HEADER HYDROLASE 04-OCT-10 3P32
TITLE HYDROLYSIS OF GTP TO GDP BY AN MCM-ASSOCIATED AND MEAB- AND MMAA-LIKE
TITLE 2 G-PROTEIN FROM MYCOBACTERIUM TUBERCULOSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE GTPASE RV1496/MT1543;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.6.-.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 GENE: MT1543, MTCY277.18, RV1496;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: AVA0421
KEYWDS STRUCTURAL GENOMICS, SEATTLE STRUCTURAL GENOMICS CENTER FOR
KEYWDS 2 INFECTIOUS DISEASE, SSGCID, MEAB, MMAA, METHYLMALONIC ACIDURIA
KEYWDS 3 PROTEIN A, GTPASE, G-PROTEIN, MCM, METHYLMALONYL-COA MUTASE,
KEYWDS 4 INCORRECTLY ASSIGNED AS AN ARGININE/ORNITHINE TRANSPORT SYSTEM
KEYWDS 5 ATPASE, METHYLMAOLONYL PATHWAY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)
REVDAT 4 06-SEP-23 3P32 1 REMARK SEQADV
REVDAT 3 03-JUN-15 3P32 1 JRNL
REVDAT 2 22-APR-15 3P32 1 JRNL VERSN
REVDAT 1 10-NOV-10 3P32 0
JRNL AUTH T.E.EDWARDS,L.BAUGH,J.BULLEN,R.O.BAYDO,P.WITTE,K.THOMPKINS,
JRNL AUTH 2 I.Q.PHAN,J.ABENDROTH,M.C.CLIFTON,B.SANKARAN,W.C.VAN VOORHIS,
JRNL AUTH 3 P.J.MYLER,B.L.STAKER,C.GRUNDNER,D.D.LORIMER
JRNL TITL CRYSTAL STRUCTURES OF MYCOBACTERIAL MEAB AND MMAA-LIKE
JRNL TITL 2 GTPASES.
JRNL REF J.STRUCT.FUNCT.GENOM. V. 16 91 2015
JRNL REFN ISSN 1345-711X
JRNL PMID 25832174
JRNL DOI 10.1007/S10969-015-9197-2
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) : 45.43
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 32897
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) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1670
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) : 2285
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.97
REMARK 3 BIN R VALUE (WORKING SET) : 0.3240
REMARK 3 BIN FREE R VALUE SET COUNT : 112
REMARK 3 BIN FREE R VALUE : 0.4100
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2255
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 48
REMARK 3 SOLVENT ATOMS : 140
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 36.61
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.81
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.38000
REMARK 3 B22 (A**2) : -1.23000
REMARK 3 B33 (A**2) : -0.15000
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): 0.130
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.121
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.080
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.836
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.937
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2348 ; 0.015 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3202 ; 1.406 ; 1.986
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 305 ; 5.680 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 92 ;33.275 ;23.478
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 354 ;13.131 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 21 ;18.526 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 391 ; 0.097 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1728 ; 0.006 ; 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): 1517 ; 0.923 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2418 ; 1.653 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 831 ; 2.423 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 783 ; 4.045 ; 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 10 A 165
REMARK 3 ORIGIN FOR THE GROUP (A): 20.5463 23.8091 -1.7719
REMARK 3 T TENSOR
REMARK 3 T11: 0.2732 T22: 0.1763
REMARK 3 T33: 0.2891 T12: 0.0820
REMARK 3 T13: -0.1117 T23: -0.0884
REMARK 3 L TENSOR
REMARK 3 L11: 1.0055 L22: 1.2442
REMARK 3 L33: 0.1662 L12: 0.0883
REMARK 3 L13: 0.4248 L23: -0.3716
REMARK 3 S TENSOR
REMARK 3 S11: 0.2217 S12: 0.2123 S13: -0.2637
REMARK 3 S21: 0.0242 S22: 0.0110 S23: -0.1816
REMARK 3 S31: 0.1485 S32: 0.1596 S33: -0.2327
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 166 A 257
REMARK 3 ORIGIN FOR THE GROUP (A): 9.7613 44.1240 -9.6764
REMARK 3 T TENSOR
REMARK 3 T11: 0.1757 T22: 0.2604
REMARK 3 T33: 0.2019 T12: -0.0152
REMARK 3 T13: -0.0088 T23: 0.0141
REMARK 3 L TENSOR
REMARK 3 L11: 0.1564 L22: 0.1936
REMARK 3 L33: 1.0748 L12: -0.1499
REMARK 3 L13: 0.3223 L23: -0.0242
REMARK 3 S TENSOR
REMARK 3 S11: -0.0431 S12: 0.0993 S13: 0.0281
REMARK 3 S21: 0.0470 S22: -0.0097 S23: 0.0078
REMARK 3 S31: -0.0279 S32: 0.0728 S33: 0.0528
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 : A 258 A 292
REMARK 3 ORIGIN FOR THE GROUP (A): 3.8486 24.5299 -1.4382
REMARK 3 T TENSOR
REMARK 3 T11: 0.2596 T22: 0.1551
REMARK 3 T33: 0.2324 T12: -0.0379
REMARK 3 T13: 0.0046 T23: 0.0156
REMARK 3 L TENSOR
REMARK 3 L11: 0.1940 L22: 2.6476
REMARK 3 L33: 1.6802 L12: -0.0145
REMARK 3 L13: 0.5151 L23: 1.7625
REMARK 3 S TENSOR
REMARK 3 S11: -0.0129 S12: -0.1148 S13: -0.0815
REMARK 3 S21: 0.0925 S22: 0.0715 S23: 0.1189
REMARK 3 S31: 0.1052 S32: -0.0202 S33: -0.0587
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 : A 293 A 333
REMARK 3 ORIGIN FOR THE GROUP (A): 1.2335 7.6293 -31.4455
REMARK 3 T TENSOR
REMARK 3 T11: 0.4361 T22: 0.0171
REMARK 3 T33: 0.1242 T12: 0.0822
REMARK 3 T13: -0.0487 T23: -0.0467
REMARK 3 L TENSOR
REMARK 3 L11: 0.1109 L22: 6.8560
REMARK 3 L33: 3.5112 L12: -2.4944
REMARK 3 L13: 1.2026 L23: 0.6828
REMARK 3 S TENSOR
REMARK 3 S11: 0.4105 S12: -0.0878 S13: -0.1350
REMARK 3 S21: -0.7498 S22: 0.0161 S23: 0.1040
REMARK 3 S31: 0.1477 S32: 0.2134 S33: -0.4266
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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:
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 3 U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 3P32 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-OCT-10.
REMARK 100 THE DEPOSITION ID IS D_1000061893.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-MAY-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97946
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32985
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 7.300
REMARK 200 R MERGE (I) : 0.04400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.1600
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) : 1.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.55500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.500
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 3MDO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22.0 MG/ML MYTUD00200AA1 PW25862
REMARK 280 AGAINST 48% PEG 200, 0.1 M NA/K PHOSPHATE PH 6.2, 0.2 M NACL,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 33.25000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 33.25000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 32.93000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 94.11000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 32.93000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 94.11000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 33.25000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 32.93000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 94.11000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 33.25000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 32.93000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 94.11000
REMARK 290 SMTRY3 8 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: 7210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26440 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -33.25000
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 -20
REMARK 465 ALA A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 MET A -12
REMARK 465 GLY A -11
REMARK 465 THR A -10
REMARK 465 LEU A -9
REMARK 465 GLU A -8
REMARK 465 ALA A -7
REMARK 465 GLN A -6
REMARK 465 THR A -5
REMARK 465 GLN A -4
REMARK 465 GLY A -3
REMARK 465 PRO A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 MET A 2
REMARK 465 ALA A 3
REMARK 465 ALA A 4
REMARK 465 SER A 5
REMARK 465 HIS A 6
REMARK 465 ASP A 7
REMARK 465 ASP A 8
REMARK 465 ASP A 9
REMARK 465 PRO A 96
REMARK 465 SER A 97
REMARK 465 SER A 98
REMARK 465 THR A 99
REMARK 465 ARG A 100
REMARK 465 THR A 101
REMARK 465 GLY A 102
REMARK 465 GLY A 103
REMARK 465 SER A 104
REMARK 465 ILE A 105
REMARK 465 LEU A 106
REMARK 465 GLY A 107
REMARK 465 ASP A 108
REMARK 465 LYS A 109
REMARK 465 THR A 110
REMARK 465 ARG A 111
REMARK 465 THR A 128
REMARK 465 SER A 129
REMARK 465 ARG A 334
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 23 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 28 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 37 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 41 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 50 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 95 CG OD1 OD2
REMARK 470 ARG A 114 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 124 CG CD NE CZ NH1 NH2
REMARK 470 VAL A 159 CG1 CG2
REMARK 470 LYS A 191 CG CD CE NZ
REMARK 470 GLU A 209 CG CD OE1 OE2
REMARK 470 LYS A 212 CG CD CE NZ
REMARK 470 ARG A 215 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 219 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 293 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 301 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 302 CG CD CE NZ
REMARK 470 GLN A 324 CG CD OE1 NE2
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 ASP A 185 18.10 -141.47
REMARK 500 LYS A 205 35.78 76.95
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 VAL A 161 GLY A 162 148.34
REMARK 500 GLY A 162 GLN A 163 143.68
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 GDP A 335
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A 336
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A 337
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3MDO RELATED DB: PDB
REMARK 900 STRUCTURE CRYSTALLIZED IN THE PRESENCE OF GDP
REMARK 900 RELATED ID: 3NXS RELATED DB: PDB
REMARK 900 STRUCTURE OF SAME PROTEIN FROM MYCOBACTERIUM SMEGATIS BOUND TO GDP
REMARK 900 RELATED ID: 2GM7 RELATED DB: PDB
REMARK 900 MEAB, A BACTERIAL HOMOLOG OF MMAA, BOUND TO GDP
REMARK 900 RELATED ID: 2WWW RELATED DB: PDB
REMARK 900 HUMAN METHYLMALONIC ACIDEMIA TYPE A PROTEIN MMAA
REMARK 900 RELATED ID: MYTUD.00200.A RELATED DB: TARGETDB
DBREF 3P32 A 1 334 UNP P63577 Y1496_MYCTU 1 334
SEQADV 3P32 MET A -20 UNP P63577 EXPRESSION TAG
SEQADV 3P32 ALA A -19 UNP P63577 EXPRESSION TAG
SEQADV 3P32 HIS A -18 UNP P63577 EXPRESSION TAG
SEQADV 3P32 HIS A -17 UNP P63577 EXPRESSION TAG
SEQADV 3P32 HIS A -16 UNP P63577 EXPRESSION TAG
SEQADV 3P32 HIS A -15 UNP P63577 EXPRESSION TAG
SEQADV 3P32 HIS A -14 UNP P63577 EXPRESSION TAG
SEQADV 3P32 HIS A -13 UNP P63577 EXPRESSION TAG
SEQADV 3P32 MET A -12 UNP P63577 EXPRESSION TAG
SEQADV 3P32 GLY A -11 UNP P63577 EXPRESSION TAG
SEQADV 3P32 THR A -10 UNP P63577 EXPRESSION TAG
SEQADV 3P32 LEU A -9 UNP P63577 EXPRESSION TAG
SEQADV 3P32 GLU A -8 UNP P63577 EXPRESSION TAG
SEQADV 3P32 ALA A -7 UNP P63577 EXPRESSION TAG
SEQADV 3P32 GLN A -6 UNP P63577 EXPRESSION TAG
SEQADV 3P32 THR A -5 UNP P63577 EXPRESSION TAG
SEQADV 3P32 GLN A -4 UNP P63577 EXPRESSION TAG
SEQADV 3P32 GLY A -3 UNP P63577 EXPRESSION TAG
SEQADV 3P32 PRO A -2 UNP P63577 EXPRESSION TAG
SEQADV 3P32 GLY A -1 UNP P63577 EXPRESSION TAG
SEQADV 3P32 SER A 0 UNP P63577 EXPRESSION TAG
SEQRES 1 A 355 MET ALA HIS HIS HIS HIS HIS HIS MET GLY THR LEU GLU
SEQRES 2 A 355 ALA GLN THR GLN GLY PRO GLY SER MET MET ALA ALA SER
SEQRES 3 A 355 HIS ASP ASP ASP THR VAL ASP GLY LEU ALA THR ALA VAL
SEQRES 4 A 355 ARG GLY GLY ASP ARG ALA ALA LEU PRO ARG ALA ILE THR
SEQRES 5 A 355 LEU VAL GLU SER THR ARG PRO ASP HIS ARG GLU GLN ALA
SEQRES 6 A 355 GLN GLN LEU LEU LEU ARG LEU LEU PRO ASP SER GLY ASN
SEQRES 7 A 355 ALA HIS ARG VAL GLY ILE THR GLY VAL PRO GLY VAL GLY
SEQRES 8 A 355 LYS SER THR ALA ILE GLU ALA LEU GLY MET HIS LEU ILE
SEQRES 9 A 355 GLU ARG GLY HIS ARG VAL ALA VAL LEU ALA VAL ASP PRO
SEQRES 10 A 355 SER SER THR ARG THR GLY GLY SER ILE LEU GLY ASP LYS
SEQRES 11 A 355 THR ARG MET ALA ARG LEU ALA VAL HIS PRO ASN ALA TYR
SEQRES 12 A 355 ILE ARG PRO SER PRO THR SER GLY THR LEU GLY GLY VAL
SEQRES 13 A 355 THR ARG ALA THR ARG GLU THR VAL VAL LEU LEU GLU ALA
SEQRES 14 A 355 ALA GLY PHE ASP VAL ILE LEU ILE GLU THR VAL GLY VAL
SEQRES 15 A 355 GLY GLN SER GLU VAL ALA VAL ALA ASN MET VAL ASP THR
SEQRES 16 A 355 PHE VAL LEU LEU THR LEU ALA ARG THR GLY ASP GLN LEU
SEQRES 17 A 355 GLN GLY ILE LYS LYS GLY VAL LEU GLU LEU ALA ASP ILE
SEQRES 18 A 355 VAL VAL VAL ASN LYS ALA ASP GLY GLU HIS HIS LYS GLU
SEQRES 19 A 355 ALA ARG LEU ALA ALA ARG GLU LEU SER ALA ALA ILE ARG
SEQRES 20 A 355 LEU ILE TYR PRO ARG GLU ALA LEU TRP ARG PRO PRO VAL
SEQRES 21 A 355 LEU THR MET SER ALA VAL GLU GLY ARG GLY LEU ALA GLU
SEQRES 22 A 355 LEU TRP ASP THR VAL GLU ARG HIS ARG GLN VAL LEU THR
SEQRES 23 A 355 GLY ALA GLY GLU PHE ASP ALA ARG ARG ARG ASP GLN GLN
SEQRES 24 A 355 VAL ASP TRP THR TRP GLN LEU VAL ARG ASP ALA VAL LEU
SEQRES 25 A 355 ASP ARG VAL TRP SER ASN PRO THR VAL ARG LYS VAL ARG
SEQRES 26 A 355 SER GLU LEU GLU ARG ARG VAL ARG ALA GLY GLU LEU THR
SEQRES 27 A 355 PRO ALA LEU ALA ALA GLN GLN ILE LEU GLU ILE ALA ASN
SEQRES 28 A 355 LEU THR ASP ARG
HET GDP A 335 28
HET PGE A 336 20
HET PGE A 337 10
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
HETNAM PGE TRIETHYLENE GLYCOL
FORMUL 2 GDP C10 H15 N5 O11 P2
FORMUL 3 PGE 2(C6 H14 O4)
FORMUL 5 HOH *140(H2 O)
HELIX 1 1 THR A 10 GLY A 20 1 11
HELIX 2 2 ALA A 24 SER A 35 1 12
HELIX 3 3 ARG A 37 LEU A 52 1 16
HELIX 4 4 PRO A 53 SER A 55 5 3
HELIX 5 5 GLY A 70 GLU A 84 1 15
HELIX 6 6 MET A 112 VAL A 117 1 6
HELIX 7 7 THR A 131 ALA A 149 1 19
HELIX 8 8 GLN A 163 ASN A 170 1 8
HELIX 9 9 VAL A 194 ALA A 198 5 5
HELIX 10 10 ASP A 207 GLU A 209 5 3
HELIX 11 11 HIS A 210 TYR A 229 1 20
HELIX 12 12 SER A 243 GLY A 247 5 5
HELIX 13 13 GLY A 249 ALA A 267 1 19
HELIX 14 14 GLY A 268 SER A 296 1 29
HELIX 15 15 ASN A 297 ALA A 313 1 17
HELIX 16 16 THR A 317 ASP A 333 1 17
SHEET 1 A 7 ALA A 121 ARG A 124 0
SHEET 2 A 7 VAL A 89 VAL A 94 1 N VAL A 91 O TYR A 122
SHEET 3 A 7 VAL A 153 THR A 158 1 O LEU A 155 N ALA A 90
SHEET 4 A 7 HIS A 59 THR A 64 1 N VAL A 61 O ILE A 154
SHEET 5 A 7 THR A 174 LEU A 180 1 O VAL A 176 N GLY A 62
SHEET 6 A 7 ILE A 200 ASN A 204 1 O VAL A 202 N LEU A 177
SHEET 7 A 7 VAL A 239 MET A 242 1 O LEU A 240 N VAL A 203
SITE 1 AC1 15 GLY A 68 VAL A 69 GLY A 70 LYS A 71
SITE 2 AC1 15 SER A 72 THR A 73 ASN A 204 LYS A 205
SITE 3 AC1 15 ASP A 207 SER A 243 ALA A 244 VAL A 245
SITE 4 AC1 15 HOH A 415 HOH A 460 HOH A 461
SITE 1 AC2 7 GLU A 232 ALA A 233 LEU A 234 TRP A 235
SITE 2 AC2 7 ARG A 236 HOH A 475 HOH A 476
SITE 1 AC3 11 LYS A 192 GLU A 196 LEU A 197 ALA A 198
SITE 2 AC3 11 ASP A 199 TYR A 229 GLU A 232 TRP A 235
SITE 3 AC3 11 ARG A 273 HOH A 382 HOH A 474
CRYST1 65.860 188.220 66.500 90.00 90.00 90.00 C 2 2 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 0.015184 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005313 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015038 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
