HEADER PROTEIN TRANSPORT 15-SEP-04 1VMA
TITLE CRYSTAL STRUCTURE OF CELL DIVISION PROTEIN FTSY (TM0570) FROM
TITLE 2 THERMOTOGA MARITIMA AT 1.60 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CELL DIVISION PROTEIN FTSY;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA;
SOURCE 3 ORGANISM_TAXID: 2336;
SOURCE 4 GENE: TM0570;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS TM0570, CELL DIVISION PROTEIN FTSY, STRUCTURAL GENOMICS, JCSG,
KEYWDS 2 PROTEIN STRUCTURE INITIATIVE, PSI, JOINT CENTER FOR STRUCTURAL
KEYWDS 3 GENOMICS, PROTEIN TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 6 23-AUG-23 1VMA 1 REMARK SEQADV LINK
REVDAT 5 13-JUL-11 1VMA 1 VERSN
REVDAT 4 24-FEB-09 1VMA 1 VERSN
REVDAT 3 28-MAR-06 1VMA 1 JRNL
REVDAT 2 18-JAN-05 1VMA 1 AUTHOR KEYWDS REMARK
REVDAT 1 28-SEP-04 1VMA 0
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
JRNL TITL CRYSTAL STRUCTURE OF CELL DIVISION PROTEIN FTSY (TM0570)
JRNL TITL 2 FROM THERMOTOGA MARITIMA AT 1.60 A RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC (5.2.0001)
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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.88
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 79919
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) : 0.209
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4219
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) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5765
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2530
REMARK 3 BIN FREE R VALUE SET COUNT : 327
REMARK 3 BIN FREE R VALUE : 0.3090
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4408
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 14
REMARK 3 SOLVENT ATOMS : 394
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 28.56
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.77
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.75000
REMARK 3 B22 (A**2) : -0.44000
REMARK 3 B33 (A**2) : -0.28000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.06000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.096
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.102
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.082
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.645
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.928
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4529 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 4396 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6133 ; 1.660 ; 1.979
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10205 ; 0.845 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 586 ; 5.904 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 173 ;30.222 ;25.491
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 831 ;14.474 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;14.058 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 755 ; 0.100 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4964 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 810 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1148 ; 0.224 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 4679 ; 0.177 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 2710 ; 0.087 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 283 ; 0.130 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 1 ; 0.085 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 16 ; 0.234 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 50 ; 0.237 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 20 ; 0.183 ; 0.200
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): 3009 ; 2.371 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1208 ; 0.723 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4720 ; 3.202 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1673 ; 5.106 ; 8.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1413 ; 7.219 ;11.000
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 : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
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 82
REMARK 3 ORIGIN FOR THE GROUP (A): 7.7831 -0.8535 1.3226
REMARK 3 T TENSOR
REMARK 3 T11: -0.0449 T22: -0.1049
REMARK 3 T33: -0.1777 T12: 0.0282
REMARK 3 T13: -0.0006 T23: 0.0017
REMARK 3 L TENSOR
REMARK 3 L11: 1.4537 L22: 1.7393
REMARK 3 L33: 1.5782 L12: 0.2817
REMARK 3 L13: -0.1920 L23: -0.0271
REMARK 3 S TENSOR
REMARK 3 S11: 0.0196 S12: 0.1676 S13: -0.0471
REMARK 3 S21: -0.3305 S22: -0.0606 S23: -0.0281
REMARK 3 S31: 0.0404 S32: 0.0971 S33: 0.0409
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 83 A 282
REMARK 3 ORIGIN FOR THE GROUP (A): -7.4407 1.3693 26.7954
REMARK 3 T TENSOR
REMARK 3 T11: -0.0846 T22: -0.0567
REMARK 3 T33: -0.0646 T12: 0.0009
REMARK 3 T13: 0.0748 T23: -0.0172
REMARK 3 L TENSOR
REMARK 3 L11: 0.7539 L22: 2.1553
REMARK 3 L33: 2.0946 L12: -0.1021
REMARK 3 L13: -0.4383 L23: -0.2179
REMARK 3 S TENSOR
REMARK 3 S11: 0.0371 S12: -0.0970 S13: -0.0512
REMARK 3 S21: 0.3735 S22: -0.0402 S23: 0.4638
REMARK 3 S31: -0.1511 S32: -0.2265 S33: 0.0031
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 283 A 294
REMARK 3 ORIGIN FOR THE GROUP (A): 0.2483 -6.6338 3.1385
REMARK 3 T TENSOR
REMARK 3 T11: -0.0566 T22: -0.1173
REMARK 3 T33: -0.1271 T12: 0.0119
REMARK 3 T13: -0.0350 T23: -0.0144
REMARK 3 L TENSOR
REMARK 3 L11: 1.8609 L22: 3.4407
REMARK 3 L33: 8.3237 L12: 2.0194
REMARK 3 L13: -1.8316 L23: 0.8666
REMARK 3 S TENSOR
REMARK 3 S11: -0.0310 S12: 0.1066 S13: -0.1713
REMARK 3 S21: -0.2949 S22: -0.1296 S23: 0.0671
REMARK 3 S31: 0.2148 S32: 0.0757 S33: 0.1606
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 1 B 82
REMARK 3 ORIGIN FOR THE GROUP (A): 17.8105 -2.0668 41.7072
REMARK 3 T TENSOR
REMARK 3 T11: 0.1631 T22: -0.0591
REMARK 3 T33: -0.0612 T12: -0.0387
REMARK 3 T13: -0.1340 T23: 0.0053
REMARK 3 L TENSOR
REMARK 3 L11: 1.4326 L22: 1.0813
REMARK 3 L33: 1.7578 L12: -0.5131
REMARK 3 L13: -0.3252 L23: -0.1618
REMARK 3 S TENSOR
REMARK 3 S11: 0.0171 S12: -0.2845 S13: -0.0165
REMARK 3 S21: 0.3843 S22: -0.0044 S23: -0.0916
REMARK 3 S31: 0.2071 S32: -0.0194 S33: -0.0126
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 83 B 282
REMARK 3 ORIGIN FOR THE GROUP (A): 32.8553 0.5503 16.1629
REMARK 3 T TENSOR
REMARK 3 T11: -0.1290 T22: -0.0691
REMARK 3 T33: 0.1073 T12: -0.0058
REMARK 3 T13: -0.0417 T23: -0.0020
REMARK 3 L TENSOR
REMARK 3 L11: 0.8160 L22: 1.4307
REMARK 3 L33: 2.2181 L12: -0.0806
REMARK 3 L13: -0.3187 L23: 0.4966
REMARK 3 S TENSOR
REMARK 3 S11: 0.0508 S12: 0.0397 S13: 0.0271
REMARK 3 S21: 0.0535 S22: 0.0773 S23: -0.5734
REMARK 3 S31: -0.0327 S32: 0.2750 S33: -0.1280
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 283 B 294
REMARK 3 ORIGIN FOR THE GROUP (A): 25.0913 -8.2797 39.2181
REMARK 3 T TENSOR
REMARK 3 T11: 0.2101 T22: -0.0737
REMARK 3 T33: -0.0080 T12: 0.0144
REMARK 3 T13: -0.1834 T23: 0.0316
REMARK 3 L TENSOR
REMARK 3 L11: 1.2430 L22: 3.3465
REMARK 3 L33: 5.9593 L12: -1.3140
REMARK 3 L13: -1.6751 L23: 2.8516
REMARK 3 S TENSOR
REMARK 3 S11: 0.0326 S12: -0.2538 S13: -0.1083
REMARK 3 S21: 0.1565 S22: -0.0664 S23: -0.0111
REMARK 3 S31: 0.4574 S32: 0.2412 S33: 0.0338
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 1VMA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-SEP-04.
REMARK 100 THE DEPOSITION ID IS D_1000002006.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-APR-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000034
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA (CCP4 4.2), CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 84144
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 24.880
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 8.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.6
REMARK 200 DATA REDUNDANCY IN SHELL : 7.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.42700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.200
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 1FTS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10.0% PEG-6000, 0.1M CITRATE, PH 5.0,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, NANODROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 24.05100
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: MONOMERIC
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 -11
REMARK 465 GLY A -10
REMARK 465 SER A -9
REMARK 465 ASP A -8
REMARK 465 LYS A -7
REMARK 465 ILE A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 MET B -11
REMARK 465 GLY B -10
REMARK 465 SER B -9
REMARK 465 ASP B -8
REMARK 465 LYS B -7
REMARK 465 ILE B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
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 MET A 1 N
REMARK 470 LYS A 24 CE NZ
REMARK 470 LYS A 84 CE NZ
REMARK 470 GLU A 144 CD OE1 OE2
REMARK 470 ARG A 173 CD NE CZ NH1 NH2
REMARK 470 ARG A 185 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 186 CG CD1 CD2
REMARK 470 HIS A 187 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 190 CD CE NZ
REMARK 470 ASN A 191 CG OD1 ND2
REMARK 470 GLU A 194 CD OE1 OE2
REMARK 470 LYS A 198 CD CE NZ
REMARK 470 LYS A 206 CD CE NZ
REMARK 470 GLU A 274 CG CD OE1 OE2
REMARK 470 LYS A 275 CG CD CE NZ
REMARK 470 LEU B 3 CD1
REMARK 470 LYS B 29 CE NZ
REMARK 470 LYS B 30 CG CD CE NZ
REMARK 470 LYS B 84 CD CE NZ
REMARK 470 LYS B 111 CD CE NZ
REMARK 470 LYS B 114 CE NZ
REMARK 470 LYS B 121 CD CE NZ
REMARK 470 GLN B 138 CD OE1 NE2
REMARK 470 ARG B 173 CD NE CZ NH1 NH2
REMARK 470 LYS B 175 CE NZ
REMARK 470 LEU B 186 CG CD1 CD2
REMARK 470 HIS B 187 CG ND1 CD2 CE1 NE2
REMARK 470 GLU B 274 CG CD OE1 OE2
REMARK 470 LYS B 275 CG CD CE NZ
REMARK 470 GLU B 277 CB CG CD OE1 OE2
REMARK 470 GLU B 294 CG CD OE1 OE2
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 158 CB - CG - OD1 ANGL. DEV. = 7.2 DEGREES
REMARK 500 ASP B 32 CB - CG - OD1 ANGL. DEV. = 5.6 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 PHE A 18 -55.37 -134.00
REMARK 500 ASN A 80 59.76 -96.12
REMARK 500 THR A 188 83.62 -150.69
REMARK 500 PHE B 18 -51.47 -126.15
REMARK 500 THR B 188 74.86 -152.94
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 MG A 295 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 316 O
REMARK 620 2 HOH A 349 O 101.3
REMARK 620 3 HOH A 381 O 131.1 76.5
REMARK 620 4 HOH A 418 O 66.8 168.0 109.5
REMARK 620 5 HOH A 435 O 137.8 81.3 90.8 108.5
REMARK 620 6 HOH A 484 O 67.2 90.3 158.8 86.7 70.7
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 MG A 295
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT B 295
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 282443 RELATED DB: TARGETDB
DBREF 1VMA A 1 294 UNP Q9WZ40 Q9WZ40_THEMA 1 294
DBREF 1VMA B 1 294 UNP Q9WZ40 Q9WZ40_THEMA 1 294
SEQADV 1VMA MET A -11 UNP Q9WZ40 EXPRESSION TAG
SEQADV 1VMA GLY A -10 UNP Q9WZ40 EXPRESSION TAG
SEQADV 1VMA SER A -9 UNP Q9WZ40 EXPRESSION TAG
SEQADV 1VMA ASP A -8 UNP Q9WZ40 EXPRESSION TAG
SEQADV 1VMA LYS A -7 UNP Q9WZ40 EXPRESSION TAG
SEQADV 1VMA ILE A -6 UNP Q9WZ40 EXPRESSION TAG
SEQADV 1VMA HIS A -5 UNP Q9WZ40 EXPRESSION TAG
SEQADV 1VMA HIS A -4 UNP Q9WZ40 EXPRESSION TAG
SEQADV 1VMA HIS A -3 UNP Q9WZ40 EXPRESSION TAG
SEQADV 1VMA HIS A -2 UNP Q9WZ40 EXPRESSION TAG
SEQADV 1VMA HIS A -1 UNP Q9WZ40 EXPRESSION TAG
SEQADV 1VMA HIS A 0 UNP Q9WZ40 EXPRESSION TAG
SEQADV 1VMA MET B -11 UNP Q9WZ40 EXPRESSION TAG
SEQADV 1VMA GLY B -10 UNP Q9WZ40 EXPRESSION TAG
SEQADV 1VMA SER B -9 UNP Q9WZ40 EXPRESSION TAG
SEQADV 1VMA ASP B -8 UNP Q9WZ40 EXPRESSION TAG
SEQADV 1VMA LYS B -7 UNP Q9WZ40 EXPRESSION TAG
SEQADV 1VMA ILE B -6 UNP Q9WZ40 EXPRESSION TAG
SEQADV 1VMA HIS B -5 UNP Q9WZ40 EXPRESSION TAG
SEQADV 1VMA HIS B -4 UNP Q9WZ40 EXPRESSION TAG
SEQADV 1VMA HIS B -3 UNP Q9WZ40 EXPRESSION TAG
SEQADV 1VMA HIS B -2 UNP Q9WZ40 EXPRESSION TAG
SEQADV 1VMA HIS B -1 UNP Q9WZ40 EXPRESSION TAG
SEQADV 1VMA HIS B 0 UNP Q9WZ40 EXPRESSION TAG
SEQRES 1 A 306 MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MET
SEQRES 2 A 306 GLY LEU PHE ASP PHE LEU LYS LYS GLY LEU GLN LYS THR
SEQRES 3 A 306 LYS GLU THR PHE PHE GLY ARG VAL VAL LYS LEU LEU LYS
SEQRES 4 A 306 GLY LYS LYS LEU ASP ASP GLU THR ARG GLU GLU LEU GLU
SEQRES 5 A 306 GLU LEU LEU ILE GLN ALA ASP VAL GLY VAL GLU THR THR
SEQRES 6 A 306 GLU TYR ILE LEU GLU ARG LEU GLU GLU LYS ASP GLY ASP
SEQRES 7 A 306 ALA LEU GLU SER LEU LYS GLU ILE ILE LEU GLU ILE LEU
SEQRES 8 A 306 ASN PHE ASP THR LYS LEU ASN VAL PRO PRO GLU PRO PRO
SEQRES 9 A 306 PHE VAL ILE MET VAL VAL GLY VAL ASN GLY THR GLY LYS
SEQRES 10 A 306 THR THR SER CYS GLY LYS LEU ALA LYS MET PHE VAL ASP
SEQRES 11 A 306 GLU GLY LYS SER VAL VAL LEU ALA ALA ALA ASP THR PHE
SEQRES 12 A 306 ARG ALA ALA ALA ILE GLU GLN LEU LYS ILE TRP GLY GLU
SEQRES 13 A 306 ARG VAL GLY ALA THR VAL ILE SER HIS SER GLU GLY ALA
SEQRES 14 A 306 ASP PRO ALA ALA VAL ALA PHE ASP ALA VAL ALA HIS ALA
SEQRES 15 A 306 LEU ALA ARG ASN LYS ASP VAL VAL ILE ILE ASP THR ALA
SEQRES 16 A 306 GLY ARG LEU HIS THR LYS LYS ASN LEU MET GLU GLU LEU
SEQRES 17 A 306 ARG LYS VAL HIS ARG VAL VAL LYS LYS LYS ILE PRO ASP
SEQRES 18 A 306 ALA PRO HIS GLU THR LEU LEU VAL ILE ASP ALA THR THR
SEQRES 19 A 306 GLY GLN ASN GLY LEU VAL GLN ALA LYS ILE PHE LYS GLU
SEQRES 20 A 306 ALA VAL ASN VAL THR GLY ILE ILE LEU THR LYS LEU ASP
SEQRES 21 A 306 GLY THR ALA LYS GLY GLY ILE THR LEU ALA ILE ALA ARG
SEQRES 22 A 306 GLU LEU GLY ILE PRO ILE LYS PHE ILE GLY VAL GLY GLU
SEQRES 23 A 306 LYS ALA GLU ASP LEU ARG PRO PHE ASP PRO GLU ALA PHE
SEQRES 24 A 306 VAL GLU VAL LEU LEU SER GLU
SEQRES 1 B 306 MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MET
SEQRES 2 B 306 GLY LEU PHE ASP PHE LEU LYS LYS GLY LEU GLN LYS THR
SEQRES 3 B 306 LYS GLU THR PHE PHE GLY ARG VAL VAL LYS LEU LEU LYS
SEQRES 4 B 306 GLY LYS LYS LEU ASP ASP GLU THR ARG GLU GLU LEU GLU
SEQRES 5 B 306 GLU LEU LEU ILE GLN ALA ASP VAL GLY VAL GLU THR THR
SEQRES 6 B 306 GLU TYR ILE LEU GLU ARG LEU GLU GLU LYS ASP GLY ASP
SEQRES 7 B 306 ALA LEU GLU SER LEU LYS GLU ILE ILE LEU GLU ILE LEU
SEQRES 8 B 306 ASN PHE ASP THR LYS LEU ASN VAL PRO PRO GLU PRO PRO
SEQRES 9 B 306 PHE VAL ILE MET VAL VAL GLY VAL ASN GLY THR GLY LYS
SEQRES 10 B 306 THR THR SER CYS GLY LYS LEU ALA LYS MET PHE VAL ASP
SEQRES 11 B 306 GLU GLY LYS SER VAL VAL LEU ALA ALA ALA ASP THR PHE
SEQRES 12 B 306 ARG ALA ALA ALA ILE GLU GLN LEU LYS ILE TRP GLY GLU
SEQRES 13 B 306 ARG VAL GLY ALA THR VAL ILE SER HIS SER GLU GLY ALA
SEQRES 14 B 306 ASP PRO ALA ALA VAL ALA PHE ASP ALA VAL ALA HIS ALA
SEQRES 15 B 306 LEU ALA ARG ASN LYS ASP VAL VAL ILE ILE ASP THR ALA
SEQRES 16 B 306 GLY ARG LEU HIS THR LYS LYS ASN LEU MET GLU GLU LEU
SEQRES 17 B 306 ARG LYS VAL HIS ARG VAL VAL LYS LYS LYS ILE PRO ASP
SEQRES 18 B 306 ALA PRO HIS GLU THR LEU LEU VAL ILE ASP ALA THR THR
SEQRES 19 B 306 GLY GLN ASN GLY LEU VAL GLN ALA LYS ILE PHE LYS GLU
SEQRES 20 B 306 ALA VAL ASN VAL THR GLY ILE ILE LEU THR LYS LEU ASP
SEQRES 21 B 306 GLY THR ALA LYS GLY GLY ILE THR LEU ALA ILE ALA ARG
SEQRES 22 B 306 GLU LEU GLY ILE PRO ILE LYS PHE ILE GLY VAL GLY GLU
SEQRES 23 B 306 LYS ALA GLU ASP LEU ARG PRO PHE ASP PRO GLU ALA PHE
SEQRES 24 B 306 VAL GLU VAL LEU LEU SER GLU
HET MG A 295 1
HET CIT B 295 13
HETNAM MG MAGNESIUM ION
HETNAM CIT CITRIC ACID
FORMUL 3 MG MG 2+
FORMUL 4 CIT C6 H8 O7
FORMUL 5 HOH *394(H2 O)
HELIX 1 1 GLY A 2 PHE A 18 1 17
HELIX 2 2 PHE A 18 LYS A 27 1 10
HELIX 3 3 ASP A 32 ALA A 46 1 15
HELIX 4 4 GLY A 49 GLU A 61 1 13
HELIX 5 5 ASP A 66 LEU A 79 1 14
HELIX 6 6 GLY A 104 GLU A 119 1 16
HELIX 7 7 ARG A 132 GLY A 147 1 16
HELIX 8 8 ASP A 158 ARG A 173 1 16
HELIX 9 9 THR A 188 VAL A 203 1 16
HELIX 10 10 LYS A 204 LYS A 206 5 3
HELIX 11 11 THR A 222 VAL A 237 1 16
HELIX 12 12 LYS A 246 THR A 250 5 5
HELIX 13 13 GLY A 254 GLY A 264 1 11
HELIX 14 14 LYS A 275 GLU A 277 5 3
HELIX 15 15 ASP A 283 LEU A 292 1 10
HELIX 16 16 GLY B 2 PHE B 18 1 17
HELIX 17 17 PHE B 18 LYS B 27 1 10
HELIX 18 18 ASP B 32 ALA B 46 1 15
HELIX 19 19 GLY B 49 GLU B 62 1 14
HELIX 20 20 ASP B 66 ASN B 80 1 15
HELIX 21 21 GLY B 104 GLU B 119 1 16
HELIX 22 22 ARG B 132 GLY B 147 1 16
HELIX 23 23 ASP B 158 ARG B 173 1 16
HELIX 24 24 THR B 188 VAL B 203 1 16
HELIX 25 25 LYS B 204 LYS B 206 5 3
HELIX 26 26 THR B 222 VAL B 237 1 16
HELIX 27 27 LYS B 246 THR B 250 5 5
HELIX 28 28 GLY B 254 GLY B 264 1 11
HELIX 29 29 ASP B 283 LEU B 292 1 10
SHEET 1 A 8 THR A 149 ILE A 151 0
SHEET 2 A 8 VAL A 123 ALA A 128 1 N LEU A 125 O THR A 149
SHEET 3 A 8 VAL A 177 THR A 182 1 O ILE A 179 N ALA A 126
SHEET 4 A 8 PHE A 93 VAL A 98 1 N ILE A 95 O VAL A 178
SHEET 5 A 8 GLU A 213 ASP A 219 1 O VAL A 217 N VAL A 98
SHEET 6 A 8 GLY A 241 THR A 245 1 O ILE A 243 N ILE A 218
SHEET 7 A 8 ILE A 267 GLY A 271 1 O GLY A 271 N LEU A 244
SHEET 8 A 8 LEU A 279 PRO A 281 -1 O ARG A 280 N ILE A 270
SHEET 1 B 8 THR B 149 ILE B 151 0
SHEET 2 B 8 VAL B 123 ALA B 128 1 N LEU B 125 O THR B 149
SHEET 3 B 8 VAL B 177 THR B 182 1 O ILE B 179 N VAL B 124
SHEET 4 B 8 PHE B 93 GLY B 99 1 N ILE B 95 O VAL B 178
SHEET 5 B 8 GLU B 213 ASP B 219 1 O LEU B 215 N VAL B 98
SHEET 6 B 8 GLY B 241 THR B 245 1 O ILE B 243 N LEU B 216
SHEET 7 B 8 ILE B 267 GLY B 271 1 O GLY B 271 N LEU B 244
SHEET 8 B 8 LEU B 279 PRO B 281 -1 O ARG B 280 N ILE B 270
LINK MG MG A 295 O HOH A 316 1555 1555 3.05
LINK MG MG A 295 O HOH A 349 1555 1555 2.32
LINK MG MG A 295 O HOH A 381 1555 1555 2.35
LINK MG MG A 295 O HOH A 418 1555 1555 1.91
LINK MG MG A 295 O HOH A 435 1555 1555 2.64
LINK MG MG A 295 O HOH A 484 1555 1555 2.10
CISPEP 1 PRO A 91 PRO A 92 0 -0.22
CISPEP 2 ALA A 210 PRO A 211 0 -15.00
CISPEP 3 PRO B 91 PRO B 92 0 1.67
CISPEP 4 ALA B 210 PRO B 211 0 -11.33
SITE 1 AC1 9 GLY A 102 GLY A 104 LYS A 105 HOH A 316
SITE 2 AC1 9 HOH A 349 HOH A 381 HOH A 418 HOH A 435
SITE 3 AC1 9 HOH A 484
SITE 1 AC2 10 VAL B 100 ASN B 101 GLY B 102 THR B 103
SITE 2 AC2 10 GLY B 104 LYS B 105 THR B 106 THR B 107
SITE 3 AC2 10 ARG B 132 HOH B 325
CRYST1 78.446 48.102 90.792 90.00 107.94 90.00 P 1 21 1 4
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 0.012748 0.000000 0.004127 0.00000
SCALE2 0.000000 0.020789 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011577 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
