HEADER ISOMERASE 15-APR-13 4K6A
TITLE REVISED CRYSTAL STRUCTURE OF APO-FORM OF TRIOSEPHOSPHATE ISOMERASE
TITLE 2 (TPIA) FROM ESCHERICHIA COLI AT 1.8 ANGSTROM RESOLUTION.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRIOSEPHOSPHATE ISOMERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: TRIOSEPHOSPHATE ISOMERASE (TPIA);
COMPND 5 SYNONYM: TIM, TRIOSE-PHOSPHATE ISOMERASE;
COMPND 6 EC: 5.3.1.1;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 1110693;
SOURCE 4 STRAIN: K-12 SUBSTR. MG1655;
SOURCE 5 GENE: ECMDS42_3357, TPIA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 MAGIC;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS STRUCTURAL GENOMICS, NIAID, NATIONAL INSTITUTE OF ALLERGY AND
KEYWDS 2 INFECTIOUS DISEASES, CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS
KEYWDS 3 DISEASES, CSGID, TIM BETA/ALPHA BARREL, TRIOSE-PHOSPHATE ISOMERASE
KEYWDS 4 ACTIVITY, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.MINASOV,M.KUHN,A.HALAVATY,L.SHUVALOVA,I.DUBROVSKA,J.WINSOR,
AUTHOR 2 S.GRIMSHAW,W.F.ANDERSON,CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS
AUTHOR 3 DISEASES (CSGID)
REVDAT 3 20-SEP-23 4K6A 1 REMARK SEQADV LINK
REVDAT 2 06-SEP-17 4K6A 1 JRNL REMARK
REVDAT 1 01-MAY-13 4K6A 0
JRNL AUTH M.L.KUHN,B.ZEMAITAITIS,L.I.HU,A.SAHU,D.SORENSEN,G.MINASOV,
JRNL AUTH 2 B.P.LIMA,M.SCHOLLE,M.MRKSICH,W.F.ANDERSON,B.W.GIBSON,
JRNL AUTH 3 B.SCHILLING,A.J.WOLFE
JRNL TITL STRUCTURAL, KINETIC AND PROTEOMIC CHARACTERIZATION OF ACETYL
JRNL TITL 2 PHOSPHATE-DEPENDENT BACTERIAL PROTEIN ACETYLATION.
JRNL REF PLOS ONE V. 9 94816 2014
JRNL REFN ESSN 1932-6203
JRNL PMID 24756028
JRNL DOI 10.1371/JOURNAL.PONE.0094816
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.06
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 41906
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) : 0.151
REMARK 3 R VALUE (WORKING SET) : 0.149
REMARK 3 FREE R VALUE : 0.185
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2228
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3023
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.51
REMARK 3 BIN R VALUE (WORKING SET) : 0.1940
REMARK 3 BIN FREE R VALUE SET COUNT : 157
REMARK 3 BIN FREE R VALUE : 0.2360
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3786
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 546
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.87
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.02000
REMARK 3 B22 (A**2) : -0.16000
REMARK 3 B33 (A**2) : 0.13000
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): 0.122
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.113
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.071
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.006
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.951
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4175 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2752 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5691 ; 1.327 ; 1.949
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6789 ; 0.878 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 579 ; 2.769 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 176 ;33.452 ;25.114
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 724 ; 9.469 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;10.237 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 635 ; 0.080 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4933 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 805 ; 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): 2737 ; 0.973 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1124 ; 0.329 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4388 ; 1.584 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1438 ; 2.815 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1303 ; 4.664 ; 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 : 4
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 1 A 142
REMARK 3 ORIGIN FOR THE GROUP (A): 2.5585 -22.5557 17.9840
REMARK 3 T TENSOR
REMARK 3 T11: 0.0274 T22: 0.0223
REMARK 3 T33: 0.0052 T12: 0.0035
REMARK 3 T13: -0.0052 T23: 0.0031
REMARK 3 L TENSOR
REMARK 3 L11: 0.7111 L22: 0.7941
REMARK 3 L33: 0.5964 L12: 0.2294
REMARK 3 L13: -0.0946 L23: -0.0197
REMARK 3 S TENSOR
REMARK 3 S11: 0.0115 S12: -0.0562 S13: -0.0192
REMARK 3 S21: 0.0230 S22: 0.0202 S23: 0.0236
REMARK 3 S31: 0.1121 S32: -0.0090 S33: -0.0317
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 : A 143 A 255
REMARK 3 ORIGIN FOR THE GROUP (A): -0.7898 -36.1754 23.7996
REMARK 3 T TENSOR
REMARK 3 T11: 0.1073 T22: 0.0196
REMARK 3 T33: 0.0290 T12: -0.0003
REMARK 3 T13: -0.0097 T23: 0.0205
REMARK 3 L TENSOR
REMARK 3 L11: 0.8828 L22: 0.8986
REMARK 3 L33: 1.4945 L12: -0.1060
REMARK 3 L13: -0.3067 L23: 0.2971
REMARK 3 S TENSOR
REMARK 3 S11: 0.0291 S12: -0.0753 S13: -0.1128
REMARK 3 S21: 0.0544 S22: 0.0238 S23: -0.0088
REMARK 3 S31: 0.2526 S32: 0.0055 S33: -0.0529
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 142
REMARK 3 ORIGIN FOR THE GROUP (A): 14.8202 -2.6658 14.7919
REMARK 3 T TENSOR
REMARK 3 T11: 0.0166 T22: 0.0401
REMARK 3 T33: 0.0174 T12: 0.0131
REMARK 3 T13: 0.0091 T23: -0.0053
REMARK 3 L TENSOR
REMARK 3 L11: 0.8950 L22: 1.0503
REMARK 3 L33: 0.7608 L12: 0.0856
REMARK 3 L13: -0.0694 L23: 0.1821
REMARK 3 S TENSOR
REMARK 3 S11: -0.0155 S12: -0.0513 S13: 0.0332
REMARK 3 S21: -0.0418 S22: 0.0599 S23: -0.0060
REMARK 3 S31: -0.0338 S32: 0.0668 S33: -0.0443
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 143 B 255
REMARK 3 ORIGIN FOR THE GROUP (A): 22.5818 9.4145 18.5280
REMARK 3 T TENSOR
REMARK 3 T11: 0.0545 T22: 0.0718
REMARK 3 T33: 0.0683 T12: -0.0174
REMARK 3 T13: 0.0252 T23: -0.0357
REMARK 3 L TENSOR
REMARK 3 L11: 1.0513 L22: 1.6919
REMARK 3 L33: 1.2193 L12: -0.4696
REMARK 3 L13: 0.2250 L23: 0.2030
REMARK 3 S TENSOR
REMARK 3 S11: -0.0519 S12: -0.1071 S13: 0.1734
REMARK 3 S21: -0.0123 S22: 0.0959 S23: -0.1536
REMARK 3 S31: -0.2204 S32: 0.1251 S33: -0.0440
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 : 1.20
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
REMARK 4
REMARK 4 4K6A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-APR-13.
REMARK 100 THE DEPOSITION ID IS D_1000078944.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAR-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.03326
REMARK 200 MONOCHROMATOR : SI {1,1,1}
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44231
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.08800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.4
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 0.52900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
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: 1TRE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.96
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN: 7.6MG/ML, 0.5M SODIUM
REMARK 280 CLORIDE, 0.01M TRIS-HCL PH 8.3; SCREEN: PACT (D11), 0.2M CALCIUM
REMARK 280 CHLORIDE, 0.1M TRIS-HCL PH 8.0, 20% (W/V) PEG 6000., VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 295K
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 23.03300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 74.88450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.74400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 74.88450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.03300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 33.74400
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: 3420 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20070 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 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 MET 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 ASN A -1
REMARK 465 ALA A 0
REMARK 465 MET 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 465 ASN B -1
REMARK 465 ALA B 0
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 -145.05 51.96
REMARK 500 LYS B 11 -145.70 55.24
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 A 301 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 76 O
REMARK 620 2 HOH A 444 O 97.8
REMARK 620 3 HOH B 354 O 90.4 167.7
REMARK 620 4 HOH B 454 O 167.4 90.4 80.1
REMARK 620 5 HOH B 477 O 90.5 104.3 84.7 96.8
REMARK 620 6 HOH B 512 O 88.5 91.4 79.6 81.8 164.2
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 A 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1TRE RELATED DB: PDB
REMARK 900 STRUCTURE OF TRIOSEPHOSPHATE ISOMERASE FROM ESCHERICHIA COLI
REMARK 900 DETERMINED AT 2.6 A RESOLUTION.
REMARK 900 RELATED ID: IDP91829 RELATED DB: TARGETTRACK
REMARK 900 RELATED ID: CSGID-IDP91829 RELATED DB: TARGETTRACK
DBREF 4K6A A 1 255 UNP H0QFE6 H0QFE6_ECOLI 1 255
DBREF 4K6A B 1 255 UNP H0QFE6 H0QFE6_ECOLI 1 255
SEQADV 4K6A MET A -23 UNP H0QFE6 EXPRESSION TAG
SEQADV 4K6A HIS A -22 UNP H0QFE6 EXPRESSION TAG
SEQADV 4K6A HIS A -21 UNP H0QFE6 EXPRESSION TAG
SEQADV 4K6A HIS A -20 UNP H0QFE6 EXPRESSION TAG
SEQADV 4K6A HIS A -19 UNP H0QFE6 EXPRESSION TAG
SEQADV 4K6A HIS A -18 UNP H0QFE6 EXPRESSION TAG
SEQADV 4K6A HIS A -17 UNP H0QFE6 EXPRESSION TAG
SEQADV 4K6A SER A -16 UNP H0QFE6 EXPRESSION TAG
SEQADV 4K6A SER A -15 UNP H0QFE6 EXPRESSION TAG
SEQADV 4K6A GLY A -14 UNP H0QFE6 EXPRESSION TAG
SEQADV 4K6A VAL A -13 UNP H0QFE6 EXPRESSION TAG
SEQADV 4K6A ASP A -12 UNP H0QFE6 EXPRESSION TAG
SEQADV 4K6A LEU A -11 UNP H0QFE6 EXPRESSION TAG
SEQADV 4K6A GLY A -10 UNP H0QFE6 EXPRESSION TAG
SEQADV 4K6A THR A -9 UNP H0QFE6 EXPRESSION TAG
SEQADV 4K6A GLU A -8 UNP H0QFE6 EXPRESSION TAG
SEQADV 4K6A ASN A -7 UNP H0QFE6 EXPRESSION TAG
SEQADV 4K6A LEU A -6 UNP H0QFE6 EXPRESSION TAG
SEQADV 4K6A TYR A -5 UNP H0QFE6 EXPRESSION TAG
SEQADV 4K6A PHE A -4 UNP H0QFE6 EXPRESSION TAG
SEQADV 4K6A GLN A -3 UNP H0QFE6 EXPRESSION TAG
SEQADV 4K6A SER A -2 UNP H0QFE6 EXPRESSION TAG
SEQADV 4K6A ASN A -1 UNP H0QFE6 EXPRESSION TAG
SEQADV 4K6A ALA A 0 UNP H0QFE6 EXPRESSION TAG
SEQADV 4K6A MET B -23 UNP H0QFE6 EXPRESSION TAG
SEQADV 4K6A HIS B -22 UNP H0QFE6 EXPRESSION TAG
SEQADV 4K6A HIS B -21 UNP H0QFE6 EXPRESSION TAG
SEQADV 4K6A HIS B -20 UNP H0QFE6 EXPRESSION TAG
SEQADV 4K6A HIS B -19 UNP H0QFE6 EXPRESSION TAG
SEQADV 4K6A HIS B -18 UNP H0QFE6 EXPRESSION TAG
SEQADV 4K6A HIS B -17 UNP H0QFE6 EXPRESSION TAG
SEQADV 4K6A SER B -16 UNP H0QFE6 EXPRESSION TAG
SEQADV 4K6A SER B -15 UNP H0QFE6 EXPRESSION TAG
SEQADV 4K6A GLY B -14 UNP H0QFE6 EXPRESSION TAG
SEQADV 4K6A VAL B -13 UNP H0QFE6 EXPRESSION TAG
SEQADV 4K6A ASP B -12 UNP H0QFE6 EXPRESSION TAG
SEQADV 4K6A LEU B -11 UNP H0QFE6 EXPRESSION TAG
SEQADV 4K6A GLY B -10 UNP H0QFE6 EXPRESSION TAG
SEQADV 4K6A THR B -9 UNP H0QFE6 EXPRESSION TAG
SEQADV 4K6A GLU B -8 UNP H0QFE6 EXPRESSION TAG
SEQADV 4K6A ASN B -7 UNP H0QFE6 EXPRESSION TAG
SEQADV 4K6A LEU B -6 UNP H0QFE6 EXPRESSION TAG
SEQADV 4K6A TYR B -5 UNP H0QFE6 EXPRESSION TAG
SEQADV 4K6A PHE B -4 UNP H0QFE6 EXPRESSION TAG
SEQADV 4K6A GLN B -3 UNP H0QFE6 EXPRESSION TAG
SEQADV 4K6A SER B -2 UNP H0QFE6 EXPRESSION TAG
SEQADV 4K6A ASN B -1 UNP H0QFE6 EXPRESSION TAG
SEQADV 4K6A ALA B 0 UNP H0QFE6 EXPRESSION TAG
SEQRES 1 A 279 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 279 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA MET ARG
SEQRES 3 A 279 HIS PRO LEU VAL MET GLY ASN TRP LYS LEU ASN GLY SER
SEQRES 4 A 279 ARG HIS MET VAL HIS GLU LEU VAL SER ASN LEU ARG LYS
SEQRES 5 A 279 GLU LEU ALA GLY VAL ALA GLY CYS ALA VAL ALA ILE ALA
SEQRES 6 A 279 PRO PRO GLU MET TYR ILE ASP MET ALA LYS ARG GLU ALA
SEQRES 7 A 279 GLU GLY SER HIS ILE MET LEU GLY ALA GLN ASN VAL ASP
SEQRES 8 A 279 LEU ASN LEU SER GLY ALA PHE THR GLY GLU THR SER ALA
SEQRES 9 A 279 ALA MET LEU LYS ASP ILE GLY ALA GLN TYR ILE ILE ILE
SEQRES 10 A 279 GLY HIS SER GLU ARG ARG THR TYR HIS LYS GLU SER ASP
SEQRES 11 A 279 GLU LEU ILE ALA LYS LYS PHE ALA VAL LEU LYS GLU GLN
SEQRES 12 A 279 GLY LEU THR PRO VAL LEU CYS ILE GLY GLU THR GLU ALA
SEQRES 13 A 279 GLU ASN GLU ALA GLY LYS THR GLU GLU VAL CYS ALA ARG
SEQRES 14 A 279 GLN ILE ASP ALA VAL LEU LYS THR GLN GLY ALA ALA ALA
SEQRES 15 A 279 PHE GLU GLY ALA VAL ILE ALA TYR GLU PRO VAL TRP ALA
SEQRES 16 A 279 ILE GLY THR GLY LYS SER ALA THR PRO ALA GLN ALA GLN
SEQRES 17 A 279 ALA VAL HIS LYS PHE ILE ARG ASP HIS ILE ALA LYS VAL
SEQRES 18 A 279 ASP ALA ASN ILE ALA GLU GLN VAL ILE ILE GLN TYR GLY
SEQRES 19 A 279 GLY SER VAL ASN ALA SER ASN ALA ALA GLU LEU PHE ALA
SEQRES 20 A 279 GLN PRO ASP ILE ASP GLY ALA LEU VAL GLY GLY ALA SER
SEQRES 21 A 279 LEU LYS ALA ASP ALA PHE ALA VAL ILE VAL LYS ALA ALA
SEQRES 22 A 279 GLU ALA ALA LYS GLN ALA
SEQRES 1 B 279 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 B 279 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA MET ARG
SEQRES 3 B 279 HIS PRO LEU VAL MET GLY ASN TRP LYS LEU ASN GLY SER
SEQRES 4 B 279 ARG HIS MET VAL HIS GLU LEU VAL SER ASN LEU ARG LYS
SEQRES 5 B 279 GLU LEU ALA GLY VAL ALA GLY CYS ALA VAL ALA ILE ALA
SEQRES 6 B 279 PRO PRO GLU MET TYR ILE ASP MET ALA LYS ARG GLU ALA
SEQRES 7 B 279 GLU GLY SER HIS ILE MET LEU GLY ALA GLN ASN VAL ASP
SEQRES 8 B 279 LEU ASN LEU SER GLY ALA PHE THR GLY GLU THR SER ALA
SEQRES 9 B 279 ALA MET LEU LYS ASP ILE GLY ALA GLN TYR ILE ILE ILE
SEQRES 10 B 279 GLY HIS SER GLU ARG ARG THR TYR HIS LYS GLU SER ASP
SEQRES 11 B 279 GLU LEU ILE ALA LYS LYS PHE ALA VAL LEU LYS GLU GLN
SEQRES 12 B 279 GLY LEU THR PRO VAL LEU CYS ILE GLY GLU THR GLU ALA
SEQRES 13 B 279 GLU ASN GLU ALA GLY LYS THR GLU GLU VAL CYS ALA ARG
SEQRES 14 B 279 GLN ILE ASP ALA VAL LEU LYS THR GLN GLY ALA ALA ALA
SEQRES 15 B 279 PHE GLU GLY ALA VAL ILE ALA TYR GLU PRO VAL TRP ALA
SEQRES 16 B 279 ILE GLY THR GLY LYS SER ALA THR PRO ALA GLN ALA GLN
SEQRES 17 B 279 ALA VAL HIS LYS PHE ILE ARG ASP HIS ILE ALA LYS VAL
SEQRES 18 B 279 ASP ALA ASN ILE ALA GLU GLN VAL ILE ILE GLN TYR GLY
SEQRES 19 B 279 GLY SER VAL ASN ALA SER ASN ALA ALA GLU LEU PHE ALA
SEQRES 20 B 279 GLN PRO ASP ILE ASP GLY ALA LEU VAL GLY GLY ALA SER
SEQRES 21 B 279 LEU LYS ALA ASP ALA PHE ALA VAL ILE VAL LYS ALA ALA
SEQRES 22 B 279 GLU ALA ALA LYS GLN ALA
HET NA A 301 1
HETNAM NA SODIUM ION
FORMUL 3 NA NA 1+
FORMUL 4 HOH *546(H2 O)
HELIX 1 1 SER A 15 ALA A 31 1 17
HELIX 2 2 PRO A 43 MET A 45 5 3
HELIX 3 3 TYR A 46 GLU A 55 1 10
HELIX 4 4 SER A 79 GLY A 87 1 9
HELIX 5 5 HIS A 95 HIS A 102 1 8
HELIX 6 6 SER A 105 GLN A 119 1 15
HELIX 7 7 THR A 130 ALA A 136 1 7
HELIX 8 8 LYS A 138 GLY A 155 1 18
HELIX 9 9 ALA A 156 GLU A 160 5 5
HELIX 10 10 PRO A 168 ILE A 172 5 5
HELIX 11 11 THR A 179 LYS A 196 1 18
HELIX 12 12 ASP A 198 VAL A 205 1 8
HELIX 13 13 ASN A 217 ALA A 223 1 7
HELIX 14 14 GLY A 233 LEU A 237 5 5
HELIX 15 15 LYS A 238 GLN A 254 1 17
HELIX 16 16 SER B 15 LEU B 30 1 16
HELIX 17 17 PRO B 43 MET B 45 5 3
HELIX 18 18 TYR B 46 ALA B 54 1 9
HELIX 19 19 SER B 79 ILE B 86 1 8
HELIX 20 20 HIS B 95 HIS B 102 1 8
HELIX 21 21 SER B 105 GLY B 120 1 16
HELIX 22 22 THR B 130 ALA B 136 1 7
HELIX 23 23 LYS B 138 GLY B 155 1 18
HELIX 24 24 ALA B 156 GLU B 160 5 5
HELIX 25 25 PRO B 168 ILE B 172 5 5
HELIX 26 26 THR B 179 LYS B 196 1 18
HELIX 27 27 ASP B 198 VAL B 205 1 8
HELIX 28 28 ASN B 217 ALA B 223 1 7
HELIX 29 29 GLY B 233 LEU B 237 5 5
HELIX 30 30 LYS B 238 GLN B 254 1 17
SHEET 1 A 9 LEU A 5 ASN A 9 0
SHEET 2 A 9 ALA A 37 ALA A 41 1 O ALA A 39 N GLY A 8
SHEET 3 A 9 ILE A 59 ALA A 63 1 O MET A 60 N VAL A 38
SHEET 4 A 9 TYR A 90 ILE A 93 1 O ILE A 92 N ALA A 63
SHEET 5 A 9 THR A 122 ILE A 127 1 O CYS A 126 N ILE A 93
SHEET 6 A 9 VAL A 163 TYR A 166 1 O VAL A 163 N LEU A 125
SHEET 7 A 9 ILE A 206 TYR A 209 1 O GLN A 208 N ILE A 164
SHEET 8 A 9 GLY A 229 VAL A 232 1 O GLY A 229 N TYR A 209
SHEET 9 A 9 LEU A 5 ASN A 9 1 N MET A 7 O VAL A 232
SHEET 1 B 9 LEU B 5 ASN B 9 0
SHEET 2 B 9 ALA B 37 ALA B 41 1 O ALA B 39 N GLY B 8
SHEET 3 B 9 MET B 60 ALA B 63 1 O MET B 60 N VAL B 38
SHEET 4 B 9 TYR B 90 ILE B 93 1 O ILE B 92 N ALA B 63
SHEET 5 B 9 THR B 122 ILE B 127 1 O CYS B 126 N ILE B 93
SHEET 6 B 9 VAL B 163 TYR B 166 1 O VAL B 163 N LEU B 125
SHEET 7 B 9 ILE B 206 TYR B 209 1 O GLN B 208 N ILE B 164
SHEET 8 B 9 GLY B 229 VAL B 232 1 O GLY B 229 N TYR B 209
SHEET 9 B 9 LEU B 5 ASN B 9 1 N ASN B 9 O VAL B 232
LINK O GLY A 76 NA NA A 301 1555 1555 2.48
LINK NA NA A 301 O HOH A 444 1555 1555 2.07
LINK NA NA A 301 O HOH B 354 1555 1555 2.21
LINK NA NA A 301 O HOH B 454 1555 1555 2.68
LINK NA NA A 301 O HOH B 477 1555 1555 2.50
LINK NA NA A 301 O HOH B 512 1555 1555 2.44
SITE 1 AC1 6 GLY A 76 HOH A 444 HOH B 354 HOH B 454
SITE 2 AC1 6 HOH B 477 HOH B 512
CRYST1 46.066 67.488 149.769 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 0.021708 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014817 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006677 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
