HEADER HYDROLASE 15-APR-16 5JCV
TITLE SORTASE B FROM LISTERIA MONOCYTOGENES.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LMO2181 PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LISTERIA MONOCYTOGENES SEROVAR 1/2A (STRAIN
SOURCE 3 ATCC BAA-679 / EGD-E);
SOURCE 4 ORGANISM_TAXID: 169963;
SOURCE 5 STRAIN: ATCC BAA-679 / EGD-E;
SOURCE 6 GENE: LMO2181;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PMCSG53
KEYWDS SORTASE, STRUCTURAL GENOMICS, CENTER FOR STRUCTURAL GENOMICS OF
KEYWDS 2 INFECTIOUS DISEASES, CSGID, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.OSIPIUK,M.ZHOU,S.GRIMSHAW,W.F.ANDERSON,A.JOACHIMIAK,CENTER FOR
AUTHOR 2 STRUCTURAL GENOMICS OF INFECTIOUS DISEASES (CSGID)
REVDAT 3 11-DEC-19 5JCV 1 REMARK
REVDAT 2 20-SEP-17 5JCV 1 REMARK
REVDAT 1 27-APR-16 5JCV 0
JRNL AUTH J.OSIPIUK,M.ZHOU,S.GRIMSHAW,W.F.ANDERSON,A.JOACHIMIAK,
JRNL AUTH 2 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES
JRNL AUTH 3 (CSGID)
JRNL TITL SORTASE B FROM LISTERIA MONOCYTOGENES.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.23 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0069
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.23
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.60
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 13369
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) : 0.209
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 683
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) : 2.23
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.29
REMARK 3 REFLECTION IN BIN (WORKING SET) : 958
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.72
REMARK 3 BIN R VALUE (WORKING SET) : 0.2850
REMARK 3 BIN FREE R VALUE SET COUNT : 45
REMARK 3 BIN FREE R VALUE : 0.2980
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1452
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 22
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 65.89
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.21000
REMARK 3 B22 (A**2) : 0.21000
REMARK 3 B33 (A**2) : -0.41000
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): 0.211
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.189
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.156
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.423
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
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): 1498 ; 0.013 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 1383 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2026 ; 1.560 ; 1.964
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3193 ; 0.795 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 177 ; 7.014 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 79 ;33.775 ;24.937
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 260 ;16.210 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 6 ;10.264 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 221 ; 0.099 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1683 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 351 ; 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): 702 ; 3.178 ; 4.309
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 701 ; 3.177 ; 4.307
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 875 ; 4.645 ; 6.439
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): 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 : 1
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 63 A 502
REMARK 3 ORIGIN FOR THE GROUP (A): 17.2656 -1.8639 67.2407
REMARK 3 T TENSOR
REMARK 3 T11: 0.0701 T22: 0.4001
REMARK 3 T33: 0.0550 T12: -0.0855
REMARK 3 T13: 0.0174 T23: -0.0752
REMARK 3 L TENSOR
REMARK 3 L11: 0.5364 L22: 1.3363
REMARK 3 L33: 2.3883 L12: 0.0243
REMARK 3 L13: 0.2210 L23: 0.4876
REMARK 3 S TENSOR
REMARK 3 S11: -0.1051 S12: 0.2127 S13: -0.0281
REMARK 3 S21: -0.0597 S22: 0.2936 S23: 0.1203
REMARK 3 S31: 0.0396 S32: 0.5836 S33: -0.1886
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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 U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 5JCV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-APR-16.
REMARK 100 THE DEPOSITION ID IS D_1000220350.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-DEC-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14055
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.230
REMARK 200 RESOLUTION RANGE LOW (A) : 33.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 10.90
REMARK 200 R MERGE (I) : 0.08700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 36.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.23
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.27
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.80
REMARK 200 R MERGE FOR SHELL (I) : 0.89000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.880
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: HKL-3000
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M LITHIUM SULFATE, 2 M AMMONIUM
REMARK 280 SULFATE, 0.1 M TRIS-CL, PH 7.0, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 3555 -Y,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X,Z+3/4
REMARK 290 5555 -X+1/2,Y,-Z+3/4
REMARK 290 6555 X,-Y+1/2,-Z+1/4
REMARK 290 7555 Y+1/2,X+1/2,-Z+1/2
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 X+1/2,Y+1/2,Z+1/2
REMARK 290 10555 -X,-Y,Z
REMARK 290 11555 -Y+1/2,X,Z+3/4
REMARK 290 12555 Y,-X+1/2,Z+1/4
REMARK 290 13555 -X,Y+1/2,-Z+1/4
REMARK 290 14555 X+1/2,-Y,-Z+3/4
REMARK 290 15555 Y,X,-Z
REMARK 290 16555 -Y+1/2,-X+1/2,-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 35.07750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 35.07750
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 112.23550
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 35.07750
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 56.11775
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 35.07750
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 168.35325
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 35.07750
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 168.35325
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 35.07750
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 56.11775
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 35.07750
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 35.07750
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 112.23550
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 0.00000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 35.07750
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 35.07750
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 112.23550
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 35.07750
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 168.35325
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 35.07750
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 56.11775
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 35.07750
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 56.11775
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 35.07750
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 168.35325
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 35.07750
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 35.07750
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 112.23550
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: 1860 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 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 350 BIOMT1 2 0.000000 -1.000000 0.000000 35.07750
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 35.07750
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 112.23550
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 SER A 61
REMARK 465 ASN A 62
REMARK 465 THR A 228
REMARK 465 GLU A 229
REMARK 465 LYS A 230
REMARK 465 ASP A 231
REMARK 465 TYR A 232
REMARK 465 GLU A 233
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 ASP A 86 78.43 -156.01
REMARK 500 SER A 92 -164.95 -126.58
REMARK 500 MSE A 140 -127.95 61.36
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 SO4 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: CSGID-IDP02804 RELATED DB: TARGETTRACK
DBREF 5JCV A 64 243 UNP Q8Y588 Q8Y588_LISMO 64 243
SEQADV 5JCV SER A 61 UNP Q8Y588 EXPRESSION TAG
SEQADV 5JCV ASN A 62 UNP Q8Y588 EXPRESSION TAG
SEQADV 5JCV ALA A 63 UNP Q8Y588 EXPRESSION TAG
SEQRES 1 A 183 SER ASN ALA LEU ARG ASP LEU GLN LYS LEU ASN LYS ASP
SEQRES 2 A 183 MSE VAL GLY TRP LEU THR ILE ILE ASP THR GLU ILE ASP
SEQRES 3 A 183 TYR PRO ILE LEU GLN SER LYS ASP ASN ASP TYR TYR LEU
SEQRES 4 A 183 HIS HIS ASN TYR LYS ASN GLU LYS ALA ARG ALA GLY SER
SEQRES 5 A 183 ILE PHE LYS ASP TYR ARG ASN THR ASN GLU PHE LEU ASP
SEQRES 6 A 183 LYS ASN THR ILE ILE TYR GLY HIS ASN MSE LYS ASP GLY
SEQRES 7 A 183 SER MSE PHE ALA ASP LEU ARG LYS TYR LEU ASP LYS ASP
SEQRES 8 A 183 PHE LEU VAL ALA HIS PRO THR PHE SER TYR GLU SER GLY
SEQRES 9 A 183 LEU THR ASN TYR GLU VAL GLU ILE PHE ALA VAL TYR GLU
SEQRES 10 A 183 THR THR THR ASP PHE TYR TYR ILE GLU THR GLU PHE PRO
SEQRES 11 A 183 GLU THR THR ASP PHE GLU ASP TYR LEU GLN LYS VAL LYS
SEQRES 12 A 183 GLN GLN SER VAL TYR THR SER ASN VAL LYS VAL SER GLY
SEQRES 13 A 183 LYS ASP ARG ILE ILE THR LEU SER THR CYS ASP THR GLU
SEQRES 14 A 183 LYS ASP TYR GLU LYS GLY ARG MSE VAL ILE GLN GLY LYS
SEQRES 15 A 183 LEU
MODRES 5JCV MSE A 74 MET MODIFIED RESIDUE
MODRES 5JCV MSE A 135 MET MODIFIED RESIDUE
MODRES 5JCV MSE A 140 MET MODIFIED RESIDUE
MODRES 5JCV MSE A 237 MET MODIFIED RESIDUE
HET MSE A 74 8
HET MSE A 135 8
HET MSE A 140 8
HET MSE A 237 8
HET SO4 A 501 5
HET CL A 502 1
HETNAM MSE SELENOMETHIONINE
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
FORMUL 1 MSE 4(C5 H11 N O2 SE)
FORMUL 2 SO4 O4 S 2-
FORMUL 3 CL CL 1-
FORMUL 4 HOH *22(H2 O)
HELIX 1 AA1 ALA A 63 ASP A 73 1 11
HELIX 2 AA2 ASP A 96 HIS A 101 1 6
HELIX 3 AA3 PHE A 141 LEU A 148 5 8
HELIX 4 AA4 ASP A 149 HIS A 156 1 8
HELIX 5 AA5 PHE A 182 GLU A 186 5 5
HELIX 6 AA6 GLU A 191 SER A 206 1 16
SHEET 1 AA1 9 MSE A 74 THR A 79 0
SHEET 2 AA1 9 ASP A 86 LEU A 90 -1 O ILE A 89 N VAL A 75
SHEET 3 AA1 9 ILE A 113 LYS A 115 1 O ILE A 113 N LEU A 90
SHEET 4 AA1 9 ASN A 127 GLY A 132 -1 O TYR A 131 N PHE A 114
SHEET 5 AA1 9 ILE A 220 THR A 225 1 O THR A 222 N THR A 128
SHEET 6 AA1 9 ARG A 236 LYS A 242 -1 O ILE A 239 N LEU A 223
SHEET 7 AA1 9 ASN A 167 THR A 178 -1 N GLU A 171 O LYS A 242
SHEET 8 AA1 9 THR A 158 GLU A 162 -1 N PHE A 159 O VAL A 170
SHEET 9 AA1 9 MSE A 74 THR A 79 -1 N TRP A 77 O GLU A 162
LINK C ASP A 73 N MSE A 74 1555 1555 1.35
LINK C MSE A 74 N VAL A 75 1555 1555 1.33
LINK C ASN A 134 N MSE A 135 1555 1555 1.33
LINK C MSE A 135 N LYS A 136 1555 1555 1.32
LINK C SER A 139 N MSE A 140 1555 1555 1.33
LINK C MSE A 140 N PHE A 141 1555 1555 1.33
LINK C ARG A 236 N MSE A 237 1555 1555 1.32
LINK C MSE A 237 N VAL A 238 1555 1555 1.32
SITE 1 AC1 3 ALA A 108 ARG A 109 HOH A 611
SITE 1 AC2 3 THR A 178 THR A 179 THR A 180
CRYST1 70.155 70.155 224.471 90.00 90.00 90.00 I 41 2 2 16
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 0.014254 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014254 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004455 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
