HEADER SPLICING 03-FEB-16 5I0A
TITLE RECA MINI INTEIN IN COMPLEX WITH CISPLATIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET45B
KEYWDS INHIBITOR, CISPLATIN, INTEIN, SPLICING
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.LI,J.ZHANG,H.M.LI
REVDAT 4 27-SEP-23 5I0A 1 REMARK
REVDAT 3 25-DEC-19 5I0A 1 REMARK
REVDAT 2 20-SEP-17 5I0A 1 REMARK
REVDAT 1 21-SEP-16 5I0A 0
JRNL AUTH H.CHAN,S.PEARSON,C.GREEN,Z.LI,J.ZHANG,S.LIPPARD,G.BELFORT,
JRNL AUTH 2 A.SHEKHTMAN,H.M.LI,M.BELFORT
JRNL TITL STRUCTURAL INSIGHTS INTO PROTEIN SPLICING INHIBITION BY
JRNL TITL 2 PLATINUM THERAPEUTICS AS POTENTIAL ANTI-MICROBIALS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.17
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 42316
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.193
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.890
REMARK 3 FREE R VALUE TEST SET COUNT : 3761
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
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 : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.920
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.85
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
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 1 THROUGH 15 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.4105 10.0081 -4.8302
REMARK 3 T TENSOR
REMARK 3 T11: 0.0792 T22: 0.0870
REMARK 3 T33: 0.1754 T12: -0.0163
REMARK 3 T13: -0.0281 T23: 0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 0.8648 L22: 2.7925
REMARK 3 L33: 8.1605 L12: -0.3922
REMARK 3 L13: 0.0768 L23: 1.8296
REMARK 3 S TENSOR
REMARK 3 S11: -0.0344 S12: -0.0168 S13: 0.1529
REMARK 3 S21: -0.1765 S22: -0.0307 S23: 0.2488
REMARK 3 S31: -0.3512 S32: -0.2895 S33: 0.0606
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 16 THROUGH 24 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.7315 15.8513 -8.2260
REMARK 3 T TENSOR
REMARK 3 T11: 0.2480 T22: 0.1091
REMARK 3 T33: 0.2422 T12: 0.0076
REMARK 3 T13: -0.1265 T23: 0.0255
REMARK 3 L TENSOR
REMARK 3 L11: 1.3999 L22: 4.8764
REMARK 3 L33: 6.2703 L12: 1.4338
REMARK 3 L13: -1.1898 L23: 0.4851
REMARK 3 S TENSOR
REMARK 3 S11: -0.3251 S12: 0.2467 S13: 0.3970
REMARK 3 S21: -0.6886 S22: -0.0476 S23: 0.7380
REMARK 3 S31: -0.9932 S32: -0.3749 S33: 0.2315
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 25 THROUGH 61 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.9525 9.3996 -5.1547
REMARK 3 T TENSOR
REMARK 3 T11: 0.0950 T22: 0.1158
REMARK 3 T33: 0.1261 T12: -0.0380
REMARK 3 T13: -0.0216 T23: 0.0011
REMARK 3 L TENSOR
REMARK 3 L11: 0.8810 L22: 2.6550
REMARK 3 L33: 4.2183 L12: 0.0691
REMARK 3 L13: 0.2501 L23: 2.1061
REMARK 3 S TENSOR
REMARK 3 S11: -0.0991 S12: 0.0590 S13: 0.1139
REMARK 3 S21: -0.1455 S22: 0.1629 S23: -0.0671
REMARK 3 S31: -0.3006 S32: 0.4983 S33: -0.0276
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 62 THROUGH 79 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.1671 -1.6503 -11.6883
REMARK 3 T TENSOR
REMARK 3 T11: 0.0748 T22: 0.1250
REMARK 3 T33: 0.0746 T12: 0.0002
REMARK 3 T13: 0.0134 T23: -0.0196
REMARK 3 L TENSOR
REMARK 3 L11: 2.7033 L22: 5.1479
REMARK 3 L33: 4.1392 L12: -0.3709
REMARK 3 L13: 1.2038 L23: -1.1817
REMARK 3 S TENSOR
REMARK 3 S11: -0.0162 S12: 0.0832 S13: -0.1232
REMARK 3 S21: -0.1464 S22: -0.0405 S23: -0.0872
REMARK 3 S31: -0.0159 S32: 0.4336 S33: 0.0524
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 80 THROUGH 86 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.8033 -2.9317 -11.9626
REMARK 3 T TENSOR
REMARK 3 T11: 0.1200 T22: 0.2353
REMARK 3 T33: 0.1441 T12: 0.0521
REMARK 3 T13: 0.0397 T23: -0.0088
REMARK 3 L TENSOR
REMARK 3 L11: 5.4385 L22: 5.4485
REMARK 3 L33: 6.5070 L12: -0.0485
REMARK 3 L13: 5.0104 L23: -3.2497
REMARK 3 S TENSOR
REMARK 3 S11: 0.0896 S12: 0.3460 S13: -0.0836
REMARK 3 S21: -0.4055 S22: -0.2735 S23: -0.3228
REMARK 3 S31: 0.5845 S32: 0.8925 S33: 0.1731
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 87 THROUGH 96 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.1788 -7.1715 -10.0483
REMARK 3 T TENSOR
REMARK 3 T11: 0.0996 T22: 0.1070
REMARK 3 T33: 0.1339 T12: 0.0212
REMARK 3 T13: -0.0331 T23: -0.0252
REMARK 3 L TENSOR
REMARK 3 L11: 2.2649 L22: 5.7397
REMARK 3 L33: 6.7503 L12: -0.8444
REMARK 3 L13: -0.2987 L23: 2.7198
REMARK 3 S TENSOR
REMARK 3 S11: 0.0649 S12: 0.3064 S13: -0.2350
REMARK 3 S21: -0.1498 S22: -0.0254 S23: 0.1712
REMARK 3 S31: 0.4467 S32: 0.1746 S33: -0.0243
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 97 THROUGH 413 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.5021 -6.1561 -5.7010
REMARK 3 T TENSOR
REMARK 3 T11: 0.1380 T22: 0.0930
REMARK 3 T33: 0.2400 T12: 0.0138
REMARK 3 T13: 0.0107 T23: -0.0078
REMARK 3 L TENSOR
REMARK 3 L11: 1.7713 L22: 2.9829
REMARK 3 L33: 6.6689 L12: 0.3999
REMARK 3 L13: -0.7425 L23: 0.5666
REMARK 3 S TENSOR
REMARK 3 S11: 0.0368 S12: -0.0477 S13: -0.0543
REMARK 3 S21: 0.1972 S22: -0.0190 S23: 0.5379
REMARK 3 S31: 0.3847 S32: -0.4152 S33: -0.0227
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 414 THROUGH 425 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.8780 11.0558 -15.6858
REMARK 3 T TENSOR
REMARK 3 T11: 0.3516 T22: 0.1998
REMARK 3 T33: 0.1419 T12: -0.0751
REMARK 3 T13: -0.0105 T23: 0.0147
REMARK 3 L TENSOR
REMARK 3 L11: 0.4558 L22: 1.5596
REMARK 3 L33: 1.4098 L12: -0.5221
REMARK 3 L13: -0.3310 L23: 0.9900
REMARK 3 S TENSOR
REMARK 3 S11: -0.0974 S12: 0.2129 S13: 0.1312
REMARK 3 S21: -0.5994 S22: 0.0244 S23: -0.0070
REMARK 3 S31: -0.8359 S32: 0.2876 S33: 0.0667
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 426 THROUGH 433 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.2055 7.6334 0.2628
REMARK 3 T TENSOR
REMARK 3 T11: 0.1033 T22: 0.2234
REMARK 3 T33: 0.1391 T12: -0.0340
REMARK 3 T13: -0.0140 T23: -0.0149
REMARK 3 L TENSOR
REMARK 3 L11: 7.6503 L22: 3.9346
REMARK 3 L33: 5.9031 L12: 2.9494
REMARK 3 L13: 4.1839 L23: 2.7030
REMARK 3 S TENSOR
REMARK 3 S11: -0.4267 S12: -0.2193 S13: 0.0587
REMARK 3 S21: -0.1889 S22: 0.3493 S23: -0.2119
REMARK 3 S31: -0.5129 S32: 0.7864 S33: 0.0665
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 434 THROUGH 443 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.1599 6.0123 -6.3268
REMARK 3 T TENSOR
REMARK 3 T11: 0.1260 T22: 0.1852
REMARK 3 T33: 0.1492 T12: -0.0333
REMARK 3 T13: 0.0095 T23: -0.0013
REMARK 3 L TENSOR
REMARK 3 L11: 4.6926 L22: 6.7259
REMARK 3 L33: 4.7104 L12: -0.7366
REMARK 3 L13: 0.3527 L23: -0.2926
REMARK 3 S TENSOR
REMARK 3 S11: -0.0576 S12: 0.0392 S13: 0.3486
REMARK 3 S21: -0.1241 S22: 0.0274 S23: -0.6234
REMARK 3 S31: -0.3886 S32: 0.6853 S33: 0.0099
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'C'
REMARK 3 ORIGIN FOR THE GROUP (A): -2.7663 3.4762 -4.3504
REMARK 3 T TENSOR
REMARK 3 T11: 0.3225 T22: 0.8529
REMARK 3 T33: 0.9312 T12: 0.1114
REMARK 3 T13: 0.6232 T23: 0.2649
REMARK 3 L TENSOR
REMARK 3 L11: 2.0046 L22: 2.0044
REMARK 3 L33: 2.0001 L12: 1.9980
REMARK 3 L13: 2.0015 L23: 1.9985
REMARK 3 S TENSOR
REMARK 3 S11: 0.7156 S12: 0.6615 S13: 0.0836
REMARK 3 S21: -0.0922 S22: -0.0070 S23: -0.1674
REMARK 3 S31: -1.1505 S32: -0.6871 S33: -0.7141
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 5I0A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-FEB-16.
REMARK 100 THE DEPOSITION ID IS D_1000218031.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-AUG-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0711
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22614
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : 0.06600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.50
REMARK 200 R MERGE FOR SHELL (I) : 0.60300
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: SAD
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 2IN0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 58% AMMONIUM SULFATE, 0.1M TRIS, PH
REMARK 280 8.5, 2% ISOPROPANOL, 2 MM CISPLATIN, EVAPORATION, TEMPERATURE
REMARK 280 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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 28.63450
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.02550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.63450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 32.02550
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 772 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 792 LIES ON A SPECIAL POSITION.
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 PRO A 444
REMARK 465 PHE A 445
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 O HOH A 743 O HOH A 777 1.99
REMARK 500 O HOH A 601 O HOH A 768 2.15
REMARK 500 O HOH A 660 O HOH A 737 2.15
REMARK 500 O HOH A 601 O HOH A 724 2.17
REMARK 500 O HOH A 759 O HOH A 788 2.18
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 GLU A 427 -52.97 70.39
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 790 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH A 791 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH A 792 DISTANCE = 6.31 ANGSTROMS
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 TCE A 503
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 CPT A 502 PT1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 1 N
REMARK 620 2 CYS A 1 SG 77.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CPT A 501 PT1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 439 NE2
REMARK 620 2 CYS A 441 SG 96.4
REMARK 620 3 HOH A 777 O 174.4 82.9
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CPT A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CPT A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TCE A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 504
DBREF 5I0A A 1 445 PDB 5I0A 5I0A 1 445
SEQRES 1 A 144 CYS LEU ALA GLU GLY THR ARG ILE PHE ASP PRO VAL THR
SEQRES 2 A 144 GLY THR THR HIS ARG ILE GLU ASP VAL VAL ASP GLY ARG
SEQRES 3 A 144 LYS PRO ILE HIS VAL VAL ALA ALA ALA LYS ASP GLY THR
SEQRES 4 A 144 LEU HIS ALA ARG PRO VAL VAL SER TRP PHE ASP GLN GLY
SEQRES 5 A 144 THR ARG ASP VAL ILE GLY LEU ARG ILE ALA GLY GLY ALA
SEQRES 6 A 144 ILE LEU TRP ALA THR PRO ASP HIS LYS VAL LEU THR GLU
SEQRES 7 A 144 TYR GLY TRP ARG ALA ALA GLY GLU LEU ARG LYS GLY ASP
SEQRES 8 A 144 ARG VAL ALA VAL ARG ASP VAL GLU THR GLY GLU LEU ARG
SEQRES 9 A 144 TYR SER VAL ILE ARG GLU VAL LEU PRO THR ARG ARG ALA
SEQRES 10 A 144 ARG THR PHE ASP LEU GLU VAL GLU GLU LEU HIS THR LEU
SEQRES 11 A 144 VAL ALA GLU GLY VAL VAL VAL HIS ALA CYS SER PRO PRO
SEQRES 12 A 144 PHE
HET CPT A 501 1
HET CPT A 502 1
HET TCE A 503 11
HET SO4 A 504 5
HETNAM CPT CISPLATIN
HETNAM TCE 3,3',3''-PHOSPHANETRIYLTRIPROPANOIC ACID
HETNAM SO4 SULFATE ION
HETSYN CPT DIAMMINE(DICHLORO)PLATINUM
HETSYN TCE 3-[BIS(2-CARBOXYETHYL)PHOSPHANYL]PROPANOIC ACID
FORMUL 2 CPT 2(CL2 H6 N2 PT)
FORMUL 4 TCE C9 H15 O6 P
FORMUL 5 SO4 O4 S 2-
FORMUL 6 HOH *192(H2 O)
HELIX 1 AA1 ILE A 19 GLY A 25 1 7
HELIX 2 AA2 GLY A 85 LEU A 87 5 3
SHEET 1 AA1 6 HIS A 30 ALA A 34 0
SHEET 2 AA1 6 LEU A 40 ILE A 61 -1 O HIS A 41 N ALA A 33
SHEET 3 AA1 6 ILE A 66 ALA A 69 -1 O ALA A 69 N ILE A 57
SHEET 4 AA1 6 LEU A 2 ALA A 3 -1 N ALA A 3 O TRP A 68
SHEET 5 AA1 6 LEU A 404 VAL A 425 -1 O PHE A 421 N LEU A 2
SHEET 6 AA1 6 ARG A 92 ARG A 96 -1 N VAL A 95 O ARG A 405
SHEET 1 AA2 4 HIS A 30 ALA A 34 0
SHEET 2 AA2 4 LEU A 40 ILE A 61 -1 O HIS A 41 N ALA A 33
SHEET 3 AA2 4 LEU A 404 VAL A 425 -1 O LEU A 413 N GLY A 58
SHEET 4 AA2 4 ARG A 92 ARG A 96 -1 N VAL A 95 O ARG A 405
SHEET 1 AA3 2 ARG A 7 PHE A 9 0
SHEET 2 AA3 2 THR A 16 ARG A 18 -1 O HIS A 17 N ILE A 8
SHEET 1 AA4 2 LYS A 74 THR A 77 0
SHEET 2 AA4 2 GLY A 80 ALA A 83 -1 O ARG A 82 N VAL A 75
SHEET 1 AA5 2 THR A 430 ALA A 433 0
SHEET 2 AA5 2 VAL A 436 HIS A 439 -1 O VAL A 438 N LEU A 431
LINK N CYS A 1 PT1 CPT A 502 1555 1555 2.24
LINK SG CYS A 1 PT1 CPT A 502 1555 1555 2.25
LINK NE2 HIS A 439 PT1 CPT A 501 1555 1555 2.20
LINK SG CYS A 441 PT1 CPT A 501 1555 1555 2.25
LINK PT1 CPT A 501 O HOH A 777 1555 1555 2.23
SITE 1 AC1 6 HIS A 439 CYS A 441 TCE A 503 HOH A 735
SITE 2 AC1 6 HOH A 743 HOH A 777
SITE 1 AC2 2 CYS A 1 ASP A 422
SITE 1 AC3 6 LYS A 36 LYS A 74 LEU A 428 HIS A 429
SITE 2 AC3 6 HIS A 439 CPT A 501
SITE 1 AC4 8 ARG A 7 ARG A 18 ALA A 62 GLY A 63
SITE 2 AC4 8 ARG A 410 HOH A 601 HOH A 650 HOH A 724
CRYST1 57.269 64.051 37.167 90.00 90.00 90.00 P 21 21 2 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 0.017461 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015613 0.000000 0.00000
SCALE3 0.000000 0.000000 0.026906 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
