HEADER TRANSFERASE 11-MAR-13 4JKS
TITLE CRYSTAL STRUCTURE OF PROBABLE SUGAR KINASE PROTEIN FROM RHIZOBIUM ETLI
TITLE 2 CFN 42 COMPLEXED WITH DMSO, NYSGRC TARGET 14306
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE SUGAR KINASE PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHIZOBIUM ETLI;
SOURCE 3 ORGANISM_TAXID: 347834;
SOURCE 4 STRAIN: CFN 42;
SOURCE 5 GENE: RHE_CH00135;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)CODON+RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: BC-PSGX3(BC)
KEYWDS STRUCTURAL GENOMICS, PROTEIN STRUCTURE INITIATIVE, NYSGRC, PSI-
KEYWDS 2 BIOLOGY, NEW YORK STRUCTURAL GENOMICS RESEARCH CONSORTIUM,
KEYWDS 3 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.N.MALASHKEVICH,R.BHOSLE,R.TORO,B.HILLERICH,A.GIZZI,S.GARFORTH,
AUTHOR 2 A.KAR,M.K.CHAN,J.LAFLUER,H.PATEL,B.MATIKAINEN,S.CHAMALA,S.LIM,
AUTHOR 3 A.CELIKGIL,G.VILLEGAS,B.EVANS,J.LOVE,A.FISER,K.KHAFIZOV,R.SEIDEL,
AUTHOR 4 J.B.BONANNO,S.C.ALMO,NEW YORK STRUCTURAL GENOMICS RESEARCH
AUTHOR 5 CONSORTIUM (NYSGRC)
REVDAT 3 06-DEC-23 4JKS 1 REMARK
REVDAT 2 20-SEP-23 4JKS 1 REMARK SEQADV LINK
REVDAT 1 27-MAR-13 4JKS 0
JRNL AUTH V.N.MALASHKEVICH,R.BHOSLE,R.TORO,B.HILLERICH,A.GIZZI,
JRNL AUTH 2 S.GARFORTH,A.KAR,M.K.CHAN,J.LAFLUER,H.PATEL,B.MATIKAINEN,
JRNL AUTH 3 S.CHAMALA,S.LIM,A.CELIKGIL,G.VILLEGAS,B.EVANS,J.LOVE,
JRNL AUTH 4 A.FISER,K.KHAFIZOV,R.SEIDEL,J.B.BONANNO,S.C.ALMO
JRNL TITL CRYSTAL STRUCTURE OF PROBABLE SUGAR KINASE PROTEIN FROM
JRNL TITL 2 RHIZOBIUM ETLI CFN 42 COMPLEXED WITH DMSO, NYSGRC TARGET
JRNL TITL 3 14306
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.51 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) : 1.51
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.22
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 107348
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) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.202
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5359
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) : 1.51
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.55
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7430
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.71
REMARK 3 BIN R VALUE (WORKING SET) : 0.1570
REMARK 3 BIN FREE R VALUE SET COUNT : 381
REMARK 3 BIN FREE R VALUE : 0.1890
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5008
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 54
REMARK 3 SOLVENT ATOMS : 616
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.68
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.33000
REMARK 3 B22 (A**2) : -0.26000
REMARK 3 B33 (A**2) : 0.59000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.019
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.016
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.022
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.197
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.972
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.961
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5325 ; 0.007 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7242 ; 1.175 ; 1.982
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 714 ; 5.292 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 256 ;37.112 ;24.023
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 831 ;12.746 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 46 ;12.677 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 812 ; 0.077 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4121 ; 0.005 ; 0.021
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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): 5325 ; 2.592 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 195 ;22.238 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 5642 ;11.741 ; 5.000
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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A -1 A 328
REMARK 3 RESIDUE RANGE : A 401 A 403
REMARK 3 ORIGIN FOR THE GROUP (A): 13.7346 -7.5369 -20.4648
REMARK 3 T TENSOR
REMARK 3 T11: 0.0112 T22: 0.0156
REMARK 3 T33: 0.0012 T12: -0.0025
REMARK 3 T13: -0.0024 T23: 0.0009
REMARK 3 L TENSOR
REMARK 3 L11: 0.1781 L22: 0.1872
REMARK 3 L33: 0.1280 L12: 0.0177
REMARK 3 L13: -0.0313 L23: -0.0398
REMARK 3 S TENSOR
REMARK 3 S11: 0.0057 S12: -0.0049 S13: -0.0070
REMARK 3 S21: 0.0032 S22: 0.0016 S23: 0.0053
REMARK 3 S31: 0.0129 S32: 0.0102 S33: -0.0073
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B -1 B 328
REMARK 3 RESIDUE RANGE : B 401 B 403
REMARK 3 ORIGIN FOR THE GROUP (A): 26.7203 29.3683 -20.3165
REMARK 3 T TENSOR
REMARK 3 T11: 0.0116 T22: 0.0166
REMARK 3 T33: 0.0013 T12: -0.0014
REMARK 3 T13: 0.0032 T23: -0.0013
REMARK 3 L TENSOR
REMARK 3 L11: 0.1564 L22: 0.2837
REMARK 3 L33: 0.1531 L12: 0.0428
REMARK 3 L13: 0.0540 L23: 0.0675
REMARK 3 S TENSOR
REMARK 3 S11: 0.0030 S12: -0.0199 S13: 0.0083
REMARK 3 S21: 0.0063 S22: 0.0005 S23: 0.0030
REMARK 3 S31: -0.0133 S32: -0.0148 S33: -0.0035
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 USED IF PRESENT IN
REMARK 3 THE INPUT U VALUES : RESIDUAL ONLY
REMARK 4
REMARK 4 4JKS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-MAR-13.
REMARK 100 THE DEPOSITION ID IS D_1000078170.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-FEB-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.075
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 107497
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.510
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.300
REMARK 200 R MERGE (I) : 0.05700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.51
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.20
REMARK 200 R MERGE FOR SHELL (I) : 0.79700
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: 4E3A
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM ACETATE, 0.1M
REMARK 280 BIS:TRIS:HCL, PH 6.5,25% PEG3350, SOAKED IN 13% DMSO, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 40.41500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 46.21450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.58250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 46.21450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 40.41500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.58250
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 9.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 MSE A -23
REMARK 465 HIS A -22
REMARK 465 HIS A -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 SER A -16
REMARK 465 SER A -15
REMARK 465 GLY A -14
REMARK 465 VAL A -13
REMARK 465 ASP A -12
REMARK 465 LEU A -11
REMARK 465 GLY A -10
REMARK 465 THR A -9
REMARK 465 GLU A -8
REMARK 465 ASN A -7
REMARK 465 LEU A -6
REMARK 465 TYR A -5
REMARK 465 PHE A -4
REMARK 465 GLN A -3
REMARK 465 SER A -2
REMARK 465 MSE B -23
REMARK 465 HIS B -22
REMARK 465 HIS B -21
REMARK 465 HIS B -20
REMARK 465 HIS B -19
REMARK 465 HIS B -18
REMARK 465 HIS B -17
REMARK 465 SER B -16
REMARK 465 SER B -15
REMARK 465 GLY B -14
REMARK 465 VAL B -13
REMARK 465 ASP B -12
REMARK 465 LEU B -11
REMARK 465 GLY B -10
REMARK 465 THR B -9
REMARK 465 GLU B -8
REMARK 465 ASN B -7
REMARK 465 LEU B -6
REMARK 465 TYR B -5
REMARK 465 PHE B -4
REMARK 465 GLN B -3
REMARK 465 SER B -2
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 LYS A 104 64.90 -107.47
REMARK 500 SER A 186 -54.13 72.68
REMARK 500 SER A 245 -124.08 50.97
REMARK 500 ASP A 270 112.90 -164.47
REMARK 500 SER B 186 -54.73 74.59
REMARK 500 SER B 245 -123.11 51.16
REMARK 500 ASP B 270 110.95 -164.69
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 ADN A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADN B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 403
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4E3A RELATED DB: PDB
REMARK 900 RELATED ID: NYSGRC-014306 RELATED DB: TARGETTRACK
REMARK 900 RELATED ID: 4JKU RELATED DB: PDB
DBREF 4JKS A -1 328 UNP Q2KDX6 Q2KDX6_RHIEC 1 330
DBREF 4JKS B -1 328 UNP Q2KDX6 Q2KDX6_RHIEC 1 330
SEQADV 4JKS MSE A -23 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4JKS HIS A -22 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4JKS HIS A -21 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4JKS HIS A -20 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4JKS HIS A -19 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4JKS HIS A -18 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4JKS HIS A -17 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4JKS SER A -16 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4JKS SER A -15 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4JKS GLY A -14 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4JKS VAL A -13 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4JKS ASP A -12 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4JKS LEU A -11 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4JKS GLY A -10 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4JKS THR A -9 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4JKS GLU A -8 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4JKS ASN A -7 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4JKS LEU A -6 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4JKS TYR A -5 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4JKS PHE A -4 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4JKS GLN A -3 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4JKS SER A -2 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4JKS MSE B -23 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4JKS HIS B -22 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4JKS HIS B -21 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4JKS HIS B -20 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4JKS HIS B -19 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4JKS HIS B -18 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4JKS HIS B -17 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4JKS SER B -16 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4JKS SER B -15 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4JKS GLY B -14 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4JKS VAL B -13 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4JKS ASP B -12 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4JKS LEU B -11 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4JKS GLY B -10 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4JKS THR B -9 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4JKS GLU B -8 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4JKS ASN B -7 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4JKS LEU B -6 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4JKS TYR B -5 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4JKS PHE B -4 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4JKS GLN B -3 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4JKS SER B -2 UNP Q2KDX6 EXPRESSION TAG
SEQRES 1 A 352 MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 352 GLY THR GLU ASN LEU TYR PHE GLN SER MSE THR ARG PHE
SEQRES 3 A 352 ASP VAL LEU THR VAL GLY ASN ALA ILE VAL ASP ILE ILE
SEQRES 4 A 352 SER ARG CYS ASN ASP GLN PHE LEU ILE ASP ASN GLN ILE
SEQRES 5 A 352 THR LYS ALA ALA MSE ASN LEU ILE ASP ALA GLU ARG ALA
SEQRES 6 A 352 GLU LEU LEU TYR SER ARG MSE GLY PRO ALA LEU GLU ALA
SEQRES 7 A 352 SER GLY GLY SER ALA GLY ASN THR ALA ALA GLY VAL ALA
SEQRES 8 A 352 ASN LEU GLY GLY LYS ALA ALA TYR PHE GLY ASN VAL ALA
SEQRES 9 A 352 ALA ASP GLN LEU GLY ASP ILE PHE THR HIS ASP ILE ARG
SEQRES 10 A 352 ALA GLN GLY VAL HIS TYR GLN THR LYS PRO LYS GLY ALA
SEQRES 11 A 352 PHE PRO PRO THR ALA ARG SER MSE ILE PHE VAL THR GLU
SEQRES 12 A 352 ASP GLY GLU ARG SER MSE ASN THR TYR LEU GLY ALA CYS
SEQRES 13 A 352 VAL GLU LEU GLY PRO GLU ASP VAL GLU ALA ASP VAL VAL
SEQRES 14 A 352 ALA ASP ALA LYS VAL THR TYR PHE GLU GLY TYR LEU TRP
SEQRES 15 A 352 ASP PRO PRO ARG ALA LYS GLU ALA ILE LEU ASP CYS ALA
SEQRES 16 A 352 ARG ILE ALA HIS GLN HIS GLY ARG GLU MSE SER MSE THR
SEQRES 17 A 352 LEU SER ASP SER PHE CYS VAL ASP ARG TYR ARG GLY GLU
SEQRES 18 A 352 PHE LEU ASP LEU MSE ARG SER GLY LYS VAL ASP ILE VAL
SEQRES 19 A 352 PHE ALA ASN ARG GLN GLU ALA LEU SER LEU TYR GLN THR
SEQRES 20 A 352 ASP ASP PHE GLU GLU ALA LEU ASN ARG ILE ALA ALA ASP
SEQRES 21 A 352 CYS LYS ILE ALA ALA VAL THR MSE SER GLU ASN GLY ALA
SEQRES 22 A 352 VAL ILE LEU LYS GLY ARG GLU ARG TYR TYR VAL ASN ALA
SEQRES 23 A 352 ILE ARG ILE ARG GLU VAL VAL ASP THR THR GLY ALA GLY
SEQRES 24 A 352 ASP LEU PHE ALA SER GLY PHE LEU TYR GLY TYR THR GLN
SEQRES 25 A 352 GLY ARG SER LEU GLU ASP CYS GLY LYS LEU GLY CYS LEU
SEQRES 26 A 352 ALA ALA GLY ILE VAL ILE GLN GLN ILE GLY PRO ARG PRO
SEQRES 27 A 352 MSE THR SER LEU SER GLU ALA ALA LYS GLN ALA GLY LEU
SEQRES 28 A 352 ILE
SEQRES 1 B 352 MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 B 352 GLY THR GLU ASN LEU TYR PHE GLN SER MSE THR ARG PHE
SEQRES 3 B 352 ASP VAL LEU THR VAL GLY ASN ALA ILE VAL ASP ILE ILE
SEQRES 4 B 352 SER ARG CYS ASN ASP GLN PHE LEU ILE ASP ASN GLN ILE
SEQRES 5 B 352 THR LYS ALA ALA MSE ASN LEU ILE ASP ALA GLU ARG ALA
SEQRES 6 B 352 GLU LEU LEU TYR SER ARG MSE GLY PRO ALA LEU GLU ALA
SEQRES 7 B 352 SER GLY GLY SER ALA GLY ASN THR ALA ALA GLY VAL ALA
SEQRES 8 B 352 ASN LEU GLY GLY LYS ALA ALA TYR PHE GLY ASN VAL ALA
SEQRES 9 B 352 ALA ASP GLN LEU GLY ASP ILE PHE THR HIS ASP ILE ARG
SEQRES 10 B 352 ALA GLN GLY VAL HIS TYR GLN THR LYS PRO LYS GLY ALA
SEQRES 11 B 352 PHE PRO PRO THR ALA ARG SER MSE ILE PHE VAL THR GLU
SEQRES 12 B 352 ASP GLY GLU ARG SER MSE ASN THR TYR LEU GLY ALA CYS
SEQRES 13 B 352 VAL GLU LEU GLY PRO GLU ASP VAL GLU ALA ASP VAL VAL
SEQRES 14 B 352 ALA ASP ALA LYS VAL THR TYR PHE GLU GLY TYR LEU TRP
SEQRES 15 B 352 ASP PRO PRO ARG ALA LYS GLU ALA ILE LEU ASP CYS ALA
SEQRES 16 B 352 ARG ILE ALA HIS GLN HIS GLY ARG GLU MSE SER MSE THR
SEQRES 17 B 352 LEU SER ASP SER PHE CYS VAL ASP ARG TYR ARG GLY GLU
SEQRES 18 B 352 PHE LEU ASP LEU MSE ARG SER GLY LYS VAL ASP ILE VAL
SEQRES 19 B 352 PHE ALA ASN ARG GLN GLU ALA LEU SER LEU TYR GLN THR
SEQRES 20 B 352 ASP ASP PHE GLU GLU ALA LEU ASN ARG ILE ALA ALA ASP
SEQRES 21 B 352 CYS LYS ILE ALA ALA VAL THR MSE SER GLU ASN GLY ALA
SEQRES 22 B 352 VAL ILE LEU LYS GLY ARG GLU ARG TYR TYR VAL ASN ALA
SEQRES 23 B 352 ILE ARG ILE ARG GLU VAL VAL ASP THR THR GLY ALA GLY
SEQRES 24 B 352 ASP LEU PHE ALA SER GLY PHE LEU TYR GLY TYR THR GLN
SEQRES 25 B 352 GLY ARG SER LEU GLU ASP CYS GLY LYS LEU GLY CYS LEU
SEQRES 26 B 352 ALA ALA GLY ILE VAL ILE GLN GLN ILE GLY PRO ARG PRO
SEQRES 27 B 352 MSE THR SER LEU SER GLU ALA ALA LYS GLN ALA GLY LEU
SEQRES 28 B 352 ILE
MODRES 4JKS MSE A -1 MET SELENOMETHIONINE
MODRES 4JKS MSE A 33 MET SELENOMETHIONINE
MODRES 4JKS MSE A 48 MET SELENOMETHIONINE
MODRES 4JKS MSE A 114 MET SELENOMETHIONINE
MODRES 4JKS MSE A 125 MET SELENOMETHIONINE
MODRES 4JKS MSE A 181 MET SELENOMETHIONINE
MODRES 4JKS MSE A 183 MET SELENOMETHIONINE
MODRES 4JKS MSE A 202 MET SELENOMETHIONINE
MODRES 4JKS MSE A 244 MET SELENOMETHIONINE
MODRES 4JKS MSE A 315 MET SELENOMETHIONINE
MODRES 4JKS MSE B -1 MET SELENOMETHIONINE
MODRES 4JKS MSE B 33 MET SELENOMETHIONINE
MODRES 4JKS MSE B 48 MET SELENOMETHIONINE
MODRES 4JKS MSE B 114 MET SELENOMETHIONINE
MODRES 4JKS MSE B 125 MET SELENOMETHIONINE
MODRES 4JKS MSE B 181 MET SELENOMETHIONINE
MODRES 4JKS MSE B 183 MET SELENOMETHIONINE
MODRES 4JKS MSE B 202 MET SELENOMETHIONINE
MODRES 4JKS MSE B 244 MET SELENOMETHIONINE
MODRES 4JKS MSE B 315 MET SELENOMETHIONINE
HET MSE A -1 8
HET MSE A 33 8
HET MSE A 48 8
HET MSE A 114 8
HET MSE A 125 8
HET MSE A 181 8
HET MSE A 183 8
HET MSE A 202 8
HET MSE A 244 8
HET MSE A 315 8
HET MSE B -1 8
HET MSE B 33 8
HET MSE B 48 8
HET MSE B 114 8
HET MSE B 125 8
HET MSE B 181 8
HET MSE B 183 8
HET MSE B 202 8
HET MSE B 244 8
HET MSE B 315 8
HET ADN A 401 19
HET DMS A 402 4
HET DMS A 403 4
HET ADN B 401 19
HET DMS B 402 4
HET DMS B 403 4
HETNAM MSE SELENOMETHIONINE
HETNAM ADN ADENOSINE
HETNAM DMS DIMETHYL SULFOXIDE
FORMUL 1 MSE 20(C5 H11 N O2 SE)
FORMUL 3 ADN 2(C10 H13 N5 O4)
FORMUL 4 DMS 4(C2 H6 O S)
FORMUL 9 HOH *616(H2 O)
HELIX 1 1 ASN A 19 ASN A 26 1 8
HELIX 2 2 ASP A 37 MSE A 48 1 12
HELIX 3 3 GLY A 57 GLY A 70 1 14
HELIX 4 4 ASP A 82 GLN A 95 1 14
HELIX 5 5 LEU A 129 LEU A 135 5 7
HELIX 6 6 GLY A 136 VAL A 140 5 5
HELIX 7 7 GLU A 141 ASP A 147 1 7
HELIX 8 8 TYR A 156 ASP A 159 5 4
HELIX 9 9 ARG A 162 HIS A 177 1 16
HELIX 10 10 ASP A 187 SER A 204 1 18
HELIX 11 11 ARG A 214 TYR A 221 1 8
HELIX 12 12 ASP A 225 CYS A 237 1 13
HELIX 13 13 SER A 245 ASN A 247 5 3
HELIX 14 14 GLY A 273 GLN A 288 1 16
HELIX 15 15 SER A 291 ILE A 307 1 17
HELIX 16 16 SER A 317 ALA A 325 1 9
HELIX 17 17 ASN B 19 ASN B 26 1 8
HELIX 18 18 ASP B 37 MSE B 48 1 12
HELIX 19 19 GLY B 57 GLY B 70 1 14
HELIX 20 20 ASP B 82 GLN B 95 1 14
HELIX 21 21 LEU B 129 LEU B 135 5 7
HELIX 22 22 GLY B 136 VAL B 140 5 5
HELIX 23 23 GLU B 141 ASP B 147 1 7
HELIX 24 24 TYR B 156 ASP B 159 5 4
HELIX 25 25 ARG B 162 HIS B 177 1 16
HELIX 26 26 ASP B 187 SER B 204 1 18
HELIX 27 27 ARG B 214 GLN B 222 1 9
HELIX 28 28 ASP B 225 CYS B 237 1 13
HELIX 29 29 SER B 245 ASN B 247 5 3
HELIX 30 30 GLY B 273 GLN B 288 1 16
HELIX 31 31 SER B 291 ILE B 307 1 17
HELIX 32 32 SER B 317 ALA B 325 1 9
SHEET 1 A 9 HIS A 98 TYR A 99 0
SHEET 2 A 9 ALA A 73 PHE A 76 1 N ALA A 73 O HIS A 98
SHEET 3 A 9 PHE A 2 VAL A 7 1 N THR A 6 O ALA A 74
SHEET 4 A 9 ALA A 148 GLU A 154 1 O TYR A 152 N LEU A 5
SHEET 5 A 9 GLU A 180 THR A 184 1 O SER A 182 N THR A 151
SHEET 6 A 9 ILE A 209 ASN A 213 1 O PHE A 211 N MSE A 183
SHEET 7 A 9 ILE A 239 THR A 243 1 O ALA A 241 N VAL A 210
SHEET 8 A 9 ALA A 249 LYS A 253 -1 O LEU A 252 N ALA A 240
SHEET 9 A 9 GLU A 256 VAL A 260 -1 O VAL A 260 N ALA A 249
SHEET 1 B 5 MSE A 33 LEU A 35 0
SHEET 2 B 5 ARG A 123 TYR A 128 1 O MSE A 125 N ASN A 34
SHEET 3 B 5 ALA A 111 VAL A 117 -1 N MSE A 114 O ASN A 126
SHEET 4 B 5 ILE A 11 ARG A 17 1 N ILE A 14 O ILE A 115
SHEET 5 B 5 LEU A 52 SER A 55 -1 O LEU A 52 N ILE A 15
SHEET 1 C 9 HIS B 98 TYR B 99 0
SHEET 2 C 9 ALA B 73 PHE B 76 1 N TYR B 75 O HIS B 98
SHEET 3 C 9 PHE B 2 VAL B 7 1 N THR B 6 O ALA B 74
SHEET 4 C 9 ALA B 148 GLU B 154 1 O TYR B 152 N LEU B 5
SHEET 5 C 9 GLU B 180 THR B 184 1 O SER B 182 N THR B 151
SHEET 6 C 9 ILE B 209 ASN B 213 1 O PHE B 211 N MSE B 183
SHEET 7 C 9 ILE B 239 THR B 243 1 O ALA B 241 N VAL B 210
SHEET 8 C 9 ALA B 249 LYS B 253 -1 O LEU B 252 N ALA B 240
SHEET 9 C 9 GLU B 256 VAL B 260 -1 O VAL B 260 N ALA B 249
SHEET 1 D 5 MSE B 33 LEU B 35 0
SHEET 2 D 5 ARG B 123 TYR B 128 1 O MSE B 125 N ASN B 34
SHEET 3 D 5 ALA B 111 VAL B 117 -1 N MSE B 114 O ASN B 126
SHEET 4 D 5 ILE B 11 ARG B 17 1 N ILE B 14 O ILE B 115
SHEET 5 D 5 LEU B 52 SER B 55 -1 O LEU B 52 N ILE B 15
LINK C MSE A -1 N THR A 0 1555 1555 1.33
LINK C ALA A 32 N MSE A 33 1555 1555 1.33
LINK C MSE A 33 N ASN A 34 1555 1555 1.33
LINK C ARG A 47 N MSE A 48 1555 1555 1.33
LINK C MSE A 48 N GLY A 49 1555 1555 1.33
LINK C SER A 113 N MSE A 114 1555 1555 1.34
LINK C MSE A 114 N ILE A 115 1555 1555 1.33
LINK C SER A 124 N MSE A 125 1555 1555 1.33
LINK C MSE A 125 N ASN A 126 1555 1555 1.33
LINK C GLU A 180 N MSE A 181 1555 1555 1.33
LINK C MSE A 181 N SER A 182 1555 1555 1.33
LINK C SER A 182 N MSE A 183 1555 1555 1.33
LINK C MSE A 183 N THR A 184 1555 1555 1.33
LINK C LEU A 201 N MSE A 202 1555 1555 1.33
LINK C MSE A 202 N ARG A 203 1555 1555 1.33
LINK C THR A 243 N MSE A 244 1555 1555 1.33
LINK C MSE A 244 N SER A 245 1555 1555 1.33
LINK C PRO A 314 N MSE A 315 1555 1555 1.33
LINK C MSE A 315 N THR A 316 1555 1555 1.34
LINK C MSE B -1 N THR B 0 1555 1555 1.33
LINK C ALA B 32 N MSE B 33 1555 1555 1.33
LINK C MSE B 33 N ASN B 34 1555 1555 1.34
LINK C ARG B 47 N MSE B 48 1555 1555 1.33
LINK C MSE B 48 N GLY B 49 1555 1555 1.33
LINK C SER B 113 N MSE B 114 1555 1555 1.34
LINK C MSE B 114 N ILE B 115 1555 1555 1.33
LINK C SER B 124 N MSE B 125 1555 1555 1.33
LINK C MSE B 125 N ASN B 126 1555 1555 1.33
LINK C GLU B 180 N MSE B 181 1555 1555 1.33
LINK C MSE B 181 N SER B 182 1555 1555 1.33
LINK C SER B 182 N MSE B 183 1555 1555 1.33
LINK C MSE B 183 N THR B 184 1555 1555 1.32
LINK C LEU B 201 N MSE B 202 1555 1555 1.33
LINK C MSE B 202 N ARG B 203 1555 1555 1.33
LINK C THR B 243 N MSE B 244 1555 1555 1.33
LINK C MSE B 244 N SER B 245 1555 1555 1.33
LINK C PRO B 314 N MSE B 315 1555 1555 1.33
LINK C MSE B 315 N THR B 316 1555 1555 1.33
CISPEP 1 PHE A 107 PRO A 108 0 -2.13
CISPEP 2 PHE B 107 PRO B 108 0 -1.44
CISPEP 3 PHE B 107 PRO B 108 0 -0.47
SITE 1 AC1 19 ASN A 9 ILE A 11 ASP A 13 MSE A 33
SITE 2 AC1 19 GLY A 56 GLY A 57 SER A 58 ASN A 61
SITE 3 AC1 19 MSE A 125 THR A 127 GLU A 154 TYR A 156
SITE 4 AC1 19 THR A 272 ASP A 276 PRO A 312 HOH A 504
SITE 5 AC1 19 HOH A 515 HOH A 543 HOH A 699
SITE 1 AC2 6 ILE A 14 ALA A 41 TYR A 45 ARG A 112
SITE 2 AC2 6 DMS A 403 HOH A 628
SITE 1 AC3 5 ALA A 38 GLU A 42 ARG A 112 DMS A 402
SITE 2 AC3 5 HOH A 704
SITE 1 AC4 19 ASN B 9 ILE B 11 ASP B 13 MSE B 33
SITE 2 AC4 19 GLY B 56 GLY B 57 SER B 58 ASN B 61
SITE 3 AC4 19 MSE B 125 THR B 127 GLU B 154 TYR B 156
SITE 4 AC4 19 GLY B 273 ASP B 276 PRO B 312 HOH B 510
SITE 5 AC4 19 HOH B 525 HOH B 544 HOH B 691
SITE 1 AC5 4 GLU B 42 ARG B 112 DMS B 403 HOH B 703
SITE 1 AC6 6 ILE B 14 ALA B 41 GLU B 42 TYR B 45
SITE 2 AC6 6 ARG B 112 DMS B 402
CRYST1 80.830 91.165 92.429 90.00 90.00 90.00 P 21 21 21 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 0.012372 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010969 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010819 0.00000
HETATM 1 N MSE A -1 35.115 -24.415 -21.180 1.00 41.48 N
ANISOU 1 N MSE A -1 5015 4732 6014 1171 557 -720 N
HETATM 2 CA MSE A -1 34.905 -22.933 -21.233 1.00 41.18 C
ANISOU 2 CA MSE A -1 4246 4914 6485 1213 225 365 C
HETATM 3 C MSE A -1 34.221 -22.559 -22.519 1.00 39.07 C
ANISOU 3 C MSE A -1 3931 4990 5921 966 571 182 C
HETATM 4 O MSE A -1 34.509 -23.124 -23.579 1.00 38.19 O
ANISOU 4 O MSE A -1 4991 3565 5954 453 -312 9 O
HETATM 5 CB MSE A -1 36.226 -22.167 -21.074 1.00 49.45 C
ANISOU 5 CB MSE A -1 5260 6276 7253 144 358 -118 C
HETATM 6 CG MSE A -1 37.351 -22.697 -21.961 1.00 51.30 C
ANISOU 6 CG MSE A -1 5563 7608 6320 250 620 275 C
HETATM 7 SE MSE A -1 38.890 -21.462 -21.986 1.00 52.29 SE
ANISOU 7 SE MSE A -1 5257 9393 5216 122 419 1362 SE
HETATM 8 CE MSE A -1 39.651 -22.159 -23.657 1.00 30.29 C
ANISOU 8 CE MSE A -1 3012 5278 3217 -547 -1167 2488 C
(ATOM LINES ARE NOT SHOWN.)
END