HEADER LYASE 20-JAN-05 1YM3
TITLE CRYSTAL STRUCTURE OF CARBONIC ANHYDRASE RV3588C FROM MYCOBACTERIUM
TITLE 2 TUBERCULOSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBONIC ANHYDRASE (CARBONATE DEHYDRATASE) (CARBONIC
COMPND 3 DEHYDRATASE);
COMPND 4 CHAIN: A;
COMPND 5 EC: 4.2.1.1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 GENE: RV3588C;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21-AI;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PCRT7
KEYWDS ZN PROTEIN, STRUCTURAL PROTEOMICS IN EUROPE, SPINE, STRUCTURAL
KEYWDS 2 GENOMICS, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.S.COVARRUBIAS,A.M.LARSSON,M.HOGBOM,J.LINDBERG,T.BERGFORS,
AUTHOR 2 C.BJORKELID,S.L.MOWBRAY,T.UNGE,T.A.JONES,STRUCTURAL PROTEOMICS IN
AUTHOR 3 EUROPE (SPINE)
REVDAT 7 23-AUG-23 1YM3 1 REMARK SEQADV LINK
REVDAT 6 07-MAR-18 1YM3 1 REMARK
REVDAT 5 13-JUL-11 1YM3 1 VERSN
REVDAT 4 24-FEB-09 1YM3 1 VERSN
REVDAT 3 24-MAY-05 1YM3 1 JRNL
REVDAT 2 15-MAR-05 1YM3 1 EXPDTA
REVDAT 1 08-MAR-05 1YM3 0
JRNL AUTH A.SUAREZ COVARRUBIAS,A.M.LARSSON,M.HOGBOM,J.LINDBERG,
JRNL AUTH 2 T.BERGFORS,C.BJORKELID,S.L.MOWBRAY,T.UNGE,T.A.JONES
JRNL TITL STRUCTURE AND FUNCTION OF CARBONIC ANHYDRASES FROM
JRNL TITL 2 MYCOBACTERIUM TUBERCULOSIS.
JRNL REF J.BIOL.CHEM. V. 280 18782 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 15753099
JRNL DOI 10.1074/JBC.M414348200
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
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) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.20
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 82.9
REMARK 3 NUMBER OF REFLECTIONS : 13934
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) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 734
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) : 1.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.79
REMARK 3 REFLECTION IN BIN (WORKING SET) : 956
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.1860
REMARK 3 BIN FREE R VALUE SET COUNT : 59
REMARK 3 BIN FREE R VALUE : 0.2380
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1435
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 130
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.21
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.36000
REMARK 3 B22 (A**2) : 0.36000
REMARK 3 B33 (A**2) : -0.71000
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): 0.154
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.146
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.085
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.595
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1468 ; 0.016 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 1385 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1994 ; 1.484 ; 1.946
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3186 ; 0.874 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 193 ; 5.556 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 234 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1678 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 300 ; 0.009 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 288 ; 0.208 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1551 ; 0.229 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 828 ; 0.080 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 69 ; 0.184 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 1 ; 0.007 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 20 ; 0.619 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 66 ; 0.322 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 18 ; 0.176 ; 0.200
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): 956 ; 0.980 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1532 ; 1.753 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 512 ; 2.682 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 462 ; 4.272 ; 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 : 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 4 A 206
REMARK 3 ORIGIN FOR THE GROUP (A): 20.0998 22.5969 21.0858
REMARK 3 T TENSOR
REMARK 3 T11: 0.0381 T22: 0.0095
REMARK 3 T33: 0.0326 T12: -0.0001
REMARK 3 T13: -0.0093 T23: -0.0022
REMARK 3 L TENSOR
REMARK 3 L11: 0.5139 L22: 0.8383
REMARK 3 L33: 0.9139 L12: 0.1853
REMARK 3 L13: 0.1750 L23: 0.3555
REMARK 3 S TENSOR
REMARK 3 S11: 0.0211 S12: -0.0526 S13: -0.0233
REMARK 3 S21: -0.0872 S22: -0.0219 S23: 0.0198
REMARK 3 S31: 0.0856 S32: -0.0211 S33: 0.0009
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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
REMARK 4
REMARK 4 1YM3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-FEB-05.
REMARK 100 THE DEPOSITION ID IS D_1000031674.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-MAY-04
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 : MAX II
REMARK 200 BEAMLINE : I711
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.085
REMARK 200 MONOCHROMATOR : SINGLE ASYMMETRICALLY CUT
REMARK 200 SI(111) CRYSTAL WITH HORIZONTAL
REMARK 200 DIFFRACTION PLANE. THE CRYSTAL
REMARK 200 IS BENDABLE FOR HORIZONTAL
REMARK 200 FOCUSING.
REMARK 200 OPTICS : VERTICALLY FOCUSING CYLINDRICAL
REMARK 200 MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13934
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 26.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 83.3
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.3500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.81
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.1
REMARK 200 DATA REDUNDANCY IN SHELL : 4.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.29800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1I6O AND 1DDZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 34.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MGCL2, PEG 400, HEPES, PH 7.0, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 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+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
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 52.09600
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 28.18850
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 28.18850
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 26.04800
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 28.18850
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 28.18850
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 78.14400
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 28.18850
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 28.18850
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 26.04800
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 28.18850
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 28.18850
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 78.14400
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 52.09600
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 300 REMARK: THE SECOND PART OF THE BIOLOGICAL ASSEMBLY IS GENERATED
REMARK 300 BY THE TWO FOLD AXIS: -Y, -X, 1/2-Z
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 3500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 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 56.37700
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 56.37700
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 52.09600
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 313 LIES ON A SPECIAL POSITION.
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 MET A -7
REMARK 465 ALA A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 GLY A 1
REMARK 465 PRO A 2
REMARK 465 ASN A 3
REMARK 465 VAL A 32
REMARK 465 ASP A 33
REMARK 465 HIS A 34
REMARK 465 ARG A 35
REMARK 465 ALA A 36
REMARK 465 GLY A 37
REMARK 465 LEU A 38
REMARK 465 ALA A 39
REMARK 465 ALA A 40
REMARK 465 GLY A 41
REMARK 465 VAL A 207
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 OE1 GLU A 173 O HOH A 399 2.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OD1 ASP A 80 OD2 ASP A 80 8665 1.49
REMARK 500 CG ASP A 80 OD1 ASP A 80 8665 2.01
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 SER A 147 -8.26 -143.79
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 ZN A 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 51 SG
REMARK 620 2 ASP A 53 OD1 98.7
REMARK 620 3 HIS A 104 NE2 119.1 90.8
REMARK 620 4 CYS A 107 SG 112.1 123.2 111.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 199 O
REMARK 620 2 HIS A 199 ND1 82.9
REMARK 620 3 HOH A 303 O 82.9 86.6
REMARK 620 4 HOH A 305 O 93.1 174.8 96.2
REMARK 620 5 HOH A 307 O 172.7 96.6 89.8 87.7
REMARK 620 6 HOH A 315 O 94.7 91.8 177.3 85.2 92.6
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 ZN A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: RV3588 RELATED DB: TARGETDB
DBREF 1YM3 A 2 207 UNP O53573 O53573_MYCTU 2 207
SEQADV 1YM3 MET A -7 UNP O53573 CLONING ARTIFACT
SEQADV 1YM3 ALA A -6 UNP O53573 CLONING ARTIFACT
SEQADV 1YM3 HIS A -5 UNP O53573 CLONING ARTIFACT
SEQADV 1YM3 HIS A -4 UNP O53573 CLONING ARTIFACT
SEQADV 1YM3 HIS A -3 UNP O53573 CLONING ARTIFACT
SEQADV 1YM3 HIS A -2 UNP O53573 CLONING ARTIFACT
SEQADV 1YM3 HIS A -1 UNP O53573 CLONING ARTIFACT
SEQADV 1YM3 HIS A 0 UNP O53573 CLONING ARTIFACT
SEQADV 1YM3 GLY A 1 UNP O53573 CLONING ARTIFACT
SEQRES 1 A 215 MET ALA HIS HIS HIS HIS HIS HIS GLY PRO ASN THR ASN
SEQRES 2 A 215 PRO VAL ALA ALA TRP LYS ALA LEU LYS GLU GLY ASN GLU
SEQRES 3 A 215 ARG PHE VAL ALA GLY ARG PRO GLN HIS PRO SER GLN SER
SEQRES 4 A 215 VAL ASP HIS ARG ALA GLY LEU ALA ALA GLY GLN LYS PRO
SEQRES 5 A 215 THR ALA VAL ILE PHE GLY CYS ALA ASP SER ARG VAL ALA
SEQRES 6 A 215 ALA GLU ILE ILE PHE ASP GLN GLY LEU GLY ASP MET PHE
SEQRES 7 A 215 VAL VAL ARG THR ALA GLY HIS VAL ILE ASP SER ALA VAL
SEQRES 8 A 215 LEU GLY SER ILE GLU TYR ALA VAL THR VAL LEU ASN VAL
SEQRES 9 A 215 PRO LEU ILE VAL VAL LEU GLY HIS ASP SER CYS GLY ALA
SEQRES 10 A 215 VAL ASN ALA ALA LEU ALA ALA ILE ASN ASP GLY THR LEU
SEQRES 11 A 215 PRO GLY GLY TYR VAL ARG ASP VAL VAL GLU ARG VAL ALA
SEQRES 12 A 215 PRO SER VAL LEU LEU GLY ARG ARG ASP GLY LEU SER ARG
SEQRES 13 A 215 VAL ASP GLU PHE GLU GLN ARG HIS VAL HIS GLU THR VAL
SEQRES 14 A 215 ALA ILE LEU MET ALA ARG SER SER ALA ILE SER GLU ARG
SEQRES 15 A 215 ILE ALA GLY GLY SER LEU ALA ILE VAL GLY VAL THR TYR
SEQRES 16 A 215 GLN LEU ASP ASP GLY ARG ALA VAL LEU ARG ASP HIS ILE
SEQRES 17 A 215 GLY ASN ILE GLY GLU GLU VAL
HET ZN A 301 1
HET MG A 302 1
HETNAM ZN ZINC ION
HETNAM MG MAGNESIUM ION
FORMUL 2 ZN ZN 2+
FORMUL 3 MG MG 2+
FORMUL 4 HOH *130(H2 O)
HELIX 1 1 ASN A 5 GLY A 23 1 19
HELIX 2 2 HIS A 27 SER A 31 5 5
HELIX 3 3 ALA A 57 PHE A 62 1 6
HELIX 4 4 ALA A 75 VAL A 78 5 4
HELIX 5 5 ASP A 80 VAL A 93 1 14
HELIX 6 6 CYS A 107 GLY A 120 1 14
HELIX 7 7 TYR A 126 ASP A 144 1 19
HELIX 8 8 ARG A 148 SER A 168 1 21
HELIX 9 9 SER A 168 GLY A 177 1 10
SHEET 1 A 5 MET A 69 THR A 74 0
SHEET 2 A 5 ALA A 46 CYS A 51 1 N ILE A 48 O VAL A 72
SHEET 3 A 5 LEU A 98 HIS A 104 1 O VAL A 100 N PHE A 49
SHEET 4 A 5 ALA A 181 TYR A 187 1 O VAL A 185 N GLY A 103
SHEET 5 A 5 VAL A 195 ILE A 200 -1 O VAL A 195 N THR A 186
LINK SG CYS A 51 ZN ZN A 301 1555 1555 2.37
LINK OD1 ASP A 53 ZN ZN A 301 1555 1555 2.10
LINK NE2 HIS A 104 ZN ZN A 301 1555 1555 2.05
LINK SG CYS A 107 ZN ZN A 301 1555 1555 2.30
LINK O HIS A 199 MG MG A 302 1555 1555 2.04
LINK ND1 HIS A 199 MG MG A 302 1555 1555 2.27
LINK MG MG A 302 O HOH A 303 1555 1555 2.07
LINK MG MG A 302 O HOH A 305 1555 1555 2.05
LINK MG MG A 302 O HOH A 307 1555 1555 2.08
LINK MG MG A 302 O HOH A 315 1555 1555 2.13
SITE 1 AC1 4 CYS A 51 ASP A 53 HIS A 104 CYS A 107
SITE 1 AC2 5 HIS A 199 HOH A 303 HOH A 305 HOH A 307
SITE 2 AC2 5 HOH A 315
CRYST1 56.377 56.377 104.192 90.00 90.00 90.00 P 41 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 0.017738 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017738 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009598 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
