HEADER APOPTOSIS/APOPTOSIS REGULATOR 11-NOV-10 3PK1
TITLE CRYSTAL STRUCTURE OF MCL-1 IN COMPLEX WITH THE BAXBH3 DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INDUCED MYELOID LEUKEMIA CELL DIFFERENTIATION PROTEIN MCL-
COMPND 3 1;
COMPND 4 CHAIN: A, C;
COMPND 5 FRAGMENT: MCL-1 BCL-2 LIKE REGION, UNP RESIDUES 174-326;
COMPND 6 SYNONYM: BCL-2-LIKE PROTEIN 3, BCL2-L-3, BCL-2-RELATED PROTEIN
COMPND 7 EAT/MCL1, MCL1/EAT;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: APOPTOSIS REGULATOR BAX;
COMPND 11 CHAIN: B, D;
COMPND 12 FRAGMENT: BH3 DOMAIN, UNP RESIDUES 48-81;
COMPND 13 SYNONYM: BCL-2-LIKE PROTEIN 4, BCL2-L-4;
COMPND 14 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: MCL1, BCL2L3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 OTHER_DETAILS: SYNTHESIZED PEPTIDE
KEYWDS BCL-2 FAMILY FOLD, REGULATION OF APOPTOSIS, BAX, MITOCHONDRIA,
KEYWDS 2 APOPTOSIS-APOPTOSIS REGULATOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR P.E.CZABOTAR,P.M.COLMAN
REVDAT 3 01-NOV-23 3PK1 1 REMARK SEQADV
REVDAT 2 22-JAN-14 3PK1 1 JRNL VERSN
REVDAT 1 29-DEC-10 3PK1 0
JRNL AUTH P.E.CZABOTAR,E.F.LEE,G.V.THOMPSON,A.Z.WARDAK,W.D.FAIRLIE,
JRNL AUTH 2 P.M.COLMAN
JRNL TITL MUTATION TO BAX BEYOND THE BH3 DOMAIN DISRUPTS INTERACTIONS
JRNL TITL 2 WITH PRO-SURVIVAL PROTEINS AND PROMOTES APOPTOSIS
JRNL REF J.BIOL.CHEM. V. 286 7123 2011
JRNL REFN ISSN 0021-9258
JRNL PMID 21199865
JRNL DOI 10.1074/JBC.M110.161281
REMARK 2
REMARK 2 RESOLUTION. 2.49 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.4_486)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : TWIN_LSQ_F
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.49
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.14
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 13062
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.214
REMARK 3 R VALUE (WORKING SET) : 0.212
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.140
REMARK 3 FREE R VALUE TEST SET COUNT : 671
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 18.6250 - 3.9411 0.94 3168 183 0.1710 0.2054
REMARK 3 2 3.9411 - 3.1330 0.95 3127 168 0.2086 0.2298
REMARK 3 3 3.1330 - 2.7384 0.95 3137 149 0.2776 0.3379
REMARK 3 4 2.7384 - 2.4887 0.90 2959 152 0.3134 0.3583
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.35
REMARK 3 B_SOL : 61.21
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 42.400
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) : 9.54450
REMARK 3 B22 (A**2) : -11.03880
REMARK 3 B33 (A**2) : 1.49430
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 23.77260
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: 0.1540
REMARK 3 OPERATOR: H+2*L,-K,-L
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 2707
REMARK 3 ANGLE : 1.101 3627
REMARK 3 CHIRALITY : 0.067 413
REMARK 3 PLANARITY : 0.003 457
REMARK 3 DIHEDRAL : 16.400 1027
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A
REMARK 3 ORIGIN FOR THE GROUP (A): 17.2162 -45.8321 -2.5905
REMARK 3 T TENSOR
REMARK 3 T11: 0.3547 T22: 0.3451
REMARK 3 T33: 0.4216 T12: 0.0314
REMARK 3 T13: -0.0030 T23: -0.0047
REMARK 3 L TENSOR
REMARK 3 L11: -0.2368 L22: 1.0978
REMARK 3 L33: 1.3952 L12: 0.0926
REMARK 3 L13: -0.1744 L23: 0.2443
REMARK 3 S TENSOR
REMARK 3 S11: 0.0125 S12: -0.1189 S13: -0.0180
REMARK 3 S21: -0.0857 S22: -0.1744 S23: 0.1829
REMARK 3 S31: -0.0898 S32: -0.0086 S33: 0.0000
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): 22.6665 -52.5093 9.2911
REMARK 3 T TENSOR
REMARK 3 T11: 0.3402 T22: 0.3886
REMARK 3 T33: 0.3130 T12: -0.0006
REMARK 3 T13: 0.0275 T23: -0.0026
REMARK 3 L TENSOR
REMARK 3 L11: 0.0689 L22: 0.0135
REMARK 3 L33: 0.2637 L12: -0.0199
REMARK 3 L13: 0.2031 L23: -0.1305
REMARK 3 S TENSOR
REMARK 3 S11: 0.1193 S12: 0.0040 S13: -0.2361
REMARK 3 S21: 0.2739 S22: -0.0961 S23: -0.5032
REMARK 3 S31: 0.2869 S32: -0.0557 S33: 0.0002
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN C
REMARK 3 ORIGIN FOR THE GROUP (A): 3.3922 -21.8898 18.5031
REMARK 3 T TENSOR
REMARK 3 T11: 0.3644 T22: 0.3655
REMARK 3 T33: 0.3590 T12: 0.0173
REMARK 3 T13: -0.0289 T23: -0.0244
REMARK 3 L TENSOR
REMARK 3 L11: 0.7281 L22: 0.9404
REMARK 3 L33: 0.4539 L12: 0.0888
REMARK 3 L13: -1.2564 L23: 0.6271
REMARK 3 S TENSOR
REMARK 3 S11: 0.1233 S12: 0.1068 S13: -0.1156
REMARK 3 S21: 0.0480 S22: -0.0937 S23: 0.2441
REMARK 3 S31: -0.1697 S32: -0.0060 S33: 0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN D
REMARK 3 ORIGIN FOR THE GROUP (A): 16.4056 -15.3738 18.9866
REMARK 3 T TENSOR
REMARK 3 T11: 0.4078 T22: 0.3949
REMARK 3 T33: 0.3910 T12: -0.0252
REMARK 3 T13: 0.0205 T23: -0.0272
REMARK 3 L TENSOR
REMARK 3 L11: 0.1743 L22: 0.0172
REMARK 3 L33: 0.0659 L12: -0.0986
REMARK 3 L13: -0.1684 L23: -0.0613
REMARK 3 S TENSOR
REMARK 3 S11: -0.1682 S12: 0.1755 S13: -0.0123
REMARK 3 S21: 0.6728 S22: 0.0438 S23: -0.1774
REMARK 3 S31: -0.1453 S32: -0.1747 S33: -0.0000
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 2
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 173:192 OR RESSEQ
REMARK 3 205:321 )
REMARK 3 SELECTION : CHAIN C AND (RESSEQ 173:192 OR RESSEQ
REMARK 3 205:321 )
REMARK 3 ATOM PAIRS NUMBER : 1114
REMARK 3 RMSD : 0.061
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN B AND (RESSEQ 54:80 )
REMARK 3 SELECTION : CHAIN D AND (RESSEQ 54:80 )
REMARK 3 ATOM PAIRS NUMBER : 213
REMARK 3 RMSD : 0.027
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3PK1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-NOV-10.
REMARK 100 THE DEPOSITION ID IS D_1000062466.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-FEB-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95364
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13065
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.486
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.10500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.1300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.1
REMARK 200 DATA REDUNDANCY IN SHELL : 4.90
REMARK 200 R MERGE FOR SHELL (I) : 0.64100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.350
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2NL9
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1M SODIUM ACETATE, 0.1M HEPES, 25MM
REMARK 280 CADMIUM SULFATE, 5MM TCEP, PH 7.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
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 48.96150
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.73450
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 48.96150
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 40.73450
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9050 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 138
REMARK 465 SER A 139
REMARK 465 GLY A 140
REMARK 465 MET A 141
REMARK 465 LYS A 142
REMARK 465 GLU A 143
REMARK 465 THR A 144
REMARK 465 ALA A 145
REMARK 465 ALA A 146
REMARK 465 ALA A 147
REMARK 465 LYS A 148
REMARK 465 PHE A 149
REMARK 465 GLU A 150
REMARK 465 ARG A 151
REMARK 465 GLN A 152
REMARK 465 HIS A 153
REMARK 465 MET A 154
REMARK 465 ASP A 155
REMARK 465 SER A 156
REMARK 465 PRO A 157
REMARK 465 ASP A 158
REMARK 465 LEU A 159
REMARK 465 GLY A 160
REMARK 465 THR A 161
REMARK 465 ASP A 162
REMARK 465 ASP A 163
REMARK 465 ASP A 164
REMARK 465 ASP A 165
REMARK 465 LYS A 166
REMARK 465 ALA A 167
REMARK 465 MET A 168
REMARK 465 ALA A 169
REMARK 465 ASP A 170
REMARK 465 ILE A 171
REMARK 465 GLY A 172
REMARK 465 ASP A 195
REMARK 465 THR A 196
REMARK 465 LYS A 197
REMARK 465 PRO A 198
REMARK 465 MET A 199
REMARK 465 GLY A 200
REMARK 465 ARG A 201
REMARK 465 SER A 202
REMARK 465 GLY A 203
REMARK 465 GLU A 322
REMARK 465 ASP A 323
REMARK 465 LEU A 324
REMARK 465 GLU A 325
REMARK 465 GLY A 326
REMARK 465 ASP B 48
REMARK 465 PRO B 49
REMARK 465 VAL B 50
REMARK 465 PRO B 51
REMARK 465 GLN B 52
REMARK 465 ASP B 53
REMARK 465 ALA B 81
REMARK 465 GLY C 138
REMARK 465 SER C 139
REMARK 465 GLY C 140
REMARK 465 MET C 141
REMARK 465 LYS C 142
REMARK 465 GLU C 143
REMARK 465 THR C 144
REMARK 465 ALA C 145
REMARK 465 ALA C 146
REMARK 465 ALA C 147
REMARK 465 LYS C 148
REMARK 465 PHE C 149
REMARK 465 GLU C 150
REMARK 465 ARG C 151
REMARK 465 GLN C 152
REMARK 465 HIS C 153
REMARK 465 MET C 154
REMARK 465 ASP C 155
REMARK 465 SER C 156
REMARK 465 PRO C 157
REMARK 465 ASP C 158
REMARK 465 LEU C 159
REMARK 465 GLY C 160
REMARK 465 THR C 161
REMARK 465 ASP C 162
REMARK 465 ASP C 163
REMARK 465 ASP C 164
REMARK 465 ASP C 165
REMARK 465 LYS C 166
REMARK 465 ALA C 167
REMARK 465 MET C 168
REMARK 465 ALA C 169
REMARK 465 ASP C 170
REMARK 465 ILE C 171
REMARK 465 GLY C 172
REMARK 465 ALA C 193
REMARK 465 LYS C 194
REMARK 465 ASP C 195
REMARK 465 THR C 196
REMARK 465 LYS C 197
REMARK 465 PRO C 198
REMARK 465 MET C 199
REMARK 465 GLY C 200
REMARK 465 ARG C 201
REMARK 465 SER C 202
REMARK 465 GLY C 203
REMARK 465 ALA C 204
REMARK 465 GLU C 322
REMARK 465 ASP C 323
REMARK 465 LEU C 324
REMARK 465 GLU C 325
REMARK 465 GLY C 326
REMARK 465 ASP D 48
REMARK 465 PRO D 49
REMARK 465 VAL D 50
REMARK 465 PRO D 51
REMARK 465 GLN D 52
REMARK 465 ASP D 53
REMARK 465 ALA D 81
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ARG A 176 CD NE CZ NH1 NH2
REMARK 480 GLU A 211 CB CG CD OE1 OE2
REMARK 480 ARG A 233 NH1 NH2
REMARK 480 LYS A 238 CD CE NZ
REMARK 480 LYS A 244 CB CG CD CE NZ
REMARK 480 ARG A 248 CZ NH1 NH2
REMARK 480 LYS A 276 NZ
REMARK 480 GLN A 283 CG CD OE1 NE2
REMARK 480 GLU A 284 CB CG CD OE1 OE2
REMARK 480 GLU A 292 CD OE1 OE2
REMARK 480 LYS A 308 CG CD CE NZ
REMARK 480 GLU A 317 CD OE1 OE2
REMARK 480 HIS A 320 ND1 CD2 CE1 NE2
REMARK 480 LYS B 57 CB CG CD CE NZ
REMARK 480 LYS B 58 CG CD CE NZ
REMARK 480 GLU B 61 CD OE1 OE2
REMARK 480 LYS B 64 CE NZ
REMARK 480 ARG B 65 CD NE CZ NH1 NH2
REMARK 480 ARG B 78 CZ NH1 NH2
REMARK 480 MET B 79 SD CE
REMARK 480 ARG C 176 NE CZ NH1 NH2
REMARK 480 GLU C 180 CG CD OE1 OE2
REMARK 480 ARG C 184 CG CD NE CZ NH1 NH2
REMARK 480 ARG C 187 CG CD NE CZ NH1 NH2
REMARK 480 THR C 191 CB OG1 CG2
REMARK 480 ARG C 207 CG CD NE CZ NH1 NH2
REMARK 480 LYS C 208 CD CE NZ
REMARK 480 GLU C 211 OE1 OE2
REMARK 480 ARG C 233 NH1 NH2
REMARK 480 LYS C 234 CG CD CE NZ
REMARK 480 LYS C 238 CG CD CE NZ
REMARK 480 LYS C 244 CG CD CE NZ
REMARK 480 THR C 280 OG1 CG2
REMARK 480 GLN C 283 OE1 NE2
REMARK 480 GLU C 288 CD OE1 OE2
REMARK 480 ARG C 303 CD NE CZ NH1 NH2
REMARK 480 LYS C 308 CD CE NZ
REMARK 480 GLU C 317 CG CD OE1 OE2
REMARK 480 THR D 56 CB OG1 CG2
REMARK 480 LYS D 57 CB CG CD CE NZ
REMARK 480 LYS D 58 CG CD CE NZ
REMARK 480 GLU D 61 CG CD OE1 OE2
REMARK 480 LYS D 64 CD CE NZ
REMARK 480 ARG D 65 CG CD NE CZ NH1 NH2
REMARK 480 GLU D 75 CD OE1 OE2
REMARK 480 ARG D 78 NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 207 CD - NE - CZ ANGL. DEV. = 9.6 DEGREES
REMARK 500 ARG A 207 NE - CZ - NH1 ANGL. DEV. = -6.7 DEGREES
REMARK 500 ARG A 207 NE - CZ - NH2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 ARG A 233 NE - CZ - NH1 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ARG A 233 NE - CZ - NH2 ANGL. DEV. = 5.3 DEGREES
REMARK 500 ARG C 207 CD - NE - CZ ANGL. DEV. = 8.9 DEGREES
REMARK 500 ARG C 207 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG C 207 NE - CZ - NH2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ARG C 233 NE - CZ - NH1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG C 233 NE - CZ - NH2 ANGL. DEV. = -6.0 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 ASN A 282 99.64 -166.69
REMARK 500 SER A 285 149.77 -39.01
REMARK 500 MET B 79 -3.91 -55.31
REMARK 500 ASN C 282 99.57 -167.93
REMARK 500 MET D 79 -3.20 -53.67
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 CD A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 12
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 13
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 14
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 17
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 18
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 7
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 8
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD C 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD C 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD C 10
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD C 11
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD C 15
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD C 16
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD D 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD D 9
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3PL7 RELATED DB: PDB
DBREF 3PK1 A 174 326 UNP Q07820 MCL1_HUMAN 174 326
DBREF 3PK1 B 48 81 UNP Q07812 BAX_HUMAN 48 81
DBREF 3PK1 C 174 326 UNP Q07820 MCL1_HUMAN 174 326
DBREF 3PK1 D 48 81 UNP Q07812 BAX_HUMAN 48 81
SEQADV 3PK1 GLY A 138 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 SER A 139 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 GLY A 140 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 MET A 141 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 LYS A 142 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 GLU A 143 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 THR A 144 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 ALA A 145 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 ALA A 146 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 ALA A 147 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 LYS A 148 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 PHE A 149 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 GLU A 150 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 ARG A 151 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 GLN A 152 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 HIS A 153 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 MET A 154 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 ASP A 155 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 SER A 156 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 PRO A 157 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 ASP A 158 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 LEU A 159 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 GLY A 160 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 THR A 161 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 ASP A 162 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 ASP A 163 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 ASP A 164 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 ASP A 165 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 LYS A 166 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 ALA A 167 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 MET A 168 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 ALA A 169 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 ASP A 170 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 ILE A 171 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 GLY A 172 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 SER A 173 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 GLY C 138 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 SER C 139 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 GLY C 140 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 MET C 141 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 LYS C 142 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 GLU C 143 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 THR C 144 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 ALA C 145 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 ALA C 146 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 ALA C 147 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 LYS C 148 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 PHE C 149 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 GLU C 150 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 ARG C 151 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 GLN C 152 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 HIS C 153 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 MET C 154 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 ASP C 155 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 SER C 156 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 PRO C 157 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 ASP C 158 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 LEU C 159 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 GLY C 160 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 THR C 161 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 ASP C 162 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 ASP C 163 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 ASP C 164 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 ASP C 165 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 LYS C 166 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 ALA C 167 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 MET C 168 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 ALA C 169 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 ASP C 170 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 ILE C 171 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 GLY C 172 UNP Q07820 EXPRESSION TAG
SEQADV 3PK1 SER C 173 UNP Q07820 EXPRESSION TAG
SEQRES 1 A 189 GLY SER GLY MET LYS GLU THR ALA ALA ALA LYS PHE GLU
SEQRES 2 A 189 ARG GLN HIS MET ASP SER PRO ASP LEU GLY THR ASP ASP
SEQRES 3 A 189 ASP ASP LYS ALA MET ALA ASP ILE GLY SER LEU TYR ARG
SEQRES 4 A 189 GLN SER LEU GLU ILE ILE SER ARG TYR LEU ARG GLU GLN
SEQRES 5 A 189 ALA THR GLY ALA LYS ASP THR LYS PRO MET GLY ARG SER
SEQRES 6 A 189 GLY ALA THR SER ARG LYS ALA LEU GLU THR LEU ARG ARG
SEQRES 7 A 189 VAL GLY ASP GLY VAL GLN ARG ASN HIS GLU THR ALA PHE
SEQRES 8 A 189 GLN GLY MET LEU ARG LYS LEU ASP ILE LYS ASN GLU ASP
SEQRES 9 A 189 ASP VAL LYS SER LEU SER ARG VAL MET ILE HIS VAL PHE
SEQRES 10 A 189 SER ASP GLY VAL THR ASN TRP GLY ARG ILE VAL THR LEU
SEQRES 11 A 189 ILE SER PHE GLY ALA PHE VAL ALA LYS HIS LEU LYS THR
SEQRES 12 A 189 ILE ASN GLN GLU SER CYS ILE GLU PRO LEU ALA GLU SER
SEQRES 13 A 189 ILE THR ASP VAL LEU VAL ARG THR LYS ARG ASP TRP LEU
SEQRES 14 A 189 VAL LYS GLN ARG GLY TRP ASP GLY PHE VAL GLU PHE PHE
SEQRES 15 A 189 HIS VAL GLU ASP LEU GLU GLY
SEQRES 1 B 34 ASP PRO VAL PRO GLN ASP ALA SER THR LYS LYS LEU SER
SEQRES 2 B 34 GLU CYS LEU LYS ARG ILE GLY ASP GLU LEU ASP SER ASN
SEQRES 3 B 34 MET GLU LEU GLN ARG MET ILE ALA
SEQRES 1 C 189 GLY SER GLY MET LYS GLU THR ALA ALA ALA LYS PHE GLU
SEQRES 2 C 189 ARG GLN HIS MET ASP SER PRO ASP LEU GLY THR ASP ASP
SEQRES 3 C 189 ASP ASP LYS ALA MET ALA ASP ILE GLY SER LEU TYR ARG
SEQRES 4 C 189 GLN SER LEU GLU ILE ILE SER ARG TYR LEU ARG GLU GLN
SEQRES 5 C 189 ALA THR GLY ALA LYS ASP THR LYS PRO MET GLY ARG SER
SEQRES 6 C 189 GLY ALA THR SER ARG LYS ALA LEU GLU THR LEU ARG ARG
SEQRES 7 C 189 VAL GLY ASP GLY VAL GLN ARG ASN HIS GLU THR ALA PHE
SEQRES 8 C 189 GLN GLY MET LEU ARG LYS LEU ASP ILE LYS ASN GLU ASP
SEQRES 9 C 189 ASP VAL LYS SER LEU SER ARG VAL MET ILE HIS VAL PHE
SEQRES 10 C 189 SER ASP GLY VAL THR ASN TRP GLY ARG ILE VAL THR LEU
SEQRES 11 C 189 ILE SER PHE GLY ALA PHE VAL ALA LYS HIS LEU LYS THR
SEQRES 12 C 189 ILE ASN GLN GLU SER CYS ILE GLU PRO LEU ALA GLU SER
SEQRES 13 C 189 ILE THR ASP VAL LEU VAL ARG THR LYS ARG ASP TRP LEU
SEQRES 14 C 189 VAL LYS GLN ARG GLY TRP ASP GLY PHE VAL GLU PHE PHE
SEQRES 15 C 189 HIS VAL GLU ASP LEU GLU GLY
SEQRES 1 D 34 ASP PRO VAL PRO GLN ASP ALA SER THR LYS LYS LEU SER
SEQRES 2 D 34 GLU CYS LEU LYS ARG ILE GLY ASP GLU LEU ASP SER ASN
SEQRES 3 D 34 MET GLU LEU GLN ARG MET ILE ALA
HET CD A 1 1
HET CD A 2 1
HET CD A 5 1
HET CD A 12 1
HET CD A 13 1
HET CD A 14 1
HET CD A 17 1
HET CD A 18 1
HET CD B 7 1
HET CD B 8 1
HET CD C 3 1
HET CD C 4 1
HET CD C 10 1
HET CD C 11 1
HET CD C 15 1
HET CD C 16 1
HET CD D 6 1
HET CD D 9 1
HETNAM CD CADMIUM ION
FORMUL 5 CD 18(CD 2+)
FORMUL 23 HOH *49(H2 O)
HELIX 1 1 SER A 173 GLY A 192 1 20
HELIX 2 2 ALA A 204 HIS A 224 1 21
HELIX 3 3 HIS A 224 ASP A 236 1 13
HELIX 4 4 VAL A 243 PHE A 254 1 12
HELIX 5 5 ASN A 260 ASN A 282 1 23
HELIX 6 6 ILE A 287 GLN A 309 1 23
HELIX 7 7 GLY A 311 HIS A 320 1 10
HELIX 8 8 SER B 55 MET B 79 1 25
HELIX 9 9 SER C 173 GLY C 192 1 20
HELIX 10 10 THR C 205 HIS C 224 1 20
HELIX 11 11 HIS C 224 ASP C 236 1 13
HELIX 12 12 VAL C 243 PHE C 254 1 12
HELIX 13 13 ASN C 260 ASN C 282 1 23
HELIX 14 14 ILE C 287 GLN C 309 1 23
HELIX 15 15 GLY C 311 HIS C 320 1 10
HELIX 16 16 SER D 55 MET D 79 1 25
SITE 1 AC1 4 GLU A 225 HOH C 21 HIS C 277 HOH C 327
SITE 1 AC2 3 HIS A 277 HOH C 25 GLU C 225
SITE 1 AC3 4 HOH A 23 HIS A 224 GLU B 69 ASP C 304
SITE 1 AC4 2 CD A 14 CYS A 286
SITE 1 AC5 2 CYS A 286 GLU A 288
SITE 1 AC6 3 CD A 12 GLU A 240 CYS A 286
SITE 1 AC7 2 GLU A 240 ASP A 241
SITE 1 AC8 2 GLU A 180 GLU C 284
SITE 1 AC9 2 CD B 8 CYS B 62
SITE 1 BC1 3 CD B 7 HOH B 18 CYS B 62
SITE 1 BC2 4 ASP A 304 HOH C 22 HIS C 224 GLU D 69
SITE 1 BC3 2 HOH C 34 HIS C 252
SITE 1 BC4 2 CD C 11 CD C 15
SITE 1 BC5 2 CD C 10 CYS C 286
SITE 1 BC6 2 CD C 10 GLU C 240
SITE 1 BC7 2 GLU C 240 ASP C 241
SITE 1 BC8 1 CYS D 62
SITE 1 BC9 1 CYS D 62
CRYST1 97.923 81.469 57.927 90.00 124.23 90.00 C 1 2 1 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 0.010212 0.000000 0.006948 0.00000
SCALE2 0.000000 0.012275 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020880 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
