HIS A 63 UNP P35790 EXPRESSION TAG
SEQADV 3G15 HIS A 64 UNP P35790 EXPRESSION TAG
SEQADV 3G15 HIS A 65 UNP P35790 EXPRESSION TAG
SEQADV 3G15 SER A 66 UNP P35790 EXPRESSION TAG
SEQADV 3G15 SER A 67 UNP P35790 EXPRESSION TAG
SEQADV 3G15 GLY A 68 UNP P35790 EXPRESSION TAG
SEQADV 3G15 LEU A 69 UNP P35790 EXPRESSION TAG
SEQADV 3G15 VAL A 70 UNP P35790 EXPRESSION TAG
SEQADV 3G15 PRO A 71 UNP P35790 EXPRESSION TAG
SEQADV 3G15 ARG A 72 UNP P35790 EXPRESSION TAG
SEQADV 3G15 GLY A 73 UNP P35790 EXPRESSION TAG
SEQADV 3G15 SER A 74 UNP P35790 EXPRESSION TAG
SEQADV 3G15 MET A 154 UNP P35790 VAL 154 VARIANT
SEQADV 3G15 SER A 220 UNP P35790 GLY 220 VARIANT
SEQADV 3G15 LEU A 422 UNP P35790 GLN 422 VARIANT
SEQADV 3G15 GLY B 57 UNP P35790 EXPRESSION TAG
SEQADV 3G15 SER B 58 UNP P35790 EXPRESSION TAG
SEQADV 3G15 SER B 59 UNP P35790 EXPRESSION TAG
SEQADV 3G15 HIS B 60 UNP P35790 EXPRESSION TAG
SEQADV 3G15 HIS B 61 UNP P35790 EXPRESSION TAG
SEQADV 3G15 HIS B 62 UNP P35790 EXPRESSION TAG
SEQADV 3G15 HIS B 63 UNP P35790 EXPRESSION TAG
SEQADV 3G15 HIS B 64 UNP P35790 EXPRESSION TAG
SEQADV 3G15 HIS B 65 UNP P35790 EXPRESSION TAG
SEQADV 3G15 SER B 66 UNP P35790 EXPRESSION TAG
SEQADV 3G15 SER B 67 UNP P35790 EXPRESSION TAG
SEQADV 3G15 GLY B 68 UNP P35790 EXPRESSION TAG
SEQADV 3G15 LEU B 69 UNP P35790 EXPRESSION TAG
SEQADV 3G15 VAL B 70 UNP P35790 EXPRESSION TAG
SEQADV 3G15 PRO B 71 UNP P35790 EXPRESSION TAG
SEQADV 3G15 ARG B 72 UNP P35790 EXPRESSION TAG
SEQADV 3G15 GLY B 73 UNP P35790 EXPRESSION TAG
SEQADV 3G15 SER B 74 UNP P35790 EXPRESSION TAG
SEQADV 3G15 MET B 154 UNP P35790 VAL 154 VARIANT
SEQADV 3G15 SER B 220 UNP P35790 GLY 220 VARIANT
SEQADV 3G15 LEU B 422 UNP P35790 GLN 422 VARIANT
SEQRES 1 A 401 GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU
SEQRES 2 A 401 VAL PRO ARG GLY SER PRO GLN PRO PRO ALA ASP GLU GLN
SEQRES 3 A 401 PRO GLU PRO ARG THR ARG ARG ARG ALA TYR LEU TRP CYS
SEQRES 4 A 401 LYS GLU PHE LEU PRO GLY ALA TRP ARG GLY LEU ARG GLU
SEQRES 5 A 401 ASP GLU PHE HIS ILE SER VAL ILE ARG GLY GLY LEU SER
SEQRES 6 A 401 ASN MET LEU PHE GLN CYS SER LEU PRO ASP THR THR ALA
SEQRES 7 A 401 THR LEU GLY ASP GLU PRO ARG LYS VAL LEU LEU ARG LEU
SEQRES 8 A 401 TYR GLY ALA ILE LEU GLN MET ARG SER CYS ASN LYS GLU
SEQRES 9 A 401 GLY SER GLU GLN ALA GLN LYS GLU ASN GLU PHE GLN GLY
SEQRES 10 A 401 ALA GLU ALA MET VAL LEU GLU SER VAL MET PHE ALA ILE
SEQRES 11 A 401 LEU ALA GLU ARG SER LEU GLY PRO LYS LEU TYR GLY ILE
SEQRES 12 A 401 PHE PRO GLN GLY ARG LEU GLU GLN PHE ILE PRO SER ARG
SEQRES 13 A 401 ARG LEU ASP THR GLU GLU LEU SER LEU PRO ASP ILE SER
SEQRES 14 A 401 ALA GLU ILE ALA GLU LYS MET ALA THR PHE HIS GLY MET
SEQRES 15 A 401 LYS MET PRO PHE ASN LYS GLU PRO LYS TRP LEU PHE GLY
SEQRES 16 A 401 THR MET GLU LYS TYR LEU LYS GLU VAL LEU ARG ILE LYS
SEQRES 17 A 401 PHE THR GLU GLU SER ARG ILE LYS LYS LEU HIS LYS LEU
SEQRES 18 A 401 LEU SER TYR ASN LEU PRO LEU GLU LEU GLU ASN LEU ARG
SEQRES 19 A 401 SER LEU LEU GLU SER THR PRO SER PRO VAL VAL PHE CYS
SEQRES 20 A 401 HIS ASN ASP CYS GLN GLU GLY ASN ILE LEU LEU LEU GLU
SEQRES 21 A 401 GLY ARG GLU ASN SER GLU LYS GLN LYS LEU MET LEU ILE
SEQRES 22 A 401 ASP PHE GLU TYR SER SER TYR ASN TYR ARG GLY PHE ASP
SEQRES 23 A 401 ILE GLY ASN HIS PHE CYS GLU TRP MET TYR ASP TYR SER
SEQRES 24 A 401 TYR GLU LYS TYR PRO PHE PHE ARG ALA ASN ILE ARG LYS
SEQRES 25 A 401 TYR PRO THR LYS LYS GLN GLN LEU HIS PHE ILE SER SER
SEQRES 26 A 401 TYR LEU PRO ALA PHE GLN ASN ASP PHE GLU ASN LEU SER
SEQRES 27 A 401 THR GLU GLU LYS SER ILE ILE LYS GLU GLU MET LEU LEU
SEQRES 28 A 401 GLU VAL ASN ARG PHE ALA LEU ALA SER HIS PHE LEU TRP
SEQRES 29 A 401 GLY LEU TRP SER ILE VAL GLN ALA LYS ILE SER SER ILE
SEQRES 30 A 401 GLU PHE GLY TYR MET ASP TYR ALA GLN ALA ARG PHE ASP
SEQRES 31 A 401 ALA TYR PHE HIS GLN LYS ARG LYS LEU GLY VAL
SEQRES 1 B 401 GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU
SEQRES 2 B 401 VAL PRO ARG GLY SER PRO GLN PRO PRO ALA ASP GLU GLN
SEQRES 3 B 401 PRO GLU PRO ARG THR ARG ARG ARG ALA TYR LEU TRP CYS
SEQRES 4 B 401 LYS GLU PHE LEU PRO GLY ALA TRP ARG GLY LEU ARG GLU
SEQRES 5 B 401 ASP GLU PHE HIS ILE SER VAL ILE ARG GLY GLY LEU SER
SEQRES 6 B 401 ASN MET LEU PHE GLN CYS SER LEU PRO ASP THR THR ALA
SEQRES 7 B 401 THR LEU GLY ASP GLU PRO ARG LYS VAL LEU LEU ARG LEU
SEQRES 8 B 401 TYR GLY ALA ILE LEU GLN MET ARG SER CYS ASN LYS GLU
SEQRES 9 B 401 GLY SER GLU GLN ALA GLN LYS GLU ASN GLU PHE GLN GLY
SEQRES 10 B 401 ALA GLU ALA MET VAL LEU GLU SER VAL MET PHE ALA ILE
SEQRES 11 B 401 LEU ALA GLU ARG SER LEU GLY PRO LYS LEU TYR GLY ILE
SEQRES 12 B 401 PHE PRO GLN GLY ARG LEU GLU GLN PHE ILE PRO SER ARG
SEQRES 13 B 401 ARG LEU ASP THR GLU GLU LEU SER LEU PRO ASP ILE SER
SEQRES 14 B 401 ALA GLU ILE ALA GLU LYS MET ALA THR PHE HIS GLY MET
SEQRES 15 B 401 LYS MET PRO PHE ASN LYS GLU PRO LYS TRP LEU PHE GLY
SEQRES 16 B 401 THR MET GLU LYS TYR LEU LYS GLU VAL LEU ARG ILE LYS
SEQRES 17 B 401 PHE THR GLU GLU SER ARG ILE LYS LYS LEU HIS LYS LEU
SEQRES 18 B 401 LEU SER TYR ASN LEU PRO LEU GLU LEU GLU ASN LEU ARG
SEQRES 19 B 401 SER LEU LEU GLU SER THR PRO SER PRO VAL VAL PHE CYS
SEQRES 20 B 401 HIS ASN ASP CYS GLN GLU GLY ASN ILE LEU LEU LEU GLU
SEQRES 21 B 401 GLY ARG GLU ASN SER GLU LYS GLN LYS LEU MET LEU ILE
SEQRES 22 B 401 ASP PHE GLU TYR SER SER TYR ASN TYR ARG GLY PHE ASP
SEQRES 23 B 401 ILE GLY ASN HIS PHE CYS GLU TRP MET TYR ASP TYR SER
SEQRES 24 B 401 TYR GLU LYS TYR PRO PHE PHE ARG ALA ASN ILE ARG LYS
SEQRES 25 B 401 TYR PRO THR LYS LYS GLN GLN LEU HIS PHE ILE SER SER
SEQRES 26 B 401 TYR LEU PRO ALA PHE GLN ASN ASP PHE GLU ASN LEU SER
SEQRES 27 B 401 THR GLU GLU LYS SER ILE ILE LYS GLU GLU MET LEU LEU
SEQRES 28 B 401 GLU VAL ASN ARG PHE ALA LEU ALA SER HIS PHE LEU TRP
SEQRES 29 B 401 GLY LEU TRP SER ILE VAL GLN ALA LYS ILE SER SER ILE
SEQRES 30 B 401 GLU PHE GLY TYR MET ASP TYR ALA GLN ALA ARG PHE ASP
SEQRES 31 B 401 ALA TYR PHE HIS GLN LYS ARG LYS LEU GLY VAL
HET ADP A 601 27
HET MG A 602 1
HET HC6 A 603 30
HET SO4 A 604 5
HET MG A 605 1
HET UNX A 606 1
HET UNX A 1 1
HET UNX A 2 1
HET UNX A 3 1
HET UNX A 4 1
HET UNX A 12 1
HET UNX A 13 1
HET UNX A 14 1
HET UNX A 16 1
HET UNX A 17 1
HET UNX A 19 1
HET UNX A 20 1
HET ADP B 601 27
HET MG B 602 1
HET HC6 B 603 30
HET SO4 B 604 5
HET MG B 605 1
HET UNX B 606 1
HET UNX B 5 1
HET UNX B 6 1
HET UNX B 7 1
HET UNX B 8 1
HET UNX B 9 1
HET UNX B 10 1
HET UNX B 15 1
HET UNX B 18 1
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM MG MAGNESIUM ION
HETNAM HC6 (2S,2'S)-2,2'-BIPHENYL-4,4'-DIYLBIS(2-HYDROXY-4,4-
HETNAM 2 HC6 DIMETHYLMORPHOLIN-4-IUM)
HETNAM SO4 SULFATE ION
HETNAM UNX UNKNOWN ATOM OR ION
FORMUL 3 ADP 2(C10 H15 N5 O10 P2)
FORMUL 4 MG 4(MG 2+)
FORMUL 5 HC6 2(C24 H34 N2 O4 2+)
FORMUL 6 SO4 2(O4 S 2-)
FORMUL 8 UNX 21(X)
FORMUL 34 HOH *324(H2 O)
HELIX 1 1 GLU A 84 LEU A 99 1 16
HELIX 2 2 PRO A 100 ARG A 104 5 5
HELIX 3 3 ARG A 107 PHE A 111 5 5
HELIX 4 4 ALA A 174 ARG A 190 1 17
HELIX 5 5 ASP A 215 SER A 220 5 6
HELIX 6 6 LEU A 221 GLY A 237 1 17
HELIX 7 7 LYS A 247 ILE A 263 1 17
HELIX 8 8 GLU A 267 SER A 279 1 13
HELIX 9 9 ASN A 281 SER A 295 1 15
HELIX 10 10 GLN A 308 GLY A 310 5 3
HELIX 11 11 GLY A 317 SER A 321 5 5
HELIX 12 12 ARG A 339 TRP A 350 1 12
HELIX 13 13 ILE A 366 TYR A 369 5 4
HELIX 14 14 THR A 371 GLN A 387 1 17
HELIX 15 15 ASN A 388 LEU A 393 5 6
HELIX 16 16 SER A 394 SER A 431 1 38
HELIX 17 17 GLY A 436 VAL A 457 1 22
HELIX 18 18 ARG B 88 LEU B 99 1 12
HELIX 19 19 MET B 177 ARG B 190 1 14
HELIX 20 20 ASP B 215 SER B 220 5 6
HELIX 21 21 LEU B 221 GLY B 237 1 17
HELIX 22 22 LYS B 247 LEU B 261 1 15
HELIX 23 23 GLU B 267 SER B 279 1 13
HELIX 24 24 ASN B 281 SER B 295 1 15
HELIX 25 25 GLN B 308 GLY B 310 5 3
HELIX 26 26 ARG B 339 TRP B 350 1 12
HELIX 27 27 ILE B 366 TYR B 369 5 4
HELIX 28 28 THR B 371 GLN B 387 1 17
HELIX 29 29 ASP B 389 LEU B 393 5 5
HELIX 30 30 SER B 394 SER B 431 1 38
HELIX 31 31 GLY B 436 GLY B 456 1 21
SHEET 1 A 5 HIS A 112 ARG A 117 0
SHEET 2 A 5 SER A 121 SER A 128 -1 O LEU A 124 N ILE A 116
SHEET 3 A 5 LYS A 142 GLY A 149 -1 O LEU A 145 N PHE A 125
SHEET 4 A 5 GLY A 203 GLN A 207 -1 O GLU A 206 N LEU A 144
SHEET 5 A 5 LEU A 196 PHE A 200 -1 N TYR A 197 O LEU A 205
SHEET 1 B 3 SER A 211 ARG A 213 0
SHEET 2 B 3 ILE A 312 LEU A 315 -1 O LEU A 314 N ARG A 212
SHEET 3 B 3 LEU A 326 LEU A 328 -1 O MET A 327 N LEU A 313
SHEET 1 C 2 VAL A 300 CYS A 303 0
SHEET 2 C 2 SER A 335 TYR A 338 -1 O SER A 335 N CYS A 303
SHEET 1 D 2 TYR A 352 ASP A 353 0
SHEET 2 D 2 ARG A 363 ALA A 364 -1 O ARG A 363 N ASP A 353
SHEET 1 E 4 LEU B 124 PHE B 125 0
SHEET 2 E 4 LEU B 144 ARG B 146 -1 O LEU B 145 N PHE B 125
SHEET 3 E 4 GLY B 203 GLU B 206 -1 O GLU B 206 N LEU B 144
SHEET 4 E 4 LEU B 196 PHE B 200 -1 N TYR B 197 O LEU B 205
SHEET 1 F 3 SER B 211 ARG B 213 0
SHEET 2 F 3 ILE B 312 LEU B 315 -1 O LEU B 314 N ARG B 212
SHEET 3 F 3 LEU B 326 LEU B 328 -1 O MET B 327 N LEU B 313
SHEET 1 G 2 VAL B 300 CYS B 303 0
SHEET 2 G 2 SER B 335 TYR B 338 -1 O ASN B 337 N VAL B 301
SHEET 1 H 2 TYR B 352 ASP B 353 0
SHEET 2 H 2 ARG B 363 ALA B 364 -1 O ARG B 363 N ASP B 353
LINK O HOH A 39 MG MG A 605 1555 1555 2.57
LINK O HOH A 49 MG MG A 602 1555 1555 2.15
LINK OD1 ASN A 311 MG MG A 602 1555 1555 2.09
LINK OD1 ASP A 330 MG MG A 602 1555 1555 2.11
LINK OD1 ASP A 330 MG MG A 605 1555 1555 2.24
LINK OD2 ASP A 330 MG MG A 605 1555 1555 2.68
LINK OE2 GLU A 332 MG MG A 605 1555 1555 1.74
LINK O2B ADP A 601 MG MG A 602 1555 1555 2.05
LINK O2A ADP A 601 MG MG A 602 1555 1555 2.06
LINK O1B ADP A 601 MG MG A 605 1555 1555 2.11
LINK MG MG A 602 O2 SO4 A 604 1555 1555 2.10
LINK O4 SO4 A 604 MG MG A 605 1555 1555 1.76
LINK O HOH B 1 MG MG B 605 1555 1555 2.23
LINK O HOH B 2 MG MG B 602 1555 1555 2.16
LINK OD1 ASN B 311 MG MG B 602 1555 1555 2.16
LINK OD2 ASP B 330 MG MG B 602 1555 1555 2.15
LINK OD2 ASP B 330 MG MG B 605 1555 1555 2.22
LINK OD1 ASP B 330 MG MG B 605 1555 1555 2.52
LINK OE2 GLU B 332 MG MG B 605 1555 1555 1.84
LINK O1B ADP B 601 MG MG B 602 1555 1555 2.07
LINK O2A ADP B 601 MG MG B 602 1555 1555 2.06
LINK O3B ADP B 601 MG MG B 605 1555 1555 2.14
LINK MG MG B 602 O2 SO4 B 604 1555 1555 2.21
LINK O3 SO4 B 604 MG MG B 605 1555 1555 2.28
CISPEP 1 TYR A 359 PRO A 360 0 6.06
CISPEP 2 TYR B 359 PRO B 360 0 8.86
SITE 1 AC1 18 HOH A 49 ARG A 117 LEU A 124 LEU A 144
SITE 2 AC1 18 ARG A 146 PRO A 194 GLN A 207 ILE A 209
SITE 3 AC1 18 ARG A 213 GLY A 310 ASN A 311 ILE A 329
SITE 4 AC1 18 ASP A 330 GLU A 332 HOH A 490 MG A 602
SITE 5 AC1 18 SO4 A 604 MG A 605
SITE 1 AC2 6 HOH A 49 ASN A 311 ASP A 330 ADP A 601
SITE 2 AC2 6 SO4 A 604 MG A 605
SITE 1 AC3 13 UNX A 2 ASP A 306 GLN A 308 TYR A 333
SITE 2 AC3 13 TYR A 354 PHE A 361 TRP A 420 TRP A 423
SITE 3 AC3 13 ILE A 433 GLU A 434 PHE A 435 TYR A 440
SITE 4 AC3 13 SO4 A 604
SITE 1 AC4 12 HOH A 39 HOH A 49 HOH A 50 ASP A 306
SITE 2 AC4 12 GLN A 308 ASN A 311 ASP A 330 GLU A 332
SITE 3 AC4 12 ADP A 601 MG A 602 HC6 A 603 MG A 605
SITE 1 AC5 6 HOH A 39 ASP A 330 GLU A 332 ADP A 601
SITE 2 AC5 6 MG A 602 SO4 A 604
SITE 1 AC6 3 GLU A 309 GLU A 349 TYR A 352
SITE 1 AC7 3 PRO A 85 ARG A 86 ASN B 365
SITE 1 AC8 4 TYR A 354 TYR A 356 PHE A 361 HC6 A 603
SITE 1 AC9 3 UNX A 4 TYR A 437 MET A 438
SITE 1 BC1 7 UNX A 3 LYS A 273 TYR A 359 GLY A 436
SITE 2 BC1 7 TYR A 437 MET A 438 ASP A 439
SITE 1 BC2 5 TYR A 148 MET A 177 ILE A 199 PHE A 200
SITE 2 BC2 5 GLY A 203
SITE 1 BC3 7 HIS A 304 ASP A 306 ASP A 330 PHE A 331
SITE 2 BC3 7 GLU A 332 TYR A 333 SER A 334
SITE 1 BC4 3 PRO A 83 GLU A 84 THR A 87
SITE 1 BC5 4 PHE A 184 ALA A 188 GLY A 193 PRO A 194
SITE 1 BC6 4 ASP A 215 THR A 216 GLU A 217 HOH A 532
SITE 1 BC7 2 LEU A 455 HOH A 471
SITE 1 BC8 1 ARG A 104
SITE 1 BC9 19 HOH B 2 LEU B 124 LEU B 144 ARG B 146
SITE 2 BC9 19 PRO B 194 GLN B 207 PHE B 208 ILE B 209
SITE 3 BC9 19 GLY B 310 ASN B 311 ILE B 329 ASP B 330
SITE 4 BC9 19 GLU B 332 HOH B 488 HOH B 501 HOH B 557
SITE 5 BC9 19 MG B 602 SO4 B 604 MG B 605
SITE 1 CC1 5 HOH B 2 ASN B 311 ASP B 330 ADP B 601
SITE 2 CC1 5 SO4 B 604
SITE 1 CC2 11 ASP B 306 TYR B 333 TYR B 354 PHE B 361
SITE 2 CC2 11 TRP B 420 TRP B 423 ILE B 433 GLU B 434
SITE 3 CC2 11 PHE B 435 TYR B 440 SO4 B 604
SITE 1 CC3 11 HOH B 2 ASP B 306 GLN B 308 ASN B 311
SITE 2 CC3 11 ASP B 330 GLU B 332 HOH B 549 ADP B 601
SITE 3 CC3 11 MG B 602 HC6 B 603 MG B 605
SITE 1 CC4 5 HOH B 1 ASP B 330 GLU B 332 ADP B 601
SITE 2 CC4 5 SO4 B 604
SITE 1 CC5 3 GLU B 309 GLU B 349 TYR B 352
SITE 1 CC6 2 ARG B 212 ARG B 213
SITE 1 CC7 2 PRO B 222 ASP B 223
SITE 1 CC8 4 PHE B 265 THR B 266 GLU B 267 ARG B 270
SITE 1 CC9 2 PHE B 265 ILE B 271
SITE 1 DC1 3 ARG B 270 TYR B 437 MET B 438
SITE 1 DC2 3 ARG A 86 THR A 87 ASN B 365
SITE 1 DC3 2 PRO B 246 PHE B 250
SITE 1 DC4 2 TYR B 356 GLU B 357
CRYST1 55.802 118.986 131.039 90.00 90.00 90.00 P 21 21 21 8
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 0.017921 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008404 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007631 0.00000
(ATOM LINES ARE NOT SHOWN.)
END