HEADER OXIDOREDUCTASE 23-JUL-10 3O38
TITLE CRYSTAL STRUCTURE OF A SHORT CHAIN DEHYDROGENASE FROM MYCOBACTERIUM
TITLE 2 SMEGMATIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SHORT CHAIN DEHYDROGENASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM SMEGMATIS;
SOURCE 3 ORGANISM_TAXID: 246196;
SOURCE 4 STRAIN: ATCC 700084 / MC(2)155;
SOURCE 5 GENE: MSMEG_6011;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: AVA0421
KEYWDS MYCOBACTERIUM, TUBERCULOSIS, ORTHOLOG FROM A NON-PATHOGENIC SPECIES,
KEYWDS 2 DEHYDROGENASE, STRUCTURAL GENOMICS, SEATTLE STRUCTURAL GENOMICS
KEYWDS 3 CENTER FOR INFECTIOUS DISEASE, SSGCID, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)
REVDAT 3 06-SEP-23 3O38 1 REMARK SEQADV LINK
REVDAT 2 22-APR-15 3O38 1 JRNL VERSN
REVDAT 1 11-AUG-10 3O38 0
JRNL AUTH L.BAUGH,I.PHAN,D.W.BEGLEY,M.C.CLIFTON,B.ARMOUR,D.M.DRANOW,
JRNL AUTH 2 B.M.TAYLOR,M.M.MURUTHI,J.ABENDROTH,J.W.FAIRMAN,D.FOX,
JRNL AUTH 3 S.H.DIETERICH,B.L.STAKER,A.S.GARDBERG,R.CHOI,S.N.HEWITT,
JRNL AUTH 4 A.J.NAPULI,J.MYERS,L.K.BARRETT,Y.ZHANG,M.FERRELL,E.MUNDT,
JRNL AUTH 5 K.THOMPKINS,N.TRAN,S.LYONS-ABBOTT,A.ABRAMOV,A.SEKAR,
JRNL AUTH 6 D.SERBZHINSKIY,D.LORIMER,G.W.BUCHKO,R.STACY,L.J.STEWART,
JRNL AUTH 7 T.E.EDWARDS,W.C.VAN VOORHIS,P.J.MYLER
JRNL TITL INCREASING THE STRUCTURAL COVERAGE OF TUBERCULOSIS DRUG
JRNL TITL 2 TARGETS.
JRNL REF TUBERCULOSIS (EDINB) V. 95 142 2015
JRNL REFN ISSN 1472-9792
JRNL PMID 25613812
JRNL DOI 10.1016/J.TUBE.2014.12.003
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 64451
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) : 0.165
REMARK 3 R VALUE (WORKING SET) : 0.162
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3265
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) : 1.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3746
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 80.87
REMARK 3 BIN R VALUE (WORKING SET) : 0.2140
REMARK 3 BIN FREE R VALUE SET COUNT : 190
REMARK 3 BIN FREE R VALUE : 0.2940
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7091
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 670
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.32
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.27
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.62000
REMARK 3 B22 (A**2) : -0.11000
REMARK 3 B33 (A**2) : 1.90000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.40000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.154
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.104
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.143
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.931
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7233 ; 0.015 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9854 ; 1.355 ; 1.945
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 979 ; 5.758 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 294 ;34.818 ;23.163
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1123 ;12.204 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 66 ;17.465 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1195 ; 0.092 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5444 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 4796 ; 0.764 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7635 ; 1.305 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2437 ; 2.218 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2210 ; 3.649 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A -10 A 9999
REMARK 3 ORIGIN FOR THE GROUP (A): 60.4937 36.8543 74.1212
REMARK 3 T TENSOR
REMARK 3 T11: 0.0635 T22: 0.0284
REMARK 3 T33: 0.0590 T12: -0.0035
REMARK 3 T13: 0.0072 T23: -0.0212
REMARK 3 L TENSOR
REMARK 3 L11: 0.7875 L22: 0.0620
REMARK 3 L33: 0.2524 L12: 0.1046
REMARK 3 L13: 0.0282 L23: -0.0539
REMARK 3 S TENSOR
REMARK 3 S11: 0.0147 S12: -0.0916 S13: 0.0632
REMARK 3 S21: -0.0269 S22: -0.0245 S23: 0.0130
REMARK 3 S31: 0.0159 S32: 0.0366 S33: 0.0098
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B -10 B 9999
REMARK 3 ORIGIN FOR THE GROUP (A): 26.9847 38.5197 71.1313
REMARK 3 T TENSOR
REMARK 3 T11: 0.0590 T22: 0.0250
REMARK 3 T33: 0.0989 T12: 0.0006
REMARK 3 T13: 0.0076 T23: -0.0070
REMARK 3 L TENSOR
REMARK 3 L11: 0.8352 L22: 0.0037
REMARK 3 L33: 0.1333 L12: -0.0470
REMARK 3 L13: -0.0320 L23: -0.0099
REMARK 3 S TENSOR
REMARK 3 S11: 0.0084 S12: -0.0602 S13: 0.1489
REMARK 3 S21: -0.0044 S22: 0.0105 S23: -0.0049
REMARK 3 S31: 0.0411 S32: -0.0427 S33: -0.0190
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C -10 C 9999
REMARK 3 ORIGIN FOR THE GROUP (A): 30.8429 35.1190 41.5991
REMARK 3 T TENSOR
REMARK 3 T11: 0.0570 T22: 0.1052
REMARK 3 T33: 0.0508 T12: -0.0121
REMARK 3 T13: -0.0160 T23: 0.0455
REMARK 3 L TENSOR
REMARK 3 L11: 0.6716 L22: 0.0393
REMARK 3 L33: 0.1086 L12: 0.0218
REMARK 3 L13: 0.1275 L23: 0.0548
REMARK 3 S TENSOR
REMARK 3 S11: -0.0193 S12: 0.2151 S13: 0.0506
REMARK 3 S21: 0.0262 S22: 0.0071 S23: 0.0210
REMARK 3 S31: 0.0394 S32: 0.0163 S33: 0.0122
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D -10 D 9999
REMARK 3 ORIGIN FOR THE GROUP (A): 63.4170 42.8328 45.0753
REMARK 3 T TENSOR
REMARK 3 T11: 0.0738 T22: 0.1191
REMARK 3 T33: 0.0421 T12: -0.0216
REMARK 3 T13: -0.0018 T23: 0.0629
REMARK 3 L TENSOR
REMARK 3 L11: 0.6118 L22: 0.1549
REMARK 3 L33: 0.1252 L12: 0.2861
REMARK 3 L13: -0.0775 L23: -0.0758
REMARK 3 S TENSOR
REMARK 3 S11: -0.0652 S12: 0.1814 S13: 0.1406
REMARK 3 S21: -0.0104 S22: 0.0529 S23: 0.0593
REMARK 3 S31: 0.0149 S32: 0.0633 S33: 0.0123
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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. U VALUES WITH TLS ADDED.
REMARK 4
REMARK 4 3O38 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JUL-10.
REMARK 100 THE DEPOSITION ID IS D_1000060608.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-JUL-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97946
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 64541
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.05500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.9200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 81.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.35500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1IY8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 53.4 MG/ML MYSMA00762BA1 PS00603
REMARK 280 AGAINST PACT B2, 0.1 M MIB BUFFER, 25% PEG 1500, PH 5.0, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 289K
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 37.86000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31020 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -106.0 KCAL/MOL
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 -3
REMARK 465 PRO A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 LYS A 206
REMARK 465 PHE A 207
REMARK 465 LEU A 208
REMARK 465 GLU A 209
REMARK 465 LYS A 210
REMARK 465 THR A 211
REMARK 465 SER A 212
REMARK 465 SER A 213
REMARK 465 SER A 214
REMARK 465 GLU A 215
REMARK 465 LEU A 216
REMARK 465 LEU A 217
REMARK 465 ASP A 218
REMARK 465 ARG A 219
REMARK 465 LEU A 220
REMARK 465 ALA A 221
REMARK 465 SER A 222
REMARK 465 GLY B -3
REMARK 465 PRO B -2
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 MET B 1
REMARK 465 ALA B 203
REMARK 465 ARG B 204
REMARK 465 HIS B 205
REMARK 465 LYS B 206
REMARK 465 PHE B 207
REMARK 465 LEU B 208
REMARK 465 GLU B 209
REMARK 465 LYS B 210
REMARK 465 THR B 211
REMARK 465 SER B 212
REMARK 465 SER B 213
REMARK 465 SER B 214
REMARK 465 GLU B 215
REMARK 465 LEU B 216
REMARK 465 LEU B 217
REMARK 465 ASP B 218
REMARK 465 ARG B 219
REMARK 465 LEU B 220
REMARK 465 ALA B 221
REMARK 465 SER B 222
REMARK 465 ASP B 223
REMARK 465 GLY C -3
REMARK 465 PRO C -2
REMARK 465 GLY C -1
REMARK 465 SER C 0
REMARK 465 ALA C 203
REMARK 465 ARG C 204
REMARK 465 HIS C 205
REMARK 465 LYS C 206
REMARK 465 PHE C 207
REMARK 465 LEU C 208
REMARK 465 GLU C 209
REMARK 465 LYS C 210
REMARK 465 THR C 211
REMARK 465 SER C 212
REMARK 465 SER C 213
REMARK 465 SER C 214
REMARK 465 GLU C 215
REMARK 465 LEU C 216
REMARK 465 LEU C 217
REMARK 465 ASP C 218
REMARK 465 ARG C 219
REMARK 465 LEU C 220
REMARK 465 ALA C 221
REMARK 465 SER C 222
REMARK 465 ASP C 223
REMARK 465 GLY D -3
REMARK 465 PRO D -2
REMARK 465 GLY D -1
REMARK 465 SER D 0
REMARK 465 MET D 1
REMARK 465 LYS D 206
REMARK 465 PHE D 207
REMARK 465 LEU D 208
REMARK 465 GLU D 209
REMARK 465 LYS D 210
REMARK 465 THR D 211
REMARK 465 SER D 212
REMARK 465 SER D 213
REMARK 465 SER D 214
REMARK 465 GLU D 215
REMARK 465 LEU D 216
REMARK 465 LEU D 217
REMARK 465 ASP D 218
REMARK 465 ARG D 219
REMARK 465 LEU D 220
REMARK 465 ALA D 221
REMARK 465 SER D 222
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 53 CG CD OE1 OE2
REMARK 470 ARG A 54 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 82 CG CD OE1 OE2
REMARK 470 ARG A 204 CG CD NE CZ NH1 NH2
REMARK 470 HIS A 205 CG ND1 CD2 CE1 NE2
REMARK 470 ASP A 223 CG OD1 OD2
REMARK 470 GLU B 5 CG CD OE1 OE2
REMARK 470 GLU B 82 CG CD OE1 OE2
REMARK 470 ILE B 202 CG1 CG2 CD1
REMARK 470 LYS C 8 CG CD CE NZ
REMARK 470 LYS C 17 CG CD CE NZ
REMARK 470 GLU C 53 CG CD OE1 OE2
REMARK 470 ARG C 54 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 82 CG CD OE1 OE2
REMARK 470 GLU C 119 CG CD OE1 OE2
REMARK 470 ASP C 147 CG OD1 OD2
REMARK 470 LYS D 8 CG CD CE NZ
REMARK 470 LYS D 17 CG CD CE NZ
REMARK 470 ARG D 54 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 70 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 82 CG CD OE1 OE2
REMARK 470 GLU D 119 CG CD OE1 OE2
REMARK 470 ARG D 204 CG CD NE CZ NH1 NH2
REMARK 470 ASP D 223 CG OD1 OD2
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 OD2 ASP A 118 O HOH A 634 2.16
REMARK 500 O HOH B 319 O HOH B 341 2.17
REMARK 500
REMARK 500 REMARK: NULL
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 D 162 NE - CZ - NH2 ANGL. DEV. = -3.1 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 LEU A 68 -123.77 -101.55
REMARK 500 ASP A 147 57.19 -107.66
REMARK 500 ALA A 156 -132.35 -95.80
REMARK 500 LEU B 68 -138.52 -104.02
REMARK 500 ALA B 105 133.89 -38.87
REMARK 500 ALA B 156 -130.18 -94.32
REMARK 500 SER B 157 148.68 -178.84
REMARK 500 HIS C 52 83.63 -67.05
REMARK 500 LEU C 68 -122.51 -100.49
REMARK 500 ALA C 105 123.80 -35.11
REMARK 500 ALA C 156 -132.63 -86.91
REMARK 500 SER C 157 148.43 -177.12
REMARK 500 LEU D 68 -128.92 -107.42
REMARK 500 ASP D 147 33.97 -92.79
REMARK 500 ALA D 156 -137.92 -94.47
REMARK 500
REMARK 500 REMARK: NULL
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 NA C 263 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN C 110 O
REMARK 620 2 THR C 111 OG1 72.0
REMARK 620 3 HOH C 301 O 91.7 70.9
REMARK 620 4 HOH C 370 O 89.3 151.4 88.8
REMARK 620 5 HOH C 544 O 159.1 87.9 76.0 106.9
REMARK 620 6 HOH C 545 O 80.2 101.6 170.5 96.0 110.2
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 NA C 263
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MYSMA.00762.B RELATED DB: TARGETDB
DBREF 3O38 A 1 262 UNP A0R4Z8 A0R4Z8_MYCS2 1 262
DBREF 3O38 B 1 262 UNP A0R4Z8 A0R4Z8_MYCS2 1 262
DBREF 3O38 C 1 262 UNP A0R4Z8 A0R4Z8_MYCS2 1 262
DBREF 3O38 D 1 262 UNP A0R4Z8 A0R4Z8_MYCS2 1 262
SEQADV 3O38 GLY A -3 UNP A0R4Z8 EXPRESSION TAG
SEQADV 3O38 PRO A -2 UNP A0R4Z8 EXPRESSION TAG
SEQADV 3O38 GLY A -1 UNP A0R4Z8 EXPRESSION TAG
SEQADV 3O38 SER A 0 UNP A0R4Z8 EXPRESSION TAG
SEQADV 3O38 GLY B -3 UNP A0R4Z8 EXPRESSION TAG
SEQADV 3O38 PRO B -2 UNP A0R4Z8 EXPRESSION TAG
SEQADV 3O38 GLY B -1 UNP A0R4Z8 EXPRESSION TAG
SEQADV 3O38 SER B 0 UNP A0R4Z8 EXPRESSION TAG
SEQADV 3O38 GLY C -3 UNP A0R4Z8 EXPRESSION TAG
SEQADV 3O38 PRO C -2 UNP A0R4Z8 EXPRESSION TAG
SEQADV 3O38 GLY C -1 UNP A0R4Z8 EXPRESSION TAG
SEQADV 3O38 SER C 0 UNP A0R4Z8 EXPRESSION TAG
SEQADV 3O38 GLY D -3 UNP A0R4Z8 EXPRESSION TAG
SEQADV 3O38 PRO D -2 UNP A0R4Z8 EXPRESSION TAG
SEQADV 3O38 GLY D -1 UNP A0R4Z8 EXPRESSION TAG
SEQADV 3O38 SER D 0 UNP A0R4Z8 EXPRESSION TAG
SEQRES 1 A 266 GLY PRO GLY SER MET ASN LEU SER GLU ALA PRO LYS GLU
SEQRES 2 A 266 ILE ASP GLY HIS GLY LEU LEU LYS GLY LYS VAL VAL LEU
SEQRES 3 A 266 VAL THR ALA ALA ALA GLY THR GLY ILE GLY SER THR THR
SEQRES 4 A 266 ALA ARG ARG ALA LEU LEU GLU GLY ALA ASP VAL VAL ILE
SEQRES 5 A 266 SER ASP TYR HIS GLU ARG ARG LEU GLY GLU THR ARG ASP
SEQRES 6 A 266 GLN LEU ALA ASP LEU GLY LEU GLY ARG VAL GLU ALA VAL
SEQRES 7 A 266 VAL CYS ASP VAL THR SER THR GLU ALA VAL ASP ALA LEU
SEQRES 8 A 266 ILE THR GLN THR VAL GLU LYS ALA GLY ARG LEU ASP VAL
SEQRES 9 A 266 LEU VAL ASN ASN ALA GLY LEU GLY GLY GLN THR PRO VAL
SEQRES 10 A 266 VAL ASP MET THR ASP GLU GLU TRP ASP ARG VAL LEU ASN
SEQRES 11 A 266 VAL THR LEU THR SER VAL MET ARG ALA THR ARG ALA ALA
SEQRES 12 A 266 LEU ARG TYR PHE ARG GLY VAL ASP HIS GLY GLY VAL ILE
SEQRES 13 A 266 VAL ASN ASN ALA SER VAL LEU GLY TRP ARG ALA GLN HIS
SEQRES 14 A 266 SER GLN SER HIS TYR ALA ALA ALA LYS ALA GLY VAL MET
SEQRES 15 A 266 ALA LEU THR ARG CYS SER ALA ILE GLU ALA VAL GLU PHE
SEQRES 16 A 266 GLY VAL ARG ILE ASN ALA VAL SER PRO SER ILE ALA ARG
SEQRES 17 A 266 HIS LYS PHE LEU GLU LYS THR SER SER SER GLU LEU LEU
SEQRES 18 A 266 ASP ARG LEU ALA SER ASP GLU ALA PHE GLY ARG ALA ALA
SEQRES 19 A 266 GLU PRO TRP GLU VAL ALA ALA THR ILE ALA PHE LEU ALA
SEQRES 20 A 266 SER ASP TYR SER SER TYR MET THR GLY GLU VAL VAL SER
SEQRES 21 A 266 VAL SER SER GLN ARG ALA
SEQRES 1 B 266 GLY PRO GLY SER MET ASN LEU SER GLU ALA PRO LYS GLU
SEQRES 2 B 266 ILE ASP GLY HIS GLY LEU LEU LYS GLY LYS VAL VAL LEU
SEQRES 3 B 266 VAL THR ALA ALA ALA GLY THR GLY ILE GLY SER THR THR
SEQRES 4 B 266 ALA ARG ARG ALA LEU LEU GLU GLY ALA ASP VAL VAL ILE
SEQRES 5 B 266 SER ASP TYR HIS GLU ARG ARG LEU GLY GLU THR ARG ASP
SEQRES 6 B 266 GLN LEU ALA ASP LEU GLY LEU GLY ARG VAL GLU ALA VAL
SEQRES 7 B 266 VAL CYS ASP VAL THR SER THR GLU ALA VAL ASP ALA LEU
SEQRES 8 B 266 ILE THR GLN THR VAL GLU LYS ALA GLY ARG LEU ASP VAL
SEQRES 9 B 266 LEU VAL ASN ASN ALA GLY LEU GLY GLY GLN THR PRO VAL
SEQRES 10 B 266 VAL ASP MET THR ASP GLU GLU TRP ASP ARG VAL LEU ASN
SEQRES 11 B 266 VAL THR LEU THR SER VAL MET ARG ALA THR ARG ALA ALA
SEQRES 12 B 266 LEU ARG TYR PHE ARG GLY VAL ASP HIS GLY GLY VAL ILE
SEQRES 13 B 266 VAL ASN ASN ALA SER VAL LEU GLY TRP ARG ALA GLN HIS
SEQRES 14 B 266 SER GLN SER HIS TYR ALA ALA ALA LYS ALA GLY VAL MET
SEQRES 15 B 266 ALA LEU THR ARG CYS SER ALA ILE GLU ALA VAL GLU PHE
SEQRES 16 B 266 GLY VAL ARG ILE ASN ALA VAL SER PRO SER ILE ALA ARG
SEQRES 17 B 266 HIS LYS PHE LEU GLU LYS THR SER SER SER GLU LEU LEU
SEQRES 18 B 266 ASP ARG LEU ALA SER ASP GLU ALA PHE GLY ARG ALA ALA
SEQRES 19 B 266 GLU PRO TRP GLU VAL ALA ALA THR ILE ALA PHE LEU ALA
SEQRES 20 B 266 SER ASP TYR SER SER TYR MET THR GLY GLU VAL VAL SER
SEQRES 21 B 266 VAL SER SER GLN ARG ALA
SEQRES 1 C 266 GLY PRO GLY SER MET ASN LEU SER GLU ALA PRO LYS GLU
SEQRES 2 C 266 ILE ASP GLY HIS GLY LEU LEU LYS GLY LYS VAL VAL LEU
SEQRES 3 C 266 VAL THR ALA ALA ALA GLY THR GLY ILE GLY SER THR THR
SEQRES 4 C 266 ALA ARG ARG ALA LEU LEU GLU GLY ALA ASP VAL VAL ILE
SEQRES 5 C 266 SER ASP TYR HIS GLU ARG ARG LEU GLY GLU THR ARG ASP
SEQRES 6 C 266 GLN LEU ALA ASP LEU GLY LEU GLY ARG VAL GLU ALA VAL
SEQRES 7 C 266 VAL CYS ASP VAL THR SER THR GLU ALA VAL ASP ALA LEU
SEQRES 8 C 266 ILE THR GLN THR VAL GLU LYS ALA GLY ARG LEU ASP VAL
SEQRES 9 C 266 LEU VAL ASN ASN ALA GLY LEU GLY GLY GLN THR PRO VAL
SEQRES 10 C 266 VAL ASP MET THR ASP GLU GLU TRP ASP ARG VAL LEU ASN
SEQRES 11 C 266 VAL THR LEU THR SER VAL MET ARG ALA THR ARG ALA ALA
SEQRES 12 C 266 LEU ARG TYR PHE ARG GLY VAL ASP HIS GLY GLY VAL ILE
SEQRES 13 C 266 VAL ASN ASN ALA SER VAL LEU GLY TRP ARG ALA GLN HIS
SEQRES 14 C 266 SER GLN SER HIS TYR ALA ALA ALA LYS ALA GLY VAL MET
SEQRES 15 C 266 ALA LEU THR ARG CYS SER ALA ILE GLU ALA VAL GLU PHE
SEQRES 16 C 266 GLY VAL ARG ILE ASN ALA VAL SER PRO SER ILE ALA ARG
SEQRES 17 C 266 HIS LYS PHE LEU GLU LYS THR SER SER SER GLU LEU LEU
SEQRES 18 C 266 ASP ARG LEU ALA SER ASP GLU ALA PHE GLY ARG ALA ALA
SEQRES 19 C 266 GLU PRO TRP GLU VAL ALA ALA THR ILE ALA PHE LEU ALA
SEQRES 20 C 266 SER ASP TYR SER SER TYR MET THR GLY GLU VAL VAL SER
SEQRES 21 C 266 VAL SER SER GLN ARG ALA
SEQRES 1 D 266 GLY PRO GLY SER MET ASN LEU SER GLU ALA PRO LYS GLU
SEQRES 2 D 266 ILE ASP GLY HIS GLY LEU LEU LYS GLY LYS VAL VAL LEU
SEQRES 3 D 266 VAL THR ALA ALA ALA GLY THR GLY ILE GLY SER THR THR
SEQRES 4 D 266 ALA ARG ARG ALA LEU LEU GLU GLY ALA ASP VAL VAL ILE
SEQRES 5 D 266 SER ASP TYR HIS GLU ARG ARG LEU GLY GLU THR ARG ASP
SEQRES 6 D 266 GLN LEU ALA ASP LEU GLY LEU GLY ARG VAL GLU ALA VAL
SEQRES 7 D 266 VAL CYS ASP VAL THR SER THR GLU ALA VAL ASP ALA LEU
SEQRES 8 D 266 ILE THR GLN THR VAL GLU LYS ALA GLY ARG LEU ASP VAL
SEQRES 9 D 266 LEU VAL ASN ASN ALA GLY LEU GLY GLY GLN THR PRO VAL
SEQRES 10 D 266 VAL ASP MET THR ASP GLU GLU TRP ASP ARG VAL LEU ASN
SEQRES 11 D 266 VAL THR LEU THR SER VAL MET ARG ALA THR ARG ALA ALA
SEQRES 12 D 266 LEU ARG TYR PHE ARG GLY VAL ASP HIS GLY GLY VAL ILE
SEQRES 13 D 266 VAL ASN ASN ALA SER VAL LEU GLY TRP ARG ALA GLN HIS
SEQRES 14 D 266 SER GLN SER HIS TYR ALA ALA ALA LYS ALA GLY VAL MET
SEQRES 15 D 266 ALA LEU THR ARG CYS SER ALA ILE GLU ALA VAL GLU PHE
SEQRES 16 D 266 GLY VAL ARG ILE ASN ALA VAL SER PRO SER ILE ALA ARG
SEQRES 17 D 266 HIS LYS PHE LEU GLU LYS THR SER SER SER GLU LEU LEU
SEQRES 18 D 266 ASP ARG LEU ALA SER ASP GLU ALA PHE GLY ARG ALA ALA
SEQRES 19 D 266 GLU PRO TRP GLU VAL ALA ALA THR ILE ALA PHE LEU ALA
SEQRES 20 D 266 SER ASP TYR SER SER TYR MET THR GLY GLU VAL VAL SER
SEQRES 21 D 266 VAL SER SER GLN ARG ALA
HET NA C 263 1
HETNAM NA SODIUM ION
FORMUL 5 NA NA 1+
FORMUL 6 HOH *670(H2 O)
HELIX 1 1 GLY A 30 GLU A 42 1 13
HELIX 2 2 HIS A 52 ASP A 65 1 14
HELIX 3 3 SER A 80 GLY A 96 1 17
HELIX 4 4 PRO A 112 MET A 116 5 5
HELIX 5 5 THR A 117 LEU A 129 1 13
HELIX 6 6 LEU A 129 GLY A 145 1 17
HELIX 7 7 SER A 157 TRP A 161 5 5
HELIX 8 8 GLN A 167 VAL A 189 1 23
HELIX 9 9 GLU A 231 SER A 244 1 14
HELIX 10 10 ASP A 245 SER A 248 5 4
HELIX 11 11 GLY B 30 GLU B 42 1 13
HELIX 12 12 HIS B 52 LEU B 66 1 15
HELIX 13 13 SER B 80 GLY B 96 1 17
HELIX 14 14 PRO B 112 MET B 116 5 5
HELIX 15 15 THR B 117 LEU B 129 1 13
HELIX 16 16 LEU B 129 GLY B 145 1 17
HELIX 17 17 SER B 157 TRP B 161 5 5
HELIX 18 18 GLN B 167 VAL B 189 1 23
HELIX 19 19 GLU B 231 SER B 244 1 14
HELIX 20 20 ASP B 245 SER B 248 5 4
HELIX 21 21 GLY C 30 GLU C 42 1 13
HELIX 22 22 HIS C 52 ASP C 65 1 14
HELIX 23 23 SER C 80 GLY C 96 1 17
HELIX 24 24 PRO C 112 MET C 116 5 5
HELIX 25 25 THR C 117 LEU C 129 1 13
HELIX 26 26 LEU C 129 VAL C 146 1 18
HELIX 27 27 SER C 157 TRP C 161 5 5
HELIX 28 28 GLN C 167 VAL C 189 1 23
HELIX 29 29 GLU C 231 SER C 244 1 14
HELIX 30 30 ASP C 245 SER C 248 5 4
HELIX 31 31 GLY D 30 GLU D 42 1 13
HELIX 32 32 HIS D 52 ASP D 65 1 14
HELIX 33 33 SER D 80 GLY D 96 1 17
HELIX 34 34 PRO D 112 MET D 116 5 5
HELIX 35 35 THR D 117 LEU D 129 1 13
HELIX 36 36 LEU D 129 GLY D 145 1 17
HELIX 37 37 SER D 157 TRP D 161 5 5
HELIX 38 38 GLN D 167 VAL D 189 1 23
HELIX 39 39 GLU D 231 SER D 244 1 14
HELIX 40 40 ASP D 245 SER D 248 5 4
SHEET 1 A 7 VAL A 71 VAL A 75 0
SHEET 2 A 7 ASP A 45 ASP A 50 1 N ILE A 48 O GLU A 72
SHEET 3 A 7 VAL A 20 VAL A 23 1 N VAL A 21 O ASP A 45
SHEET 4 A 7 VAL A 100 ASN A 103 1 O VAL A 100 N LEU A 22
SHEET 5 A 7 GLY A 150 ASN A 155 1 O VAL A 153 N LEU A 101
SHEET 6 A 7 VAL A 193 PRO A 200 1 O ASN A 196 N ASN A 154
SHEET 7 A 7 VAL A 254 VAL A 257 1 O VAL A 255 N SER A 199
SHEET 1 B 7 VAL B 71 VAL B 75 0
SHEET 2 B 7 ASP B 45 ASP B 50 1 N ILE B 48 O GLU B 72
SHEET 3 B 7 VAL B 20 VAL B 23 1 N VAL B 21 O ASP B 45
SHEET 4 B 7 VAL B 100 ASN B 103 1 O VAL B 100 N LEU B 22
SHEET 5 B 7 GLY B 150 ASN B 155 1 O VAL B 153 N LEU B 101
SHEET 6 B 7 VAL B 193 PRO B 200 1 O ARG B 194 N ILE B 152
SHEET 7 B 7 VAL B 254 VAL B 257 1 O VAL B 255 N ALA B 197
SHEET 1 C 7 VAL C 71 VAL C 75 0
SHEET 2 C 7 ASP C 45 ASP C 50 1 N ILE C 48 O GLU C 72
SHEET 3 C 7 VAL C 20 VAL C 23 1 N VAL C 21 O VAL C 47
SHEET 4 C 7 VAL C 100 ASN C 103 1 O VAL C 102 N LEU C 22
SHEET 5 C 7 GLY C 150 ASN C 155 1 O VAL C 153 N LEU C 101
SHEET 6 C 7 VAL C 193 PRO C 200 1 O ASN C 196 N ASN C 154
SHEET 7 C 7 VAL C 254 VAL C 257 1 O VAL C 255 N SER C 199
SHEET 1 D 7 VAL D 71 VAL D 75 0
SHEET 2 D 7 ASP D 45 ASP D 50 1 N ILE D 48 O GLU D 72
SHEET 3 D 7 VAL D 20 VAL D 23 1 N VAL D 21 O ASP D 45
SHEET 4 D 7 VAL D 100 ASN D 103 1 O VAL D 100 N LEU D 22
SHEET 5 D 7 GLY D 150 ASN D 155 1 O VAL D 153 N LEU D 101
SHEET 6 D 7 VAL D 193 PRO D 200 1 O ASN D 196 N ASN D 154
SHEET 7 D 7 VAL D 254 VAL D 257 1 O VAL D 255 N SER D 199
LINK O GLN C 110 NA NA C 263 1555 1555 2.43
LINK OG1 THR C 111 NA NA C 263 1555 1555 2.66
LINK NA NA C 263 O HOH C 301 1555 1555 2.64
LINK NA NA C 263 O HOH C 370 1555 1555 2.37
LINK NA NA C 263 O HOH C 544 1555 1555 2.31
LINK NA NA C 263 O HOH C 545 1555 1555 2.24
CISPEP 1 VAL A 257 SER A 258 0 -3.11
CISPEP 2 VAL B 257 SER B 258 0 1.45
CISPEP 3 VAL C 257 SER C 258 0 2.48
CISPEP 4 VAL D 257 SER D 258 0 5.18
SITE 1 AC1 6 GLN C 110 THR C 111 HOH C 301 HOH C 370
SITE 2 AC1 6 HOH C 544 HOH C 545
CRYST1 77.810 75.720 80.030 90.00 102.71 90.00 P 1 21 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 0.012852 0.000000 0.002898 0.00000
SCALE2 0.000000 0.013207 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012809 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
