HEADER ISOMERASE 23-MAR-10 3M9Y
TITLE CRYSTAL STRUCTURE OF TRIOSEPHOSPHATE ISOMERASE FROM METHICILLIN
TITLE 2 RESISTANT STAPHYLOCOCCUS AUREUS AT 1.9 ANGSTROM RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRIOSEPHOSPHATE ISOMERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: TIM, TRIOSE-PHOSPHATE ISOMERASE;
COMPND 5 EC: 5.3.1.1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE 3 ORGANISM_TAXID: 282458;
SOURCE 4 STRAIN: MRSA252;
SOURCE 5 GENE: SAR0830, TPI, TPIA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: M15;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PQE30
KEYWDS TIM BARREL, GLYCOLYSIS, GLUCONEOGENESIS, ISOMERASE, PENTOSE SHUNT
EXPDTA X-RAY DIFFRACTION
AUTHOR S.MUKHERJEE,D.DUTTA,B.SAHA,A.K.DAS
REVDAT 5 01-NOV-23 3M9Y 1 REMARK SEQADV LINK
REVDAT 4 26-JUN-13 3M9Y 1 JRNL
REVDAT 3 17-OCT-12 3M9Y 1 JRNL VERSN REMARK
REVDAT 2 13-APR-11 3M9Y 1 ATOM
REVDAT 1 06-APR-11 3M9Y 0
JRNL AUTH S.MUKHERJEE,A.ROYCHOWDHURY,D.DUTTA,A.K.DAS
JRNL TITL CRYSTAL STRUCTURES OF TRIOSEPHOSPHATE ISOMERASE FROM
JRNL TITL 2 METHICILLIN RESISTANT STAPHYLOCOCCUS AUREUS MRSA252 PROVIDE
JRNL TITL 3 STRUCTURAL INSIGHTS INTO NOVEL MODES OF LIGAND BINDING AND
JRNL TITL 4 UNIQUE CONFORMATIONS OF CATALYTIC LOOP
JRNL REF BIOCHIMIE V. 94 2532 2012
JRNL REFN ISSN 0300-9084
JRNL PMID 22813930
JRNL DOI 10.1016/J.BIOCHI.2012.07.001
REMARK 2
REMARK 2 RESOLUTION. 1.90 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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 44825
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) : 0.161
REMARK 3 R VALUE (WORKING SET) : 0.159
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2258
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2972
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.26
REMARK 3 BIN R VALUE (WORKING SET) : 0.2050
REMARK 3 BIN FREE R VALUE SET COUNT : 171
REMARK 3 BIN FREE R VALUE : 0.2530
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3825
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 15
REMARK 3 SOLVENT ATOMS : 481
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.10000
REMARK 3 B22 (A**2) : 1.10000
REMARK 3 B33 (A**2) : -2.21000
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): 0.128
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.127
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.083
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.189
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.969
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3916 ; 0.025 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5298 ; 1.842 ; 1.965
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 511 ; 5.822 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 171 ;38.137 ;26.374
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 702 ;13.790 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;11.336 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 608 ; 0.150 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2923 ; 0.010 ; 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): 2514 ; 1.275 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4043 ; 2.174 ; 2.500
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1402 ; 5.316 ; 5.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1251 ; 8.335 ;10.000
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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 4
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 3 A 107 2
REMARK 3 1 B 3 B 107 2
REMARK 3 2 A 110 A 156 2
REMARK 3 2 B 110 B 156 2
REMARK 3 3 A 160 A 172 2
REMARK 3 3 B 160 B 172 2
REMARK 3 4 A 186 A 242 2
REMARK 3 4 B 186 B 242 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 884 ; 0.100 ; 0.050
REMARK 3 MEDIUM POSITIONAL 1 A (A): 776 ; 0.130 ; 0.500
REMARK 3 TIGHT THERMAL 1 A (A**2): 884 ; 1.210 ; 1.500
REMARK 3 MEDIUM THERMAL 1 A (A**2): 776 ; 1.450 ; 2.500
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 : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 0 A 253
REMARK 3 ORIGIN FOR THE GROUP (A): 56.2495 13.0326 -8.0317
REMARK 3 T TENSOR
REMARK 3 T11: 0.0272 T22: 0.1290
REMARK 3 T33: 0.0744 T12: -0.0176
REMARK 3 T13: 0.0360 T23: -0.0065
REMARK 3 L TENSOR
REMARK 3 L11: 1.5165 L22: 0.5929
REMARK 3 L33: 1.3815 L12: -0.0339
REMARK 3 L13: 0.0149 L23: 0.2821
REMARK 3 S TENSOR
REMARK 3 S11: 0.0338 S12: 0.2816 S13: 0.1546
REMARK 3 S21: -0.1188 S22: 0.0555 S23: -0.1667
REMARK 3 S31: -0.1101 S32: 0.2647 S33: -0.0893
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 0 B 253
REMARK 3 ORIGIN FOR THE GROUP (A): 34.7112 19.6611 17.4992
REMARK 3 T TENSOR
REMARK 3 T11: 0.0125 T22: 0.0251
REMARK 3 T33: 0.0429 T12: 0.0053
REMARK 3 T13: -0.0055 T23: -0.0183
REMARK 3 L TENSOR
REMARK 3 L11: 0.6811 L22: 0.9265
REMARK 3 L33: 2.0168 L12: -0.1842
REMARK 3 L13: 0.1097 L23: 0.5453
REMARK 3 S TENSOR
REMARK 3 S11: -0.0207 S12: -0.0670 S13: 0.0931
REMARK 3 S21: 0.0033 S22: -0.0201 S23: 0.0436
REMARK 3 S31: -0.1309 S32: -0.1127 S33: 0.0408
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: U VALUES: RESIDUAL ONLY
REMARK 4
REMARK 4 3M9Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-MAR-10.
REMARK 100 THE DEPOSITION ID IS D_1000058293.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-OCT-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : VARIMAX MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.9
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44961
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 72.365
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 13.50
REMARK 200 R MERGE (I) : 0.05800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 29.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.9
REMARK 200 DATA REDUNDANCY IN SHELL : 12.10
REMARK 200 R MERGE FOR SHELL (I) : 0.43300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2BTM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6M TRISODIUM CITRATE DIHYDRATE, PH
REMARK 280 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 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+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
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 87.50300
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 39.73900
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 39.73900
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 131.25450
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 39.73900
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 39.73900
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 43.75150
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 39.73900
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 39.73900
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 131.25450
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 39.73900
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 39.73900
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 43.75150
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 87.50300
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: 3240 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 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 THR A 176
REMARK 465 GLY A 177
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 CG GLU B 250 O HOH B 342 2.16
REMARK 500 CE LYS B 120 O HOH B 511 2.16
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 ASP A 21 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 GLY B 175 N - CA - C ANGL. DEV. = -16.0 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LYS A 11 -149.31 53.91
REMARK 500 LYS A 14 141.78 87.85
REMARK 500 SER A 200 -99.18 -144.97
REMARK 500 LYS B 11 -139.61 53.75
REMARK 500 MET B 12 76.51 -101.19
REMARK 500 LYS B 14 145.60 83.54
REMARK 500 THR B 176 138.48 73.40
REMARK 500 SER B 200 -99.87 -145.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 254 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET B 225 O
REMARK 620 2 GLN B 227 O 98.1
REMARK 620 3 ILE B 230 O 105.3 95.4
REMARK 620 4 HOH B 305 O 87.3 171.6 89.3
REMARK 620 5 HOH B 327 O 89.7 87.3 164.2 86.4
REMARK 620 6 HOH B 359 O 167.8 90.2 82.7 83.5 81.7
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 254
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 255
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT B 256
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3UWU RELATED DB: PDB
REMARK 900 RELATED ID: 3UWV RELATED DB: PDB
REMARK 900 RELATED ID: 3UWW RELATED DB: PDB
REMARK 900 RELATED ID: 3UWY RELATED DB: PDB
REMARK 900 RELATED ID: 3UWZ RELATED DB: PDB
DBREF 3M9Y A 1 253 UNP Q6GIL6 TPIS_STAAR 1 253
DBREF 3M9Y B 1 253 UNP Q6GIL6 TPIS_STAAR 1 253
SEQADV 3M9Y SER A 0 UNP Q6GIL6 EXPRESSION TAG
SEQADV 3M9Y SER B 0 UNP Q6GIL6 EXPRESSION TAG
SEQRES 1 A 254 SER MET ARG THR PRO ILE ILE ALA GLY ASN TRP LYS MET
SEQRES 2 A 254 ASN LYS THR VAL GLN GLU ALA LYS ASP PHE VAL ASN ALA
SEQRES 3 A 254 LEU PRO THR LEU PRO ASP SER LYS GLU VAL GLU SER VAL
SEQRES 4 A 254 ILE CYS ALA PRO ALA ILE GLN LEU ASP ALA LEU THR THR
SEQRES 5 A 254 ALA VAL LYS GLU GLY LYS ALA GLN GLY LEU GLU ILE GLY
SEQRES 6 A 254 ALA GLN ASN THR TYR PHE GLU ASP ASN GLY ALA PHE THR
SEQRES 7 A 254 GLY GLU THR SER PRO VAL ALA LEU ALA ASP LEU GLY VAL
SEQRES 8 A 254 LYS TYR VAL VAL ILE GLY HIS SER GLU ARG ARG GLU LEU
SEQRES 9 A 254 PHE HIS GLU THR ASP GLU GLU ILE ASN LYS LYS ALA HIS
SEQRES 10 A 254 ALA ILE PHE LYS HIS GLY MET THR PRO ILE ILE CYS VAL
SEQRES 11 A 254 GLY GLU THR ASP GLU GLU ARG GLU SER GLY LYS ALA ASN
SEQRES 12 A 254 ASP VAL VAL GLY GLU GLN VAL LYS LYS ALA VAL ALA GLY
SEQRES 13 A 254 LEU SER GLU ASP GLN LEU LYS SER VAL VAL ILE ALA TYR
SEQRES 14 A 254 GLU PRO ILE TRP ALA ILE GLY THR GLY LYS SER SER THR
SEQRES 15 A 254 SER GLU ASP ALA ASN GLU MET CYS ALA PHE VAL ARG GLN
SEQRES 16 A 254 THR ILE ALA ASP LEU SER SER LYS GLU VAL SER GLU ALA
SEQRES 17 A 254 THR ARG ILE GLN TYR GLY GLY SER VAL LYS PRO ASN ASN
SEQRES 18 A 254 ILE LYS GLU TYR MET ALA GLN THR ASP ILE ASP GLY ALA
SEQRES 19 A 254 LEU VAL GLY GLY ALA SER LEU LYS VAL GLU ASP PHE VAL
SEQRES 20 A 254 GLN LEU LEU GLU GLY ALA LYS
SEQRES 1 B 254 SER MET ARG THR PRO ILE ILE ALA GLY ASN TRP LYS MET
SEQRES 2 B 254 ASN LYS THR VAL GLN GLU ALA LYS ASP PHE VAL ASN ALA
SEQRES 3 B 254 LEU PRO THR LEU PRO ASP SER LYS GLU VAL GLU SER VAL
SEQRES 4 B 254 ILE CYS ALA PRO ALA ILE GLN LEU ASP ALA LEU THR THR
SEQRES 5 B 254 ALA VAL LYS GLU GLY LYS ALA GLN GLY LEU GLU ILE GLY
SEQRES 6 B 254 ALA GLN ASN THR TYR PHE GLU ASP ASN GLY ALA PHE THR
SEQRES 7 B 254 GLY GLU THR SER PRO VAL ALA LEU ALA ASP LEU GLY VAL
SEQRES 8 B 254 LYS TYR VAL VAL ILE GLY HIS SER GLU ARG ARG GLU LEU
SEQRES 9 B 254 PHE HIS GLU THR ASP GLU GLU ILE ASN LYS LYS ALA HIS
SEQRES 10 B 254 ALA ILE PHE LYS HIS GLY MET THR PRO ILE ILE CYS VAL
SEQRES 11 B 254 GLY GLU THR ASP GLU GLU ARG GLU SER GLY LYS ALA ASN
SEQRES 12 B 254 ASP VAL VAL GLY GLU GLN VAL LYS LYS ALA VAL ALA GLY
SEQRES 13 B 254 LEU SER GLU ASP GLN LEU LYS SER VAL VAL ILE ALA TYR
SEQRES 14 B 254 GLU PRO ILE TRP ALA ILE GLY THR GLY LYS SER SER THR
SEQRES 15 B 254 SER GLU ASP ALA ASN GLU MET CYS ALA PHE VAL ARG GLN
SEQRES 16 B 254 THR ILE ALA ASP LEU SER SER LYS GLU VAL SER GLU ALA
SEQRES 17 B 254 THR ARG ILE GLN TYR GLY GLY SER VAL LYS PRO ASN ASN
SEQRES 18 B 254 ILE LYS GLU TYR MET ALA GLN THR ASP ILE ASP GLY ALA
SEQRES 19 B 254 LEU VAL GLY GLY ALA SER LEU LYS VAL GLU ASP PHE VAL
SEQRES 20 B 254 GLN LEU LEU GLU GLY ALA LYS
HET NA B 254 1
HET NA B 255 1
HET CIT B 256 13
HETNAM NA SODIUM ION
HETNAM CIT CITRIC ACID
FORMUL 3 NA 2(NA 1+)
FORMUL 5 CIT C6 H8 O7
FORMUL 6 HOH *481(H2 O)
HELIX 1 1 THR A 15 LEU A 26 1 12
HELIX 2 2 PRO A 42 ILE A 44 5 3
HELIX 3 3 GLN A 45 GLU A 55 1 11
HELIX 4 4 SER A 81 LEU A 88 1 8
HELIX 5 5 HIS A 97 PHE A 104 1 8
HELIX 6 6 THR A 107 HIS A 121 1 15
HELIX 7 7 THR A 132 SER A 138 1 7
HELIX 8 8 LYS A 140 ALA A 154 1 15
HELIX 9 9 SER A 157 VAL A 164 1 8
HELIX 10 10 PRO A 170 ILE A 174 5 5
HELIX 11 11 THR A 181 SER A 200 1 20
HELIX 12 12 SER A 201 GLU A 206 1 6
HELIX 13 13 ASN A 220 ALA A 226 1 7
HELIX 14 14 GLY A 236 LEU A 240 5 5
HELIX 15 15 LYS A 241 LYS A 253 1 13
HELIX 16 16 THR B 15 LEU B 26 1 12
HELIX 17 17 PRO B 42 ILE B 44 5 3
HELIX 18 18 GLN B 45 GLU B 55 1 11
HELIX 19 19 SER B 81 LEU B 88 1 8
HELIX 20 20 HIS B 97 PHE B 104 1 8
HELIX 21 21 THR B 107 HIS B 121 1 15
HELIX 22 22 THR B 132 SER B 138 1 7
HELIX 23 23 LYS B 140 VAL B 153 1 14
HELIX 24 24 SER B 157 VAL B 164 1 8
HELIX 25 25 PRO B 170 ILE B 174 5 5
HELIX 26 26 THR B 181 SER B 200 1 20
HELIX 27 27 SER B 201 GLU B 206 1 6
HELIX 28 28 ASN B 220 ALA B 226 1 7
HELIX 29 29 GLY B 236 LEU B 240 5 5
HELIX 30 30 LYS B 241 GLY B 251 1 11
SHEET 1 A 9 ILE A 5 ASN A 9 0
SHEET 2 A 9 GLU A 36 ALA A 41 1 O VAL A 38 N GLY A 8
SHEET 3 A 9 GLU A 62 ALA A 65 1 O GLY A 64 N ILE A 39
SHEET 4 A 9 TYR A 92 ILE A 95 1 O VAL A 94 N ALA A 65
SHEET 5 A 9 THR A 124 VAL A 129 1 O CYS A 128 N ILE A 95
SHEET 6 A 9 VAL A 165 TYR A 168 1 O VAL A 165 N ILE A 127
SHEET 7 A 9 ARG A 209 TYR A 212 1 O GLN A 211 N TYR A 168
SHEET 8 A 9 GLY A 232 VAL A 235 1 O GLY A 232 N TYR A 212
SHEET 9 A 9 ILE A 5 ASN A 9 1 N ASN A 9 O VAL A 235
SHEET 1 B 9 ILE B 5 ASN B 9 0
SHEET 2 B 9 GLU B 36 CYS B 40 1 O CYS B 40 N GLY B 8
SHEET 3 B 9 GLU B 62 ALA B 65 1 O GLY B 64 N ILE B 39
SHEET 4 B 9 TYR B 92 ILE B 95 1 O VAL B 94 N ALA B 65
SHEET 5 B 9 THR B 124 VAL B 129 1 O ILE B 126 N ILE B 95
SHEET 6 B 9 VAL B 165 TYR B 168 1 O VAL B 165 N ILE B 127
SHEET 7 B 9 ARG B 209 TYR B 212 1 O GLN B 211 N ILE B 166
SHEET 8 B 9 GLY B 232 VAL B 235 1 O GLY B 232 N TYR B 212
SHEET 9 B 9 ILE B 5 ASN B 9 1 N ASN B 9 O VAL B 235
LINK OG1 THR A 80 NA NA B 255 1555 1555 2.82
LINK O MET B 225 NA NA B 254 1555 1555 2.28
LINK O GLN B 227 NA NA B 254 1555 1555 2.54
LINK O ILE B 230 NA NA B 254 1555 1555 2.42
LINK NA NA B 254 O HOH B 305 1555 1555 2.42
LINK NA NA B 254 O HOH B 327 1555 1555 2.43
LINK NA NA B 254 O HOH B 359 1555 1555 2.58
SITE 1 AC1 6 MET B 225 GLN B 227 ILE B 230 HOH B 305
SITE 2 AC1 6 HOH B 327 HOH B 359
SITE 1 AC2 4 THR A 80 PRO B 42 ALA B 43 ILE B 44
SITE 1 AC3 12 LYS B 11 SER B 215 LYS B 217 GLY B 236
SITE 2 AC3 12 GLY B 237 HOH B 285 HOH B 301 HOH B 306
SITE 3 AC3 12 HOH B 354 HOH B 355 HOH B 365 HOH B 475
CRYST1 79.478 79.478 175.006 90.00 90.00 90.00 P 43 21 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 0.012582 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012582 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005714 0.00000
(ATOM LINES ARE NOT SHOWN.)
END