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HEADER HYDROLASE 29-OCT-07 2VF2
TITLE X-RAY CRYSTAL STRUCTURE OF HSAD FROM MYCOBACTERIUM
TITLE 2 TUBERCULOSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 2-HYDROXY-6-OXO-6-PHENYLHEXA-2,4-DIENOATE
COMPND 3 HYDROLASE BPHD;
COMPND 4 CHAIN: A, B;
COMPND 5 SYNONYM: 2,6-DIOXO-6-PHENYLHEXA-3-ENOATE HYDROLASE,
COMPND 6 2-HYDROXY-6-PHENYLHEXA-2,4-DIENOIC ACID HYDROLASE;
COMPND 7 EC: 3.7.1.8;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 EXPRESSION_SYSTEM: PSEUDOMONAS PUTIDA;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 303;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: KT4224;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PVLT31
KEYWDS META-CLEAVAGE PRODUCT HYDROLASE, HSAD, HYDROLASE, SERINE
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.LACK,E.D.LOWE,J.LIU,L.D.ELTIS,M.E.M.NOBLE,E.SIM,
AUTHOR 2 I.M.WESTWOOD
REVDAT 4 24-FEB-09 2VF2 1 VERSN
REVDAT 3 08-JAN-08 2VF2 1 JRNL ATOM ANISOU
REVDAT 2 20-NOV-07 2VF2 1 AUTHOR JRNL
REVDAT 1 06-NOV-07 2VF2 0
JRNL AUTH N.LACK,E.D.LOWE,J.LIU,L.D.ELTIS,M.E.M.NOBLE,E.SIM,
JRNL AUTH 2 I.M.WESTWOOD
JRNL TITL STRUCTURE OF HSAD, A STEROID-DEGRADING HYDROLASE,
JRNL TITL 2 FROM MYCOBACTERIUM TUBERCULOSIS.
JRNL REF ACTA CRYSTALLOGR.,SECT.F V. 64 2 2008
JRNL REFN ISSN 1744-3091
JRNL PMID 18097091
JRNL DOI 10.1107/S1744309107065931
REMARK 2
REMARK 2 RESOLUTION. 2.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX.REFINE
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.4
REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.9
REMARK 3 NUMBER OF REFLECTIONS : 47065
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.212
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 2496
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2VF2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-OCT-07.
REMARK 100 THE PDBE ID CODE IS EBI-34217.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-AUG-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9680
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24657
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.35
REMARK 200 RESOLUTION RANGE LOW (A) : 32.40
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.5
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 200 DATA REDUNDANCY : 3.4
REMARK 200 R MERGE (I) : 0.08
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.90
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.48
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.4
REMARK 200 R MERGE FOR SHELL (I) : 0.50
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.50
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: PDB ENTRIES 1C4X AND 2OG1
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.4
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30 % (W/V) PEG 3000, 0.1 M CHES
REMARK 280 PH 9.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 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 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y+1/2,Z
REMARK 290 7555 -X+1/2,Y,-Z
REMARK 290 8555 X,-Y,-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 41.18000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 97.33500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.23000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 97.33500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 41.18000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.23000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 41.18000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 41.23000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 97.33500
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 41.23000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 41.18000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 97.33500
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 GENERATING THE BIOMOLECULE
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: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 9790 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 49750 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.7 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 41.23000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 HOH A2011 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2079 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B2016 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 -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 THR A 2
REMARK 465 ALA A 3
REMARK 465 THR A 4
REMARK 465 GLU A 5
REMARK 465 GLU A 6
REMARK 465 ARG A 291
REMARK 465 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 ALA B 3
REMARK 465 THR B 4
REMARK 465 GLU B 5
REMARK 465 GLU B 6
REMARK 465 ARG B 291
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O THR B 8 - OG1 THR B 12 2.14
REMARK 500 OG1 THR B 8 - OG SER B 11 2.10
REMARK 500 OD1 ASP B 19 - O GLY B 22 2.00
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
REMARK 500 CD LYS A 25 NZ LYS A 25 6455 1.90
REMARK 500 CE LYS A 25 CE LYS A 25 6455 1.78
REMARK 500 CE LYS A 25 NZ LYS A 25 6455 0.46
REMARK 500 NZ LYS A 25 CD LYS A 25 6455 1.90
REMARK 500 NZ LYS A 25 CE LYS A 25 6455 0.46
REMARK 500 NZ LYS A 25 NZ LYS A 25 6455 1.17
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 HIS A 27 CB - CG - ND1 ANGL. DEV. = 9.9 DEGREES
REMARK 500 HIS A 65 CB - CG - ND1 ANGL. DEV. = 10.1 DEGREES
REMARK 500 HIS A 78 CB - CG - ND1 ANGL. DEV. = 9.9 DEGREES
REMARK 500 HIS B 27 CB - CG - ND1 ANGL. DEV. = 9.7 DEGREES
REMARK 500 HIS B 67 CB - CG - ND1 ANGL. DEV. = 9.7 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 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 PRO A 23 127.27 -34.42
REMARK 500 LYS A 81 72.36 -100.82
REMARK 500 SER A 114 -120.91 57.85
REMARK 500 MET A 221 56.05 -91.11
REMARK 500 VAL A 243 -61.17 -96.26
REMARK 500 TRP A 270 57.29 -97.58
REMARK 500 HIS B 65 -36.81 -132.77
REMARK 500 SER B 114 -124.47 49.46
REMARK 500 ARG B 133 134.43 -35.46
REMARK 500 VAL B 243 -64.45 -107.92
REMARK 500 ARG B 258 42.51 -104.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 VAL A 33 21.3 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1291
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1291
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1292
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1292
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1293
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 SEQUENCE USED IN THIS STUDY CONTAINS N-TERMINAL HEXA-
REMARK 999 HISTIDINE TAG (20 AMINO ACIDS) WHICH WAS NOT CLEAVABLE
REMARK 999 WITH THROMBIN.
DBREF 2VF2 A -19 0 PDB 2VF2 2VF2 -19 0
DBREF 2VF2 A 1 291 UNP P96851 P96851_MYCTU 1 291
DBREF 2VF2 B -19 0 PDB 2VF2 2VF2 -19 0
DBREF 2VF2 B 1 291 UNP P96851 P96851_MYCTU 1 291
SEQRES 1 A 311 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 311 LEU VAL PRO ARG GLY SER HIS MET THR ALA THR GLU GLU
SEQRES 3 A 311 LEU THR PHE GLU SER THR SER ARG PHE ALA GLU VAL ASP
SEQRES 4 A 311 VAL ASP GLY PRO LEU LYS LEU HIS TYR HIS GLU ALA GLY
SEQRES 5 A 311 VAL GLY ASN ASP GLN THR VAL VAL LEU LEU HIS GLY GLY
SEQRES 6 A 311 GLY PRO GLY ALA ALA SER TRP THR ASN PHE SER ARG ASN
SEQRES 7 A 311 ILE ALA VAL LEU ALA ARG HIS PHE HIS VAL LEU ALA VAL
SEQRES 8 A 311 ASP GLN PRO GLY TYR GLY HIS SER ASP LYS ARG ALA GLU
SEQRES 9 A 311 HIS GLY GLN PHE ASN ARG TYR ALA ALA MET ALA LEU LYS
SEQRES 10 A 311 GLY LEU PHE ASP GLN LEU GLY LEU GLY ARG VAL PRO LEU
SEQRES 11 A 311 VAL GLY ASN SER LEU GLY GLY GLY THR ALA VAL ARG PHE
SEQRES 12 A 311 ALA LEU ASP TYR PRO ALA ARG ALA GLY ARG LEU VAL LEU
SEQRES 13 A 311 MET GLY PRO GLY GLY LEU SER ILE ASN LEU PHE ALA PRO
SEQRES 14 A 311 ASP PRO THR GLU GLY VAL LYS ARG LEU SER LYS PHE SER
SEQRES 15 A 311 VAL ALA PRO THR ARG GLU ASN LEU GLU ALA PHE LEU ARG
SEQRES 16 A 311 VAL MET VAL TYR ASP LYS ASN LEU ILE THR PRO GLU LEU
SEQRES 17 A 311 VAL ASP GLN ARG PHE ALA LEU ALA SER THR PRO GLU SER
SEQRES 18 A 311 LEU THR ALA THR ARG ALA MET GLY LYS SER PHE ALA GLY
SEQRES 19 A 311 ALA ASP PHE GLU ALA GLY MET MET TRP ARG GLU VAL TYR
SEQRES 20 A 311 ARG LEU ARG GLN PRO VAL LEU LEU ILE TRP GLY ARG GLU
SEQRES 21 A 311 ASP ARG VAL ASN PRO LEU ASP GLY ALA LEU VAL ALA LEU
SEQRES 22 A 311 LYS THR ILE PRO ARG ALA GLN LEU HIS VAL PHE GLY GLN
SEQRES 23 A 311 CYS GLY HIS TRP VAL GLN VAL GLU LYS PHE ASP GLU PHE
SEQRES 24 A 311 ASN LYS LEU THR ILE GLU PHE LEU GLY GLY GLY ARG
SEQRES 1 B 311 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 311 LEU VAL PRO ARG GLY SER HIS MET THR ALA THR GLU GLU
SEQRES 3 B 311 LEU THR PHE GLU SER THR SER ARG PHE ALA GLU VAL ASP
SEQRES 4 B 311 VAL ASP GLY PRO LEU LYS LEU HIS TYR HIS GLU ALA GLY
SEQRES 5 B 311 VAL GLY ASN ASP GLN THR VAL VAL LEU LEU HIS GLY GLY
SEQRES 6 B 311 GLY PRO GLY ALA ALA SER TRP THR ASN PHE SER ARG ASN
SEQRES 7 B 311 ILE ALA VAL LEU ALA ARG HIS PHE HIS VAL LEU ALA VAL
SEQRES 8 B 311 ASP GLN PRO GLY TYR GLY HIS SER ASP LYS ARG ALA GLU
SEQRES 9 B 311 HIS GLY GLN PHE ASN ARG TYR ALA ALA MET ALA LEU LYS
SEQRES 10 B 311 GLY LEU PHE ASP GLN LEU GLY LEU GLY ARG VAL PRO LEU
SEQRES 11 B 311 VAL GLY ASN SER LEU GLY GLY GLY THR ALA VAL ARG PHE
SEQRES 12 B 311 ALA LEU ASP TYR PRO ALA ARG ALA GLY ARG LEU VAL LEU
SEQRES 13 B 311 MET GLY PRO GLY GLY LEU SER ILE ASN LEU PHE ALA PRO
SEQRES 14 B 311 ASP PRO THR GLU GLY VAL LYS ARG LEU SER LYS PHE SER
SEQRES 15 B 311 VAL ALA PRO THR ARG GLU ASN LEU GLU ALA PHE LEU ARG
SEQRES 16 B 311 VAL MET VAL TYR ASP LYS ASN LEU ILE THR PRO GLU LEU
SEQRES 17 B 311 VAL ASP GLN ARG PHE ALA LEU ALA SER THR PRO GLU SER
SEQRES 18 B 311 LEU THR ALA THR ARG ALA MET GLY LYS SER PHE ALA GLY
SEQRES 19 B 311 ALA ASP PHE GLU ALA GLY MET MET TRP ARG GLU VAL TYR
SEQRES 20 B 311 ARG LEU ARG GLN PRO VAL LEU LEU ILE TRP GLY ARG GLU
SEQRES 21 B 311 ASP ARG VAL ASN PRO LEU ASP GLY ALA LEU VAL ALA LEU
SEQRES 22 B 311 LYS THR ILE PRO ARG ALA GLN LEU HIS VAL PHE GLY GLN
SEQRES 23 B 311 CYS GLY HIS TRP VAL GLN VAL GLU LYS PHE ASP GLU PHE
SEQRES 24 B 311 ASN LYS LEU THR ILE GLU PHE LEU GLY GLY GLY ARG
HET GOL B1291 6
HET GOL A1291 6
HET GOL B1292 6
HET SO4 A1292 5
HET SO4 B1293 5
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 4 GOL 3(C3 H8 O3)
FORMUL 5 HOH *205(H2 O1)
HELIX 1 1 ALA A 50 PHE A 55 1 6
HELIX 2 2 ASN A 58 ARG A 64 1 7
HELIX 3 3 GLN A 87 GLY A 104 1 18
HELIX 4 4 SER A 114 TYR A 127 1 14
HELIX 5 5 THR A 152 ALA A 164 1 13
HELIX 6 6 THR A 166 VAL A 176 1 11
HELIX 7 7 ASP A 180 ILE A 184 5 5
HELIX 8 8 THR A 185 SER A 197 1 13
HELIX 9 9 THR A 198 PHE A 212 1 15
HELIX 10 10 ASP A 216 MET A 221 5 6
HELIX 11 11 MET A 221 GLU A 225 5 5
HELIX 12 12 GLU A 225 LEU A 229 5 5
HELIX 13 13 PRO A 245 GLY A 248 5 4
HELIX 14 14 ALA A 249 ILE A 256 1 8
HELIX 15 15 TRP A 270 LYS A 275 1 6
HELIX 16 16 LYS A 275 LEU A 287 1 13
HELIX 17 17 THR B 8 THR B 12 1 5
HELIX 18 18 ALA B 50 PHE B 55 1 6
HELIX 19 19 ASN B 58 ARG B 64 1 7
HELIX 20 20 GLN B 87 LEU B 103 1 17
HELIX 21 21 SER B 114 TYR B 127 1 14
HELIX 22 22 THR B 152 ALA B 164 1 13
HELIX 23 23 THR B 166 VAL B 176 1 11
HELIX 24 24 ASP B 180 ILE B 184 5 5
HELIX 25 25 THR B 185 SER B 197 1 13
HELIX 26 26 THR B 198 GLY B 209 1 12
HELIX 27 27 ASP B 216 MET B 221 5 6
HELIX 28 28 MET B 221 GLU B 225 5 5
HELIX 29 29 GLU B 225 LEU B 229 5 5
HELIX 30 30 PRO B 245 GLY B 248 5 4
HELIX 31 31 ALA B 249 ILE B 256 1 8
HELIX 32 32 TRP B 270 LYS B 275 1 6
HELIX 33 33 LYS B 275 GLY B 288 1 14
SHEET 1 AA 8 SER A 13 ASP A 19 0
SHEET 2 AA 8 PRO A 23 ALA A 31 -1 O LEU A 24 N VAL A 18
SHEET 3 AA 8 HIS A 67 VAL A 71 -1 O VAL A 68 N ALA A 31
SHEET 4 AA 8 THR A 38 LEU A 42 1 O VAL A 39 N LEU A 69
SHEET 5 AA 8 VAL A 108 ASN A 113 1 O PRO A 109 N VAL A 40
SHEET 6 AA 8 ALA A 131 MET A 137 1 N GLY A 132 O VAL A 108
SHEET 7 AA 8 VAL A 233 GLY A 238 1 O LEU A 234 N LEU A 136
SHEET 8 AA 8 ALA A 259 PHE A 264 1 O GLN A 260 N LEU A 235
SHEET 1 BA 8 SER B 13 VAL B 18 0
SHEET 2 BA 8 LEU B 24 ALA B 31 -1 O LEU B 24 N VAL B 18
SHEET 3 BA 8 HIS B 67 VAL B 71 -1 O VAL B 68 N ALA B 31
SHEET 4 BA 8 THR B 38 LEU B 42 1 O VAL B 39 N LEU B 69
SHEET 5 BA 8 VAL B 108 ASN B 113 1 O PRO B 109 N VAL B 40
SHEET 6 BA 8 ALA B 131 MET B 137 1 N GLY B 132 O VAL B 108
SHEET 7 BA 8 VAL B 233 GLY B 238 1 O LEU B 234 N LEU B 136
SHEET 8 BA 8 ALA B 259 PHE B 264 1 O GLN B 260 N LEU B 235
CISPEP 1 ASP A 150 PRO A 151 0 5.09
CISPEP 2 ASP B 150 PRO B 151 0 -1.46
SITE 1 AC1 4 SER B 143 ILE B 144 ASN B 145 ASP B 150
SITE 1 AC2 4 THR A 53 SER A 56 PRO A 186 GLU A 187
SITE 1 AC3 7 ASP B 21 HIS B 85 GLY B 86 TYR B 91
SITE 2 AC3 7 MET B 94 HOH B2077 HOH B2078
SITE 1 AC4 5 ARG A 157 ARG A 175 LYS A 181 HOH A2126
SITE 2 AC4 5 LYS B 156
SITE 1 AC5 3 LYS A 156 ARG B 157 LYS B 181
CRYST1 82.360 82.460 194.670 90.00 90.00 90.00 I 21 21 21 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 0.012142 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012127 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005137 0.00000
MTRIX1 1 -0.097702 0.995102 -0.015065 -20.31920 1
MTRIX2 1 0.994522 0.098188 0.035851 17.93810 1
MTRIX3 1 0.037155 -0.011480 -0.999244 51.75780 1
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