HEADER ISOMERASE 23-SEP-13 4MVA
TITLE 1.43 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF TRIOSEPHOSPHATE
TITLE 2 ISOMERASE (TPIA) FROM ESCHERICHIA COLI IN COMPLEX WITH ACETYL
TITLE 3 PHOSPHATE.
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: 595496;
SOURCE 4 STRAIN: K-12 SUBSTR. MG1655;
SOURCE 5 GENE: BWG_3588, 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.L.KUHN,I.DUBROVSKA,J.WINSOR,L.SHUVALOVA,S.GRIMSHAW,
AUTHOR 2 K.KWON,W.F.ANDERSON,CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS
AUTHOR 3 DISEASES (CSGID)
REVDAT 4 20-SEP-23 4MVA 1 REMARK SEQADV
REVDAT 3 15-NOV-17 4MVA 1 REMARK
REVDAT 2 30-APR-14 4MVA 1 JRNL
REVDAT 1 16-APR-14 4MVA 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. 1.43 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0046
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) : 1.43
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.24
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 83946
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) : 0.136
REMARK 3 R VALUE (WORKING SET) : 0.135
REMARK 3 FREE R VALUE : 0.156
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4433
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) : 1.43
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.47
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6138
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.98
REMARK 3 BIN R VALUE (WORKING SET) : 0.1920
REMARK 3 BIN FREE R VALUE SET COUNT : 326
REMARK 3 BIN FREE R VALUE : 0.2110
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3780
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 37
REMARK 3 SOLVENT ATOMS : 837
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.02
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.09000
REMARK 3 B22 (A**2) : 0.66000
REMARK 3 B33 (A**2) : -0.57000
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): 0.057
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.057
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.037
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.842
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.979
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.973
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4429 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4304 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6035 ; 1.471 ; 1.956
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9947 ; 0.762 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 616 ; 3.588 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 184 ;36.623 ;25.543
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 779 ; 9.701 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;10.242 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 667 ; 0.083 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5319 ; 0.017 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 961 ; 0.016 ; 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): 2344 ; 1.261 ; 1.210
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2343 ; 1.258 ; 1.208
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3000 ; 2.043 ; 1.809
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3001 ; 2.044 ; 1.811
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2085 ; 2.084 ; 1.456
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2085 ; 2.084 ; 1.456
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3036 ; 3.129 ; 2.082
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 5831 ; 6.988 ;12.896
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 5178 ; 6.384 ;10.660
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): 2.1178 -22.7517 17.8125
REMARK 3 T TENSOR
REMARK 3 T11: 0.0175 T22: 0.0171
REMARK 3 T33: 0.0144 T12: 0.0027
REMARK 3 T13: -0.0095 T23: 0.0006
REMARK 3 L TENSOR
REMARK 3 L11: 0.2928 L22: 0.5839
REMARK 3 L33: 0.2895 L12: 0.2313
REMARK 3 L13: -0.0967 L23: 0.0440
REMARK 3 S TENSOR
REMARK 3 S11: -0.0038 S12: -0.0404 S13: -0.0063
REMARK 3 S21: 0.0186 S22: 0.0180 S23: 0.0115
REMARK 3 S31: 0.0477 S32: 0.0026 S33: -0.0142
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 254
REMARK 3 ORIGIN FOR THE GROUP (A): -0.7196 -35.8764 23.8375
REMARK 3 T TENSOR
REMARK 3 T11: 0.0541 T22: 0.0098
REMARK 3 T33: 0.0158 T12: -0.0051
REMARK 3 T13: -0.0037 T23: 0.0117
REMARK 3 L TENSOR
REMARK 3 L11: 0.6055 L22: 0.6608
REMARK 3 L33: 0.7388 L12: -0.1188
REMARK 3 L13: -0.1856 L23: 0.0754
REMARK 3 S TENSOR
REMARK 3 S11: -0.0045 S12: -0.0574 S13: -0.0720
REMARK 3 S21: 0.0685 S22: 0.0293 S23: 0.0158
REMARK 3 S31: 0.1525 S32: -0.0278 S33: -0.0248
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): 14.4600 -2.8608 14.5349
REMARK 3 T TENSOR
REMARK 3 T11: 0.0097 T22: 0.0111
REMARK 3 T33: 0.0117 T12: 0.0009
REMARK 3 T13: 0.0014 T23: -0.0067
REMARK 3 L TENSOR
REMARK 3 L11: 0.5084 L22: 0.7393
REMARK 3 L33: 0.3143 L12: 0.1259
REMARK 3 L13: -0.0623 L23: 0.1841
REMARK 3 S TENSOR
REMARK 3 S11: -0.0008 S12: -0.0308 S13: 0.0211
REMARK 3 S21: -0.0394 S22: 0.0458 S23: 0.0024
REMARK 3 S31: -0.0168 S32: 0.0383 S33: -0.0450
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): 22.1826 9.0532 18.6170
REMARK 3 T TENSOR
REMARK 3 T11: 0.0485 T22: 0.0409
REMARK 3 T33: 0.0553 T12: -0.0149
REMARK 3 T13: 0.0170 T23: -0.0196
REMARK 3 L TENSOR
REMARK 3 L11: 1.0619 L22: 0.8804
REMARK 3 L33: 0.7399 L12: -0.2577
REMARK 3 L13: 0.4857 L23: 0.0715
REMARK 3 S TENSOR
REMARK 3 S11: -0.0475 S12: -0.0518 S13: 0.1123
REMARK 3 S21: 0.0180 S22: 0.0463 S23: -0.0826
REMARK 3 S31: -0.1311 S32: 0.1015 S33: 0.0013
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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 4MVA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-OCT-13.
REMARK 100 THE DEPOSITION ID IS D_1000082409.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-MAR-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
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-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97856
REMARK 200 MONOCHROMATOR : DIAMOND
REMARK 200 OPTICS : BERYLLIUM LENSES
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 : 88659
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.430
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 : 6.100
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.43
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.45
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.00
REMARK 200 R MERGE FOR SHELL (I) : 0.53400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.400
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 ENTRY 1TRE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN: 7.4MG/ML, 0.15M SODIUM
REMARK 280 CLORIDE, 0.01M TRIS-HCL PH 8.3; SCREEN: CLASSICS II (F11), 0.2M
REMARK 280 SODIUM CHLORIDE, 0.1M BIS-TRIS PH 6.5, 25% (W/V) PEG 3350, 10MM
REMARK 280 ACP, VAPOR 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 23.26750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 75.16800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.76450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 75.16800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.26750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 33.76450
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: 4920 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20150 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 465 ALA B 255
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 -146.06 52.75
REMARK 500 ASN A 214 -142.71 -154.31
REMARK 500 LYS B 11 -146.66 52.47
REMARK 500 GLN B 89 -47.32 -134.98
REMARK 500 THR B 100 -70.53 -84.01
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UVW A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UVW B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 303
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4K6A RELATED DB: PDB
REMARK 900 REVISED CRYSTAL STRUCTURE OF APO-FORM OF TRIOSEPHOSPHATE ISOMERASE
REMARK 900 (TPIA) FROM ESCHERICHIA COLI AT 1.8 ANGSTROM RESOLUTION.
REMARK 900 RELATED ID: IDP91829 RELATED DB: TARGETTRACK
DBREF 4MVA A 1 255 UNP C5A086 C5A086_ECOBW 1 255
DBREF 4MVA B 1 255 UNP C5A086 C5A086_ECOBW 1 255
SEQADV 4MVA MET A -23 UNP C5A086 EXPRESSION TAG
SEQADV 4MVA HIS A -22 UNP C5A086 EXPRESSION TAG
SEQADV 4MVA HIS A -21 UNP C5A086 EXPRESSION TAG
SEQADV 4MVA HIS A -20 UNP C5A086 EXPRESSION TAG
SEQADV 4MVA HIS A -19 UNP C5A086 EXPRESSION TAG
SEQADV 4MVA HIS A -18 UNP C5A086 EXPRESSION TAG
SEQADV 4MVA HIS A -17 UNP C5A086 EXPRESSION TAG
SEQADV 4MVA SER A -16 UNP C5A086 EXPRESSION TAG
SEQADV 4MVA SER A -15 UNP C5A086 EXPRESSION TAG
SEQADV 4MVA GLY A -14 UNP C5A086 EXPRESSION TAG
SEQADV 4MVA VAL A -13 UNP C5A086 EXPRESSION TAG
SEQADV 4MVA ASP A -12 UNP C5A086 EXPRESSION TAG
SEQADV 4MVA LEU A -11 UNP C5A086 EXPRESSION TAG
SEQADV 4MVA GLY A -10 UNP C5A086 EXPRESSION TAG
SEQADV 4MVA THR A -9 UNP C5A086 EXPRESSION TAG
SEQADV 4MVA GLU A -8 UNP C5A086 EXPRESSION TAG
SEQADV 4MVA ASN A -7 UNP C5A086 EXPRESSION TAG
SEQADV 4MVA LEU A -6 UNP C5A086 EXPRESSION TAG
SEQADV 4MVA TYR A -5 UNP C5A086 EXPRESSION TAG
SEQADV 4MVA PHE A -4 UNP C5A086 EXPRESSION TAG
SEQADV 4MVA GLN A -3 UNP C5A086 EXPRESSION TAG
SEQADV 4MVA SER A -2 UNP C5A086 EXPRESSION TAG
SEQADV 4MVA ASN A -1 UNP C5A086 EXPRESSION TAG
SEQADV 4MVA ALA A 0 UNP C5A086 EXPRESSION TAG
SEQADV 4MVA MET B -23 UNP C5A086 EXPRESSION TAG
SEQADV 4MVA HIS B -22 UNP C5A086 EXPRESSION TAG
SEQADV 4MVA HIS B -21 UNP C5A086 EXPRESSION TAG
SEQADV 4MVA HIS B -20 UNP C5A086 EXPRESSION TAG
SEQADV 4MVA HIS B -19 UNP C5A086 EXPRESSION TAG
SEQADV 4MVA HIS B -18 UNP C5A086 EXPRESSION TAG
SEQADV 4MVA HIS B -17 UNP C5A086 EXPRESSION TAG
SEQADV 4MVA SER B -16 UNP C5A086 EXPRESSION TAG
SEQADV 4MVA SER B -15 UNP C5A086 EXPRESSION TAG
SEQADV 4MVA GLY B -14 UNP C5A086 EXPRESSION TAG
SEQADV 4MVA VAL B -13 UNP C5A086 EXPRESSION TAG
SEQADV 4MVA ASP B -12 UNP C5A086 EXPRESSION TAG
SEQADV 4MVA LEU B -11 UNP C5A086 EXPRESSION TAG
SEQADV 4MVA GLY B -10 UNP C5A086 EXPRESSION TAG
SEQADV 4MVA THR B -9 UNP C5A086 EXPRESSION TAG
SEQADV 4MVA GLU B -8 UNP C5A086 EXPRESSION TAG
SEQADV 4MVA ASN B -7 UNP C5A086 EXPRESSION TAG
SEQADV 4MVA LEU B -6 UNP C5A086 EXPRESSION TAG
SEQADV 4MVA TYR B -5 UNP C5A086 EXPRESSION TAG
SEQADV 4MVA PHE B -4 UNP C5A086 EXPRESSION TAG
SEQADV 4MVA GLN B -3 UNP C5A086 EXPRESSION TAG
SEQADV 4MVA SER B -2 UNP C5A086 EXPRESSION TAG
SEQADV 4MVA ASN B -1 UNP C5A086 EXPRESSION TAG
SEQADV 4MVA ALA B 0 UNP C5A086 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 CL A 301 2
HET UVW A 302 8
HET PO4 A 303 5
HET EDO A 304 4
HET UVW B 301 8
HET EDO B 302 4
HET PEG B 303 7
HETNAM CL CHLORIDE ION
HETNAM UVW ACETYLPHOSPHATE
HETNAM PO4 PHOSPHATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 CL CL 1-
FORMUL 4 UVW 2(C2 H5 O5 P)
FORMUL 5 PO4 O4 P 3-
FORMUL 6 EDO 2(C2 H6 O2)
FORMUL 9 PEG C4 H10 O3
FORMUL 10 HOH *837(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 GLY B 87 1 9
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 37 N VAL A 6
SHEET 3 A 9 MET A 60 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 ASN A 9 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 41 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 ALA B 88 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 MET B 7 O VAL B 232
SITE 1 AC1 6 GLU A 21 LEU A 22 ASN A 25 ALA A 239
SITE 2 AC1 6 HOH A 535 HOH A 595
SITE 1 AC2 12 LYS A 11 SER A 212 GLY A 233 GLY A 234
SITE 2 AC2 12 HOH A 427 HOH A 429 HOH A 438 HOH A 441
SITE 3 AC2 12 HOH A 651 HOH A 702 HOH A 835 HOH A 836
SITE 1 AC3 3 ARG A 16 HOH A 839 ARG B 52
SITE 1 AC4 4 HIS A 17 ARG A 52 HOH A 740 HOH A 837
SITE 1 AC5 10 LYS B 11 ILE B 172 SER B 212 GLY B 233
SITE 2 AC5 10 GLY B 234 PEG B 303 HOH B 435 HOH B 559
SITE 3 AC5 10 HOH B 570 HOH B 756
SITE 1 AC6 6 SER A 177 ALA A 178 THR A 179 ASN B 214
SITE 2 AC6 6 SER B 216 ASN B 217
SITE 1 AC7 11 LYS B 11 HIS B 95 GLY B 233 GLY B 234
SITE 2 AC7 11 UVW B 301 HOH B 403 HOH B 435 HOH B 519
SITE 3 AC7 11 HOH B 570 HOH B 684 HOH B 756
CRYST1 46.535 67.529 150.336 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 0.021489 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014808 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006652 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
