HEADER HYDROLASE 22-SEP-16 5LXW
TITLE ATOMIC RESOLUTION X-RAY CRYSTAL STRUCTURE OF CISPLATIN BOUND TO HEN
TITLE 2 EGG WHITE LYSOZYME STORED FOR 5 YEARS ON THE SHELF
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYSOZYME C;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: 1,4-BETA-N-ACETYLMURAMIDASE C,ALLERGEN GAL D IV;
COMPND 5 EC: 3.2.1.17
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031
KEYWDS CISPLATIN LYSOZYME CHEMICAL EQUILIBRIUM, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.R.HELLIWELL
REVDAT 2 17-JAN-24 5LXW 1 LINK
REVDAT 1 05-OCT-16 5LXW 0
JRNL AUTH J.R.HELLIWELL,T.SIMON
JRNL TITL ATOMIC RESOLUTION X-RAY CRYSTAL STRUCTURE OF CISPLATIN BOUND
JRNL TITL 2 TO HEN EGG WHITE LYSOZYME STORED FOR 5 YEARS 'ON THE SHELF'
JRNL REF ZENODO 2016
JRNL DOI 10.5281/ZENODO.155068
REMARK 2
REMARK 2 RESOLUTION. 1.00 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.39
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 87.8
REMARK 3 NUMBER OF REFLECTIONS : 57620
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.230
REMARK 3 FREE R VALUE TEST SET COUNT : 3013
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 27.3962 - 2.8011 0.82 2515 151 0.1707 0.2055
REMARK 3 2 2.8011 - 2.2236 0.85 2500 122 0.1668 0.1603
REMARK 3 3 2.2236 - 1.9426 0.88 2533 136 0.1528 0.1864
REMARK 3 4 1.9426 - 1.7650 0.89 2549 139 0.1490 0.1833
REMARK 3 5 1.7650 - 1.6386 0.90 2544 152 0.1484 0.1683
REMARK 3 6 1.6386 - 1.5420 0.91 2564 136 0.1496 0.1597
REMARK 3 7 1.5420 - 1.4647 0.92 2599 132 0.1544 0.1846
REMARK 3 8 1.4647 - 1.4010 0.93 2618 161 0.1559 0.1744
REMARK 3 9 1.4010 - 1.3470 0.92 2576 158 0.1629 0.1989
REMARK 3 10 1.3470 - 1.3006 0.93 2622 152 0.1800 0.2256
REMARK 3 11 1.3006 - 1.2599 0.94 2621 124 0.1823 0.2330
REMARK 3 12 1.2599 - 1.2239 0.94 2676 141 0.1906 0.2160
REMARK 3 13 1.2239 - 1.1917 0.94 2633 152 0.2007 0.2593
REMARK 3 14 1.1917 - 1.1626 0.94 2648 131 0.2137 0.2306
REMARK 3 15 1.1626 - 1.1362 0.94 2590 168 0.2404 0.2697
REMARK 3 16 1.1362 - 1.1120 0.93 2607 133 0.2751 0.3122
REMARK 3 17 1.1120 - 1.0897 0.91 2517 146 0.2886 0.3551
REMARK 3 18 1.0897 - 1.0692 0.87 2422 135 0.3474 0.4261
REMARK 3 19 1.0692 - 1.0501 0.85 2382 115 0.3564 0.3699
REMARK 3 20 1.0501 - 1.0323 0.79 2197 136 0.3537 0.4059
REMARK 3 21 1.0323 - 1.0156 0.73 2034 114 0.3661 0.3956
REMARK 3 22 1.0156 - 1.0000 0.59 1660 79 0.3659 0.3638
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) : 0.140
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.930
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 11.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.40
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 : 0.012 1142
REMARK 3 ANGLE : 1.274 1550
REMARK 3 CHIRALITY : 0.078 156
REMARK 3 PLANARITY : 0.006 211
REMARK 3 DIHEDRAL : 12.413 423
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BOTH PHENIX_REFINE (AFONINE ET AL 2012)
REMARK 3 AND CCP4 REFMAC (MURSHUDOV ET AL 1997) WERE USED FOR THE MODEL
REMARK 3 REFINEMENT, TAKING ADVANTAGE OF THE ADVANTAGES OF EACH. COOT
REMARK 3 (EMSLEY AND COWTAN 2004) WAS USED TO INSPECT THE MOLECULAR MODEL
REMARK 3 AND THE ELECTRON DENSITY MAPS.
REMARK 4
REMARK 4 5LXW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-SEP-16.
REMARK 100 THE DEPOSITION ID IS D_1200001539.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-SEP-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.92819
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57620
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.000
REMARK 200 RESOLUTION RANGE LOW (A) : 27.390
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.0
REMARK 200 DATA REDUNDANCY : 8.100
REMARK 200 R MERGE (I) : 0.07100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 1.86900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.500
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: 4G4A
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HEN EGG WHITE LYSOZYME (49MG, IE
REMARK 280 3.2MM), CISPLATIN (3MG, IE 10MM), 462.5 MICROLITRES OF 0.04 M
REMARK 280 SODIUM ACETATE, 462.5 MICROLITRES OF 10% SODIUM CHLORIDE, AND
REMARK 280 WITH 7.5% DMSO (75 MICROLITRES IE 1MM), PH 4.7, BATCH
REMARK 280 CRYSTALLISATION METHOD AND ROOM TEMPERATURE (295K). THE
REMARK 280 CRYSTALLISATION POT WAS KEPT FOR FIVE YEARS., BATCH MODE
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 18.92000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 39.68500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 39.68500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 28.38000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 39.68500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 39.68500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 9.46000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 39.68500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 39.68500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 28.38000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 39.68500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 39.68500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 9.46000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 18.92000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 6570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -124.0 KCAL/MOL
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 388 LIES ON A SPECIAL POSITION.
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 301 O HOH A 386 2.00
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 408 DISTANCE = 5.83 ANGSTROMS
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 PT A 204 PT
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG A 14 NH2
REMARK 620 2 HIS A 15 NE2 93.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 PT A 205 PT
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 15 ND1
REMARK 620 2 NH3 A 209 N 161.4
REMARK 620 3 NH3 A 210 N 89.2 87.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 203 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 60 O
REMARK 620 2 CYS A 64 O 87.6
REMARK 620 3 SER A 72 OG 90.8 166.8
REMARK 620 4 ARG A 73 O 96.1 92.8 100.3
REMARK 620 5 HOH A 351 O 172.9 97.7 83.0 88.3
REMARK 620 6 HOH A 356 O 98.6 88.7 78.6 165.3 77.0
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 DMS A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PT A 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PT A 205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 206
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PT A 207
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 208
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NH3 A 209
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NH3 A 210
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 211
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 212
DBREF 5LXW A 1 129 UNP P00698 LYSC_CHICK 19 147
SEQRES 1 A 129 LYS VAL PHE GLY ARG CYS GLU LEU ALA ALA ALA MET LYS
SEQRES 2 A 129 ARG HIS GLY LEU ASP ASN TYR ARG GLY TYR SER LEU GLY
SEQRES 3 A 129 ASN TRP VAL CYS ALA ALA LYS PHE GLU SER ASN PHE ASN
SEQRES 4 A 129 THR GLN ALA THR ASN ARG ASN THR ASP GLY SER THR ASP
SEQRES 5 A 129 TYR GLY ILE LEU GLN ILE ASN SER ARG TRP TRP CYS ASN
SEQRES 6 A 129 ASP GLY ARG THR PRO GLY SER ARG ASN LEU CYS ASN ILE
SEQRES 7 A 129 PRO CYS SER ALA LEU LEU SER SER ASP ILE THR ALA SER
SEQRES 8 A 129 VAL ASN CYS ALA LYS LYS ILE VAL SER ASP GLY ASN GLY
SEQRES 9 A 129 MET ASN ALA TRP VAL ALA TRP ARG ASN ARG CYS LYS GLY
SEQRES 10 A 129 THR ASP VAL GLN ALA TRP ILE ARG GLY CYS ARG LEU
HET DMS A 201 10
HET CL A 202 1
HET NA A 203 1
HET PT A 204 1
HET PT A 205 1
HET CL A 206 1
HET PT A 207 1
HET CL A 208 1
HET NH3 A 209 4
HET NH3 A 210 4
HET CL A 211 1
HET CL A 212 1
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM CL CHLORIDE ION
HETNAM NA SODIUM ION
HETNAM PT PLATINUM (II) ION
HETNAM NH3 AMMONIA
FORMUL 2 DMS C2 H6 O S
FORMUL 3 CL 5(CL 1-)
FORMUL 4 NA NA 1+
FORMUL 5 PT 3(PT 2+)
FORMUL 10 NH3 2(H3 N)
FORMUL 14 HOH *108(H2 O)
HELIX 1 AA1 GLY A 4 HIS A 15 1 12
HELIX 2 AA2 ASN A 19 TYR A 23 5 5
HELIX 3 AA3 SER A 24 ASN A 37 1 14
HELIX 4 AA4 PRO A 79 SER A 85 5 7
HELIX 5 AA5 ILE A 88 SER A 100 1 13
HELIX 6 AA6 ASN A 103 ALA A 107 5 5
HELIX 7 AA7 TRP A 108 CYS A 115 1 8
HELIX 8 AA8 ASP A 119 ARG A 125 5 7
SHEET 1 AA1 3 THR A 43 ARG A 45 0
SHEET 2 AA1 3 THR A 51 TYR A 53 -1 O ASP A 52 N ASN A 44
SHEET 3 AA1 3 ILE A 58 ASN A 59 -1 O ILE A 58 N TYR A 53
SSBOND 1 CYS A 6 CYS A 127 1555 1555 2.03
SSBOND 2 CYS A 30 CYS A 115 1555 1555 2.10
SSBOND 3 CYS A 64 CYS A 80 1555 1555 2.07
SSBOND 4 CYS A 76 CYS A 94 1555 1555 2.05
LINK NH2 ARG A 14 PT PT A 204 1555 1555 2.01
LINK NH1 ARG A 14 PT PT A 207 1555 1555 2.29
LINK NE2 HIS A 15 PT PT A 204 1555 1555 2.43
LINK ND1 HIS A 15 PT PT A 205 1555 1555 2.14
LINK O SER A 60 NA NA A 203 1555 1555 2.34
LINK O CYS A 64 NA NA A 203 1555 1555 2.45
LINK OG SER A 72 NA NA A 203 1555 1555 2.54
LINK O ARG A 73 NA NA A 203 1555 1555 2.45
LINK NA NA A 203 O HOH A 351 1555 1555 2.46
LINK NA NA A 203 O HOH A 356 1555 1555 2.46
LINK PT PT A 205 N NH3 A 209 1555 1555 2.00
LINK PT PT A 205 N NH3 A 210 1555 1555 1.93
SITE 1 AC1 6 GLN A 57 ILE A 58 ASN A 59 TRP A 63
SITE 2 AC1 6 ALA A 107 HOH A 332
SITE 1 AC2 2 TYR A 23 ASN A 113
SITE 1 AC3 6 SER A 60 CYS A 64 SER A 72 ARG A 73
SITE 2 AC3 6 HOH A 351 HOH A 356
SITE 1 AC4 3 ARG A 14 HIS A 15 PT A 207
SITE 1 AC5 4 HIS A 15 CL A 206 NH3 A 209 NH3 A 210
SITE 1 AC6 5 HIS A 15 THR A 89 ASN A 93 PT A 205
SITE 2 AC6 5 NH3 A 209
SITE 1 AC7 3 ARG A 14 HIS A 15 PT A 204
SITE 1 AC8 3 SER A 24 GLY A 26 GLN A 121
SITE 1 AC9 3 PT A 205 CL A 206 NH3 A 210
SITE 1 AD1 3 HIS A 15 PT A 205 NH3 A 209
SITE 1 AD2 4 GLY A 67 ARG A 68 THR A 69 SER A 72
SITE 1 AD3 3 ASN A 44 ARG A 45 HOH A 349
CRYST1 79.370 79.370 37.840 90.00 90.00 90.00 P 43 21 2 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 0.012599 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012599 0.000000 0.00000
SCALE3 0.000000 0.000000 0.026427 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
