HEADER HYDROLASE/RNA 04-JAN-15 4S0Q
TITLE THE X-RAY STRUCTURE OF THE ADDUCT FORMED IN THE REACTION BETWEEN
TITLE 2 BOVINE PANCREATIC RIBONUCLEASE AND CARBOPLATIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBONUCLEASE PANCREATIC;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: RNASE 1, RNASE A;
COMPND 5 EC: 3.1.27.5;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: BOVINE,COW,DOMESTIC CATTLE,DOMESTIC COW;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 GENE: RNASE1, RNS1
KEYWDS RIBONUCLEASE, RNA CLEAVAGE, HYDROLASE-RNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.MERLINO
REVDAT 4 20-SEP-23 4S0Q 1 REMARK
REVDAT 3 24-FEB-16 4S0Q 1 JRNL
REVDAT 2 16-DEC-15 4S0Q 1 JRNL
REVDAT 1 18-NOV-15 4S0Q 0
JRNL AUTH L.MESSORI,T.MARZO,A.MERLINO
JRNL TITL INTERACTIONS OF CARBOPLATIN AND OXALIPLATIN WITH PROTEINS:
JRNL TITL 2 INSIGHTS FROM X-RAY STRUCTURES AND MASS SPECTROMETRY STUDIES
JRNL TITL 3 OF THEIR RIBONUCLEASE A ADDUCTS.
JRNL REF J.INORG.BIOCHEM. V. 153 136 2015
JRNL REFN ISSN 0162-0134
JRNL PMID 26239545
JRNL DOI 10.1016/J.JINORGBIO.2015.07.011
REMARK 2
REMARK 2 RESOLUTION. 2.09 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.09
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 72.71
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 13380
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.208
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.262
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 709
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.09
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 909
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.16
REMARK 3 BIN R VALUE (WORKING SET) : 0.2610
REMARK 3 BIN FREE R VALUE SET COUNT : 55
REMARK 3 BIN FREE R VALUE : 0.3160
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1844
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 104
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.84
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.17000
REMARK 3 B22 (A**2) : 0.48000
REMARK 3 B33 (A**2) : 0.68000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.16000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.259
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.214
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.171
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.663
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.945
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.912
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1884 ; 0.016 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1708 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2542 ; 1.762 ; 1.926
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3948 ; 0.846 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 234 ; 6.895 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 88 ;36.511 ;25.227
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 330 ;15.188 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;10.612 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 278 ; 0.103 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2164 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 436 ; 0.001 ; 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): 948 ; 2.744 ; 3.631
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 947 ; 2.744 ; 3.631
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1178 ; 3.991 ; 5.424
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1179 ; 3.990 ; 5.424
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 933 ; 3.219 ; 3.916
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 933 ; 3.219 ; 3.916
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1364 ; 4.656 ; 5.734
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2260 ; 6.465 ;29.136
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2233 ; 6.454 ;29.110
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4S0Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JAN-15.
REMARK 100 THE DEPOSITION ID IS D_1000088033.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14095
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.090
REMARK 200 RESOLUTION RANGE LOW (A) : 72.710
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.12400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
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: NULL
REMARK 200 STARTING MODEL: PDB CODE 1JVT, CHAIN A WITHOUT WATER MOLECULES AND
REMARK 200 LIGANDS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS OF THE RNASE A-CARBOPLATIN
REMARK 280 ADDUCT HAVE BEEN OBTAINED BY SOAKING EXPERIMENTS WHERE PRE-GROWN
REMARK 280 MONOCLINIC PROTEIN CRYSTALS WERE INCUBATED WITH AN EXCESS OF THE
REMARK 280 PLATINUM DRUG (AT A PROTEIN TO PLATINUM RATIO 1:10). CRYSTALS OF
REMARK 280 RNASE A WERE GROWN BY HANGING-DROP VAPOR MIXING 1 L OF RNASE A
REMARK 280 AT 20 MG ML-1 WITH EQUAL VOLUMES OF RESERVOIR SOLUTION
REMARK 280 CONTAINING 20% PEG4000 AND 20 MM SODIUM CITRATE BUFFER PH 5.0 AT
REMARK 280 298 K. TWO WEEKS AFTER THEIR APPEARANCE, CRYSTALS WERE SOAKED
REMARK 280 FOR FOUR DAYS IN A SOLUTION OF CARBOPLATIN DISSOLVED IN 10 L OF
REMARK 280 RESERVOIR. AT THE FINAL, PT DRUG:PROTEIN CONCENTRATIONS WERE IN
REMARK 280 10:1 RATIO., VAPOR DIFFUSION, HANGING DROP
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 50.26050
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 16.24950
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 50.26050
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 16.24950
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 THR A 17
REMARK 465 SER A 18
REMARK 465 ALA A 19
REMARK 465 ALA A 20
REMARK 465 SER A 21
REMARK 465 THR B 17
REMARK 465 SER B 18
REMARK 465 ALA B 19
REMARK 465 ALA B 20
REMARK 465 SER B 21
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 ALA A 52 O HOH A 311 2.17
REMARK 500 O HOH B 336 O HOH B 348 2.18
REMARK 500 NZ LYS B 104 O HOH B 338 2.19
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 HIS A 48 70.35 -101.61
REMARK 500 GLN A 60 -131.50 -103.08
REMARK 500 ASN A 71 42.04 -95.88
REMARK 500 GLU B 2 126.88 -18.87
REMARK 500 HIS B 48 54.62 -115.28
REMARK 500 GLN B 60 -127.28 -111.25
REMARK 500 ASN B 94 63.95 -104.52
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 QPT A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE QPT B 201
DBREF 4S0Q A 1 124 UNP P61823 RNAS1_BOVIN 27 150
DBREF 4S0Q B 1 124 UNP P61823 RNAS1_BOVIN 27 150
SEQRES 1 A 124 LYS GLU THR ALA ALA ALA LYS PHE GLU ARG GLN HIS MET
SEQRES 2 A 124 ASP SER SER THR SER ALA ALA SER SER SER ASN TYR CYS
SEQRES 3 A 124 ASN GLN MET MET LYS SER ARG ASN LEU THR LYS ASP ARG
SEQRES 4 A 124 CYS LYS PRO VAL ASN THR PHE VAL HIS GLU SER LEU ALA
SEQRES 5 A 124 ASP VAL GLN ALA VAL CYS SER GLN LYS ASN VAL ALA CYS
SEQRES 6 A 124 LYS ASN GLY GLN THR ASN CYS TYR GLN SER TYR SER THR
SEQRES 7 A 124 MET SER ILE THR ASP CYS ARG GLU THR GLY SER SER LYS
SEQRES 8 A 124 TYR PRO ASN CYS ALA TYR LYS THR THR GLN ALA ASN LYS
SEQRES 9 A 124 HIS ILE ILE VAL ALA CYS GLU GLY ASN PRO TYR VAL PRO
SEQRES 10 A 124 VAL HIS PHE ASP ALA SER VAL
SEQRES 1 B 124 LYS GLU THR ALA ALA ALA LYS PHE GLU ARG GLN HIS MET
SEQRES 2 B 124 ASP SER SER THR SER ALA ALA SER SER SER ASN TYR CYS
SEQRES 3 B 124 ASN GLN MET MET LYS SER ARG ASN LEU THR LYS ASP ARG
SEQRES 4 B 124 CYS LYS PRO VAL ASN THR PHE VAL HIS GLU SER LEU ALA
SEQRES 5 B 124 ASP VAL GLN ALA VAL CYS SER GLN LYS ASN VAL ALA CYS
SEQRES 6 B 124 LYS ASN GLY GLN THR ASN CYS TYR GLN SER TYR SER THR
SEQRES 7 B 124 MET SER ILE THR ASP CYS ARG GLU THR GLY SER SER LYS
SEQRES 8 B 124 TYR PRO ASN CYS ALA TYR LYS THR THR GLN ALA ASN LYS
SEQRES 9 B 124 HIS ILE ILE VAL ALA CYS GLU GLY ASN PRO TYR VAL PRO
SEQRES 10 B 124 VAL HIS PHE ASP ALA SER VAL
HET QPT A 201 1
HET QPT B 201 1
HETNAM QPT CARBOPLATIN
FORMUL 3 QPT 2(C6 H12 N2 O4 PT 2+)
FORMUL 5 HOH *104(H2 O)
HELIX 1 1 THR A 3 MET A 13 1 11
HELIX 2 2 ASN A 24 ARG A 33 1 10
HELIX 3 3 SER A 50 ALA A 56 1 7
HELIX 4 4 VAL A 57 GLN A 60 5 4
HELIX 5 5 THR B 3 MET B 13 1 11
HELIX 6 6 ASN B 24 ARG B 33 1 10
HELIX 7 7 SER B 50 VAL B 57 1 8
HELIX 8 8 CYS B 58 GLN B 60 5 3
SHEET 1 A 5 VAL A 43 VAL A 47 0
SHEET 2 A 5 MET A 79 GLU A 86 -1 O CYS A 84 N ASN A 44
SHEET 3 A 5 TYR A 97 GLU A 111 -1 O LYS A 98 N ARG A 85
SHEET 4 A 5 CYS A 72 GLN A 74 -1 N TYR A 73 O VAL A 108
SHEET 5 A 5 LYS A 61 VAL A 63 -1 N VAL A 63 O CYS A 72
SHEET 1 B 4 VAL A 43 VAL A 47 0
SHEET 2 B 4 MET A 79 GLU A 86 -1 O CYS A 84 N ASN A 44
SHEET 3 B 4 TYR A 97 GLU A 111 -1 O LYS A 98 N ARG A 85
SHEET 4 B 4 VAL A 116 VAL A 124 -1 O VAL A 118 N ALA A 109
SHEET 1 C 5 VAL B 43 VAL B 47 0
SHEET 2 C 5 MET B 79 GLU B 86 -1 O CYS B 84 N ASN B 44
SHEET 3 C 5 TYR B 97 GLU B 111 -1 O ALA B 102 N ILE B 81
SHEET 4 C 5 CYS B 72 GLN B 74 -1 N TYR B 73 O VAL B 108
SHEET 5 C 5 LYS B 61 VAL B 63 -1 N VAL B 63 O CYS B 72
SHEET 1 D 4 VAL B 43 VAL B 47 0
SHEET 2 D 4 MET B 79 GLU B 86 -1 O CYS B 84 N ASN B 44
SHEET 3 D 4 TYR B 97 GLU B 111 -1 O ALA B 102 N ILE B 81
SHEET 4 D 4 VAL B 116 VAL B 124 -1 O VAL B 118 N ALA B 109
SSBOND 1 CYS A 26 CYS A 84 1555 1555 2.07
SSBOND 2 CYS A 40 CYS A 95 1555 1555 2.03
SSBOND 3 CYS A 58 CYS A 110 1555 1555 2.03
SSBOND 4 CYS A 65 CYS A 72 1555 1555 2.00
SSBOND 5 CYS B 26 CYS B 84 1555 1555 2.05
SSBOND 6 CYS B 40 CYS B 95 1555 1555 2.01
SSBOND 7 CYS B 58 CYS B 110 1555 1555 2.07
SSBOND 8 CYS B 65 CYS B 72 1555 1555 2.01
LINK SD MET A 29 PT1 QPT A 201 1555 1555 2.19
LINK SD MET B 29 PT1 QPT B 201 1555 1555 2.34
CISPEP 1 TYR A 92 PRO A 93 0 11.88
CISPEP 2 ASN A 113 PRO A 114 0 10.81
CISPEP 3 TYR B 92 PRO B 93 0 2.78
CISPEP 4 ASN B 113 PRO B 114 0 3.50
SITE 1 AC1 2 MET A 29 HOH A 340
SITE 1 AC2 2 TYR B 25 MET B 29
CRYST1 100.521 32.499 72.711 90.00 89.59 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 0.009948 0.000000 -0.000071 0.00000
SCALE2 0.000000 0.030770 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013753 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
