HEADER APOPTOSIS 23-MAY-17 5VWZ
TITLE BAK IN COMPLEX WITH BIM-H3PC
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BCL-2 HOMOLOGOUS ANTAGONIST/KILLER;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: UNP RESIDUES 23-186;
COMPND 5 SYNONYM: APOPTOSIS REGULATOR BAK,BCL-2-LIKE PROTEIN 7,BCL2-L-7;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: BCL-2-LIKE PROTEIN 11;
COMPND 10 CHAIN: B, D;
COMPND 11 FRAGMENT: UNP RESIDUES 141-166;
COMPND 12 SYNONYM: BCL2-L-11,BCL2-INTERACTING MEDIATOR OF CELL DEATH;
COMPND 13 ENGINEERED: YES;
COMPND 14 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: BAK1, BAK, BCL2L7, CDN1;
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
KEYWDS APOPTOSIS, BCL-2 FAMILY, INHIBITOR
EXPDTA X-RAY DIFFRACTION
AUTHOR J.M.BROUWER,P.M.COLMAN,P.E.CZABOTAR
REVDAT 3 08-JAN-20 5VWZ 1 REMARK
REVDAT 2 29-NOV-17 5VWZ 1 JRNL
REVDAT 1 15-NOV-17 5VWZ 0
JRNL AUTH J.M.BROUWER,P.LAN,A.D.COWAN,J.P.BERNARDINI,R.W.BIRKINSHAW,
JRNL AUTH 2 M.F.VAN DELFT,B.E.SLEEBS,A.Y.ROBIN,A.WARDAK,I.K.TAN,
JRNL AUTH 3 B.RELJIC,E.F.LEE,W.D.FAIRLIE,M.J.CALL,B.J.SMITH,G.DEWSON,
JRNL AUTH 4 G.LESSENE,P.M.COLMAN,P.E.CZABOTAR
JRNL TITL CONVERSION OF BIM-BH3 FROM ACTIVATOR TO INHIBITOR OF BAK
JRNL TITL 2 THROUGH STRUCTURE-BASED DESIGN.
JRNL REF MOL. CELL V. 68 659 2017
JRNL REFN ISSN 1097-4164
JRNL PMID 29149594
JRNL DOI 10.1016/J.MOLCEL.2017.11.001
REMARK 2
REMARK 2 RESOLUTION. 1.62 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.10.1_2155
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.62
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.58
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 41867
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.156
REMARK 3 R VALUE (WORKING SET) : 0.154
REMARK 3 FREE R VALUE : 0.191
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.770
REMARK 3 FREE R VALUE TEST SET COUNT : 1996
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 38.5900 - 3.9080 1.00 2936 149 0.1322 0.1462
REMARK 3 2 3.9080 - 3.1023 1.00 2875 140 0.1284 0.1661
REMARK 3 3 3.1023 - 2.7103 1.00 2850 141 0.1463 0.1775
REMARK 3 4 2.7103 - 2.4625 1.00 2875 141 0.1484 0.1692
REMARK 3 5 2.4625 - 2.2860 1.00 2834 141 0.1467 0.2051
REMARK 3 6 2.2860 - 2.1513 1.00 2860 140 0.1468 0.1848
REMARK 3 7 2.1513 - 2.0435 1.00 2849 141 0.1528 0.1913
REMARK 3 8 2.0435 - 1.9546 1.00 2811 144 0.1605 0.1912
REMARK 3 9 1.9546 - 1.8793 1.00 2864 140 0.1792 0.2337
REMARK 3 10 1.8793 - 1.8145 1.00 2822 143 0.1841 0.2591
REMARK 3 11 1.8145 - 1.7578 1.00 2847 143 0.1898 0.2222
REMARK 3 12 1.7578 - 1.7075 1.00 2807 144 0.2112 0.2333
REMARK 3 13 1.7075 - 1.6626 1.00 2799 147 0.2117 0.2939
REMARK 3 14 1.6626 - 1.6220 0.99 2842 142 0.2227 0.2843
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.200
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.006 3307
REMARK 3 ANGLE : 1.132 4482
REMARK 3 CHIRALITY : 0.048 457
REMARK 3 PLANARITY : 0.006 601
REMARK 3 DIHEDRAL : 22.179 1942
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 11
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 21 THROUGH 48 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.9232 -50.7929 3.9929
REMARK 3 T TENSOR
REMARK 3 T11: 0.0022 T22: 0.0842
REMARK 3 T33: 0.1355 T12: -0.0109
REMARK 3 T13: 0.0199 T23: 0.0047
REMARK 3 L TENSOR
REMARK 3 L11: 2.1597 L22: 2.1560
REMARK 3 L33: 3.3989 L12: -0.2157
REMARK 3 L13: -0.0158 L23: 0.3301
REMARK 3 S TENSOR
REMARK 3 S11: 0.0521 S12: -0.0860 S13: 0.0974
REMARK 3 S21: 0.0353 S22: 0.0207 S23: 0.2313
REMARK 3 S31: -0.1303 S32: -0.1462 S33: -0.0822
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 49 THROUGH 57 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.9163 -51.6353 24.1923
REMARK 3 T TENSOR
REMARK 3 T11: 0.6801 T22: 0.4210
REMARK 3 T33: 0.4677 T12: -0.0787
REMARK 3 T13: 0.0860 T23: 0.2296
REMARK 3 L TENSOR
REMARK 3 L11: 0.8613 L22: 2.2644
REMARK 3 L33: 5.7527 L12: -1.3977
REMARK 3 L13: 2.0011 L23: -3.2780
REMARK 3 S TENSOR
REMARK 3 S11: 0.0118 S12: -1.1269 S13: -1.2382
REMARK 3 S21: 1.3497 S22: -0.4960 S23: -0.2739
REMARK 3 S31: 0.6749 S32: 0.0177 S33: 0.5156
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 58 THROUGH 82 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.1147 -50.3005 7.7924
REMARK 3 T TENSOR
REMARK 3 T11: -0.0103 T22: 0.1337
REMARK 3 T33: 0.2263 T12: 0.0079
REMARK 3 T13: 0.0551 T23: -0.0035
REMARK 3 L TENSOR
REMARK 3 L11: 2.9618 L22: 0.3324
REMARK 3 L33: 0.5910 L12: 0.5930
REMARK 3 L13: 1.1072 L23: 0.0367
REMARK 3 S TENSOR
REMARK 3 S11: -0.0375 S12: -0.2332 S13: 0.1318
REMARK 3 S21: 0.2229 S22: -0.0301 S23: 0.4078
REMARK 3 S31: -0.1011 S32: -0.1626 S33: 0.0556
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 83 THROUGH 106 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.9454 -56.1956 15.1440
REMARK 3 T TENSOR
REMARK 3 T11: 0.1335 T22: 0.0986
REMARK 3 T33: 0.1032 T12: 0.0062
REMARK 3 T13: -0.0101 T23: -0.0095
REMARK 3 L TENSOR
REMARK 3 L11: 1.9063 L22: 5.3367
REMARK 3 L33: 3.0739 L12: 2.3656
REMARK 3 L13: 0.3407 L23: -1.2608
REMARK 3 S TENSOR
REMARK 3 S11: 0.3164 S12: -0.2601 S13: 0.0649
REMARK 3 S21: 0.6974 S22: -0.3051 S23: -0.1059
REMARK 3 S31: -0.1232 S32: 0.0838 S33: -0.0134
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 107 THROUGH 186 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.1771 -54.8360 1.7993
REMARK 3 T TENSOR
REMARK 3 T11: 0.0135 T22: 0.0815
REMARK 3 T33: 0.0836 T12: 0.0025
REMARK 3 T13: 0.0118 T23: 0.0051
REMARK 3 L TENSOR
REMARK 3 L11: 0.7215 L22: 1.3549
REMARK 3 L33: 1.3096 L12: 0.0055
REMARK 3 L13: 0.2366 L23: 0.1193
REMARK 3 S TENSOR
REMARK 3 S11: 0.0145 S12: 0.0112 S13: -0.0171
REMARK 3 S21: -0.0168 S22: -0.0287 S23: -0.0115
REMARK 3 S31: -0.0426 S32: 0.0233 S33: -0.0149
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 141 THROUGH 166 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.9764 -65.5370 8.3332
REMARK 3 T TENSOR
REMARK 3 T11: 0.0400 T22: 0.0758
REMARK 3 T33: 0.1397 T12: 0.0209
REMARK 3 T13: 0.0263 T23: 0.0213
REMARK 3 L TENSOR
REMARK 3 L11: 5.6055 L22: 1.9328
REMARK 3 L33: 2.1423 L12: 1.1178
REMARK 3 L13: -0.0187 L23: 0.3717
REMARK 3 S TENSOR
REMARK 3 S11: 0.1334 S12: -0.1872 S13: -0.1093
REMARK 3 S21: -0.0047 S22: -0.1379 S23: -0.2911
REMARK 3 S31: 0.1515 S32: -0.0650 S33: 0.0001
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 21 THROUGH 69 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.5384 -78.3211 34.4191
REMARK 3 T TENSOR
REMARK 3 T11: 0.1822 T22: 0.1237
REMARK 3 T33: 0.1984 T12: -0.0301
REMARK 3 T13: -0.0172 T23: 0.0267
REMARK 3 L TENSOR
REMARK 3 L11: 2.6881 L22: 3.0011
REMARK 3 L33: 1.7752 L12: -0.0471
REMARK 3 L13: 1.1034 L23: 0.5890
REMARK 3 S TENSOR
REMARK 3 S11: 0.1938 S12: -0.0991 S13: -0.2162
REMARK 3 S21: -0.1446 S22: -0.0467 S23: 0.3903
REMARK 3 S31: 0.4306 S32: -0.3855 S33: -0.1365
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 70 THROUGH 106 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.3061 -70.9888 27.5112
REMARK 3 T TENSOR
REMARK 3 T11: 0.1306 T22: 0.0411
REMARK 3 T33: 0.0735 T12: -0.0472
REMARK 3 T13: -0.0572 T23: -0.0188
REMARK 3 L TENSOR
REMARK 3 L11: 3.2017 L22: 3.2745
REMARK 3 L33: 4.5479 L12: -0.5991
REMARK 3 L13: -1.2874 L23: -1.2174
REMARK 3 S TENSOR
REMARK 3 S11: 0.0556 S12: 0.2182 S13: -0.0262
REMARK 3 S21: -0.2147 S22: -0.0303 S23: 0.1072
REMARK 3 S31: 0.1521 S32: -0.1788 S33: -0.0609
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 107 THROUGH 150 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.3878 -73.3229 31.1297
REMARK 3 T TENSOR
REMARK 3 T11: 0.1357 T22: 0.0703
REMARK 3 T33: 0.0525 T12: 0.0053
REMARK 3 T13: 0.0031 T23: 0.0281
REMARK 3 L TENSOR
REMARK 3 L11: 1.6285 L22: 3.1034
REMARK 3 L33: 2.9645 L12: -0.4024
REMARK 3 L13: 0.1398 L23: 0.6238
REMARK 3 S TENSOR
REMARK 3 S11: 0.0416 S12: 0.0714 S13: 0.0221
REMARK 3 S21: -0.1729 S22: -0.0032 S23: -0.1069
REMARK 3 S31: 0.1805 S32: 0.0201 S33: -0.0160
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 151 THROUGH 184 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.8572 -72.7444 42.9873
REMARK 3 T TENSOR
REMARK 3 T11: 0.1709 T22: 0.1153
REMARK 3 T33: 0.0516 T12: -0.0035
REMARK 3 T13: 0.0035 T23: 0.0193
REMARK 3 L TENSOR
REMARK 3 L11: 2.5123 L22: 3.9347
REMARK 3 L33: 4.1032 L12: -0.2685
REMARK 3 L13: -0.5228 L23: 1.1759
REMARK 3 S TENSOR
REMARK 3 S11: 0.0639 S12: -0.2250 S13: 0.0824
REMARK 3 S21: 0.3364 S22: 0.0042 S23: -0.0540
REMARK 3 S31: -0.1075 S32: -0.0883 S33: -0.0500
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 141 THROUGH 166 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.0437 -61.9049 30.4237
REMARK 3 T TENSOR
REMARK 3 T11: 0.1234 T22: 0.0795
REMARK 3 T33: 0.0761 T12: -0.0225
REMARK 3 T13: -0.0406 T23: 0.0284
REMARK 3 L TENSOR
REMARK 3 L11: 7.9512 L22: 5.2578
REMARK 3 L33: 6.5901 L12: -2.0450
REMARK 3 L13: -4.2479 L23: 1.3165
REMARK 3 S TENSOR
REMARK 3 S11: 0.0204 S12: -0.0700 S13: 0.1895
REMARK 3 S21: -0.1612 S22: -0.0768 S23: -0.1634
REMARK 3 S31: -0.1558 S32: 0.2853 S33: 0.0204
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5VWZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JUN-17.
REMARK 100 THE DEPOSITION ID IS D_1000227631.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-FEB-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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) : 0.9537
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41869
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.622
REMARK 200 RESOLUTION RANGE LOW (A) : 38.580
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.400
REMARK 200 R MERGE (I) : 0.11740
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 34.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.87
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 % PEG 20000, 20 % PEG MME 550, 38
REMARK 280 MM IMIDAZOLE PH 6.5, 20 MM AMMONIUM ACETATE, 20 MM POTASSIUM
REMARK 280 SODIUM TARTRATE, 20 MM SODIUM FORMATE, 62 MM SODIUM MES PH 6.5,
REMARK 280 20 MM TRISODIUM CITRATE, AND 20 MM SODIUM OXAMATE, VAPOR
REMARK 280 DIFFUSION, TEMPERATURE 281K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 28.33400
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 17
REMARK 465 PRO A 18
REMARK 465 LEU A 19
REMARK 465 GLY A 20
REMARK 465 GLY C 17
REMARK 465 PRO C 18
REMARK 465 LEU C 19
REMARK 465 GLY C 20
REMARK 465 ASN C 185
REMARK 465 GLY C 186
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 OE2 GLU A 120 O HOH A 201 1.84
REMARK 500 O HOH B 220 O HOH B 222 1.99
REMARK 500 O HOH A 309 O HOH A 347 2.03
REMARK 500 O HOH B 224 O HOH B 226 2.05
REMARK 500 O HOH C 394 O HOH C 440 2.07
REMARK 500 O HOH C 437 O HOH C 446 2.09
REMARK 500 OE2 GLU D 145 O HOH D 301 2.11
REMARK 500 OE2 GLU A 105 O HOH A 202 2.12
REMARK 500 N SER A 21 O HOH A 203 2.13
REMARK 500 NE2 GLN C 94 O HOH C 301 2.15
REMARK 500 O HOH C 333 O HOH C 440 2.15
REMARK 500 O HOH C 387 O HOH C 392 2.17
REMARK 500 OE1 GLU A 120 O HOH A 204 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 346 O HOH B 203 1455 2.17
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 VAL A 52 -103.53 30.94
REMARK 500 ALA A 53 32.26 72.08
REMARK 500 SER A 166 -23.15 80.35
REMARK 500 TYR D 163 49.71 -102.78
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 1PG C 202
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PG C 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PG C 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NH4 D 201
DBREF 5VWZ A 23 186 UNP Q16611 BAK_HUMAN 23 186
DBREF 5VWZ B 141 166 UNP O43521 B2L11_HUMAN 141 166
DBREF 5VWZ C 23 186 UNP Q16611 BAK_HUMAN 23 186
DBREF 5VWZ D 141 166 UNP O43521 B2L11_HUMAN 141 166
SEQADV 5VWZ GLY A 17 UNP Q16611 EXPRESSION TAG
SEQADV 5VWZ PRO A 18 UNP Q16611 EXPRESSION TAG
SEQADV 5VWZ LEU A 19 UNP Q16611 EXPRESSION TAG
SEQADV 5VWZ GLY A 20 UNP Q16611 EXPRESSION TAG
SEQADV 5VWZ SER A 21 UNP Q16611 EXPRESSION TAG
SEQADV 5VWZ MET A 22 UNP Q16611 EXPRESSION TAG
SEQADV 5VWZ SER A 166 UNP Q16611 CYS 166 ENGINEERED MUTATION
SEQADV 5VWZ GLY C 17 UNP Q16611 EXPRESSION TAG
SEQADV 5VWZ PRO C 18 UNP Q16611 EXPRESSION TAG
SEQADV 5VWZ LEU C 19 UNP Q16611 EXPRESSION TAG
SEQADV 5VWZ GLY C 20 UNP Q16611 EXPRESSION TAG
SEQADV 5VWZ SER C 21 UNP Q16611 EXPRESSION TAG
SEQADV 5VWZ MET C 22 UNP Q16611 EXPRESSION TAG
SEQADV 5VWZ SER C 166 UNP Q16611 CYS 166 ENGINEERED MUTATION
SEQRES 1 A 170 GLY PRO LEU GLY SER MET SER GLU GLU GLN VAL ALA GLN
SEQRES 2 A 170 ASP THR GLU GLU VAL PHE ARG SER TYR VAL PHE TYR ARG
SEQRES 3 A 170 HIS GLN GLN GLU GLN GLU ALA GLU GLY VAL ALA ALA PRO
SEQRES 4 A 170 ALA ASP PRO GLU MET VAL THR LEU PRO LEU GLN PRO SER
SEQRES 5 A 170 SER THR MET GLY GLN VAL GLY ARG GLN LEU ALA ILE ILE
SEQRES 6 A 170 GLY ASP ASP ILE ASN ARG ARG TYR ASP SER GLU PHE GLN
SEQRES 7 A 170 THR MET LEU GLN HIS LEU GLN PRO THR ALA GLU ASN ALA
SEQRES 8 A 170 TYR GLU TYR PHE THR LYS ILE ALA THR SER LEU PHE GLU
SEQRES 9 A 170 SER GLY ILE ASN TRP GLY ARG VAL VAL ALA LEU LEU GLY
SEQRES 10 A 170 PHE GLY TYR ARG LEU ALA LEU HIS VAL TYR GLN HIS GLY
SEQRES 11 A 170 LEU THR GLY PHE LEU GLY GLN VAL THR ARG PHE VAL VAL
SEQRES 12 A 170 ASP PHE MET LEU HIS HIS SER ILE ALA ARG TRP ILE ALA
SEQRES 13 A 170 GLN ARG GLY GLY TRP VAL ALA ALA LEU ASN LEU GLY ASN
SEQRES 14 A 170 GLY
SEQRES 1 B 26 ASP MET ARG PRO GLU ILE TRP ILE ALA GLN GLU LEU ARG
SEQRES 2 B 26 ARG 9R1 GLY ASP GLU PHE ASN ALA TYR TYR ALA ARG ARG
SEQRES 1 C 170 GLY PRO LEU GLY SER MET SER GLU GLU GLN VAL ALA GLN
SEQRES 2 C 170 ASP THR GLU GLU VAL PHE ARG SER TYR VAL PHE TYR ARG
SEQRES 3 C 170 HIS GLN GLN GLU GLN GLU ALA GLU GLY VAL ALA ALA PRO
SEQRES 4 C 170 ALA ASP PRO GLU MET VAL THR LEU PRO LEU GLN PRO SER
SEQRES 5 C 170 SER THR MET GLY GLN VAL GLY ARG GLN LEU ALA ILE ILE
SEQRES 6 C 170 GLY ASP ASP ILE ASN ARG ARG TYR ASP SER GLU PHE GLN
SEQRES 7 C 170 THR MET LEU GLN HIS LEU GLN PRO THR ALA GLU ASN ALA
SEQRES 8 C 170 TYR GLU TYR PHE THR LYS ILE ALA THR SER LEU PHE GLU
SEQRES 9 C 170 SER GLY ILE ASN TRP GLY ARG VAL VAL ALA LEU LEU GLY
SEQRES 10 C 170 PHE GLY TYR ARG LEU ALA LEU HIS VAL TYR GLN HIS GLY
SEQRES 11 C 170 LEU THR GLY PHE LEU GLY GLN VAL THR ARG PHE VAL VAL
SEQRES 12 C 170 ASP PHE MET LEU HIS HIS SER ILE ALA ARG TRP ILE ALA
SEQRES 13 C 170 GLN ARG GLY GLY TRP VAL ALA ALA LEU ASN LEU GLY ASN
SEQRES 14 C 170 GLY
SEQRES 1 D 26 ASP MET ARG PRO GLU ILE TRP ILE ALA GLN GLU LEU ARG
SEQRES 2 D 26 ARG 9R1 GLY ASP GLU PHE ASN ALA TYR TYR ALA ARG ARG
MODRES 5VWZ 9R1 B 155 ILE MODIFIED RESIDUE
MODRES 5VWZ 9R1 D 155 ILE MODIFIED RESIDUE
HET 9R1 B 155 12
HET 9R1 D 155 12
HET 1PG C 201 17
HET 1PG C 202 13
HET NH4 D 201 5
HETNAM 9R1 (2S)-2-AMINOOCTANEDIOIC ACID
HETNAM 1PG 2-(2-{2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-
HETNAM 2 1PG ETHANOL
HETNAM NH4 AMMONIUM ION
FORMUL 2 9R1 2(C8 H15 N O4)
FORMUL 5 1PG 2(C11 H24 O6)
FORMUL 7 NH4 H4 N 1+
FORMUL 8 HOH *390(H2 O)
HELIX 1 AA1 SER A 23 ALA A 49 1 27
HELIX 2 AA2 ASP A 57 THR A 62 1 6
HELIX 3 AA3 SER A 69 ILE A 81 1 13
HELIX 4 AA4 GLY A 82 ARG A 88 1 7
HELIX 5 AA5 TYR A 89 GLN A 101 1 13
HELIX 6 AA6 ASN A 106 GLU A 120 1 15
HELIX 7 AA7 ASN A 124 HIS A 145 1 22
HELIX 8 AA8 PHE A 150 HIS A 165 1 16
HELIX 9 AA9 SER A 166 ARG A 174 1 9
HELIX 10 AB1 GLY A 175 LEU A 181 5 7
HELIX 11 AB2 ARG B 143 ARG B 166 1 24
HELIX 12 AB3 SER C 23 GLU C 48 1 26
HELIX 13 AB4 ASP C 57 THR C 62 1 6
HELIX 14 AB5 SER C 69 GLY C 82 1 14
HELIX 15 AB6 GLY C 82 TYR C 89 1 8
HELIX 16 AB7 TYR C 89 GLN C 101 1 13
HELIX 17 AB8 ASN C 106 SER C 121 1 16
HELIX 18 AB9 ASN C 124 HIS C 145 1 22
HELIX 19 AC1 PHE C 150 HIS C 165 1 16
HELIX 20 AC2 SER C 166 ARG C 174 1 9
HELIX 21 AC3 GLY C 175 LEU C 183 5 9
HELIX 22 AC4 ARG D 143 TYR D 163 1 21
LINK C ARG B 154 N 9R1 B 155 1555 1555 1.33
LINK C 9R1 B 155 N GLY B 156 1555 1555 1.33
LINK C ARG D 154 N 9R1 D 155 1555 1555 1.33
LINK C 9R1 D 155 N GLY D 156 1555 1555 1.33
SITE 1 AC1 7 TYR A 143 GLY A 146 THR A 148 TYR C 143
SITE 2 AC1 7 GLN C 144 GLY C 146 HOH C 366
SITE 1 AC2 6 HIS A 99 ASP B 141 MET B 142 TRP B 147
SITE 2 AC2 6 HIS C 99 TRP D 147
SITE 1 AC3 1 MET D 142
CRYST1 38.237 56.668 79.291 90.00 103.32 90.00 P 1 21 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.026153 0.000000 0.006191 0.00000
SCALE2 0.000000 0.017647 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012960 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
