HEADER TRANSFERASE 12-NOV-03 1V4A
TITLE STRUCTURE OF THE N-TERMINAL DOMAIN OF ESCHERICHIA COLI GLUTAMINE
TITLE 2 SYNTHETASE ADENYLYLTRANSFERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAMATE-AMMONIA-LIGASE ADENYLYLTRANSFERASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN;
COMPND 5 SYNONYM: GLUTAMINE-SYNTHETASE ADENYLYLTRANSFERASE, ATASE,
COMPND 6 ADENYLYLTRANSFERASE;
COMPND 7 EC: 2.7.7.42;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PDW1
KEYWDS MAIN ALPHA HELIX, DNA POLYMERASE BETA MOTIF, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.XU,R.ZHANG,A.JOACHIMIAK,P.D.CARR,D.L.OLLIS,S.G.VASUDEVAN
REVDAT 3 27-DEC-23 1V4A 1 SEQADV LINK
REVDAT 2 24-FEB-09 1V4A 1 VERSN
REVDAT 1 27-JUL-04 1V4A 0
JRNL AUTH Y.XU,R.ZHANG,A.JOACHIMIAK,P.D.CARR,T.HUBER,S.G.VASUDEVAN,
JRNL AUTH 2 D.L.OLLIS
JRNL TITL STRUCTURE OF THE N-TERMINAL DOMAIN OF ESCHERICHIA COLI
JRNL TITL 2 GLUTAMINE SYNTHETASE ADENYLYLTRANSFERASE
JRNL REF STRUCTURE V. 12 861 2004
JRNL REFN ISSN 0969-2126
JRNL PMID 15130478
JRNL DOI 10.1016/J.STR.2004.02.029
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 34466
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) : 0.230
REMARK 3 R VALUE (WORKING SET) : 0.228
REMARK 3 FREE R VALUE : 0.269
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1815
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2561
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2920
REMARK 3 BIN FREE R VALUE SET COUNT : 138
REMARK 3 BIN FREE R VALUE : 0.3570
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3370
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 171
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.53000
REMARK 3 B22 (A**2) : 0.53000
REMARK 3 B33 (A**2) : -0.79000
REMARK 3 B12 (A**2) : 0.26000
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): 0.194
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.175
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.133
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.755
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.935
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.906
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3442 ; 0.011 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 3208 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4673 ; 1.076 ; 1.950
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7384 ; 0.780 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 427 ; 5.348 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 518 ; 0.059 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3873 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 742 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 810 ; 0.198 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 3719 ; 0.218 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 2048 ; 0.083 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 145 ; 0.155 ; 0.200
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): 11 ; 0.054 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 57 ; 0.224 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 4 ; 0.173 ; 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): 2137 ; 1.941 ; 5.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3402 ; 2.887 ; 6.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1305 ; 2.573 ; 6.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1271 ; 3.726 ; 7.500
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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 1V4A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-NOV-03.
REMARK 100 THE DEPOSITION ID IS D_1000006187.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-FEB-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95372, 0.97844, 0.97855
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36424
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 35.00
REMARK 200 R MERGE (I) : 0.08300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.51700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.98
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 2000 MME, SODIUM FORMATE, SODIUM
REMARK 280 ACETATE, PH 4.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.16267
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 22.58133
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 22.58133
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 45.16267
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: 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 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 HIS A 183
REMARK 465 GLY A 184
REMARK 465 CYS A 185
REMARK 465 THR A 186
REMARK 465 GLN A 187
REMARK 465 GLY A 188
REMARK 465 GLY A 189
REMARK 465 ARG A 190
REMARK 465 ASP A 438
REMARK 465 ASP A 439
REMARK 465 GLU A 440
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 LYS A 2 CG CD CE NZ
REMARK 470 GLU A 17 CG CD OE1 OE2
REMARK 470 ARG A 18 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 25 CG CD OE1 OE2
REMARK 470 LEU A 53 CG CD1 CD2
REMARK 470 SER A 58 OG
REMARK 470 GLN A 59 CG CD OE1 NE2
REMARK 470 GLU A 75 CG CD OE1 OE2
REMARK 470 CYS A 78 CB SG
REMARK 470 ASN A 79 CG OD1 ND2
REMARK 470 THR A 144 OG1 CG2
REMARK 470 GLU A 151 CG CD OE1 OE2
REMARK 470 GLN A 153 CG CD OE1 NE2
REMARK 470 LEU A 193 CG CD1 CD2
REMARK 470 GLN A 204 CG CD OE1 NE2
REMARK 470 GLN A 247 CG CD OE1 NE2
REMARK 470 GLU A 268 CG CD OE1 OE2
REMARK 470 VAL A 270 CG1 CG2
REMARK 470 ARG A 308 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 310 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 312 CG CD1 CD2
REMARK 470 GLU A 390 CG CD OE1 OE2
REMARK 470 SER A 397 OG
REMARK 470 GLU A 399 CG CD OE1 OE2
REMARK 470 ASP A 410 CG OD1 OD2
REMARK 470 ARG A 429 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 446 O HOH A 599 2.03
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 MSE A 258 SE MSE A 258 CE -0.387
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 PRO A 3 146.35 -31.31
REMARK 500 ARG A 18 -28.08 165.75
REMARK 500 GLN A 59 93.42 -161.05
REMARK 500 ASN A 79 42.78 -97.01
REMARK 500 GLU A 141 -80.33 -91.80
REMARK 500 THR A 144 -174.72 50.28
REMARK 500 PRO A 181 -72.58 -71.94
REMARK 500 LEU A 193 6.65 80.52
REMARK 500 ASP A 194 118.34 77.71
REMARK 500 THR A 214 -166.40 -117.21
REMARK 500 VAL A 219 -66.72 -90.19
REMARK 500 ILE A 436 54.79 31.59
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1V4A A 1 440 UNP P30870 GLNE_ECOLI 1 440
SEQADV 1V4A MSE A 1 UNP P30870 MET 1 MODIFIED RESIDUE
SEQADV 1V4A MSE A 87 UNP P30870 MET 87 MODIFIED RESIDUE
SEQADV 1V4A MSE A 98 UNP P30870 MET 98 MODIFIED RESIDUE
SEQADV 1V4A MSE A 160 UNP P30870 MET 160 MODIFIED RESIDUE
SEQADV 1V4A MSE A 202 UNP P30870 MET 202 MODIFIED RESIDUE
SEQADV 1V4A MSE A 224 UNP P30870 MET 224 MODIFIED RESIDUE
SEQADV 1V4A MSE A 258 UNP P30870 MET 258 MODIFIED RESIDUE
SEQADV 1V4A MSE A 264 UNP P30870 MET 264 MODIFIED RESIDUE
SEQADV 1V4A MSE A 278 UNP P30870 MET 278 MODIFIED RESIDUE
SEQADV 1V4A MSE A 299 UNP P30870 MET 299 MODIFIED RESIDUE
SEQADV 1V4A MSE A 302 UNP P30870 MET 302 MODIFIED RESIDUE
SEQADV 1V4A MSE A 409 UNP P30870 MET 409 MODIFIED RESIDUE
SEQADV 1V4A MSE A 425 UNP P30870 MET 425 MODIFIED RESIDUE
SEQRES 1 A 440 MSE LYS PRO LEU SER SER PRO LEU GLN GLN TYR TRP GLN
SEQRES 2 A 440 THR VAL VAL GLU ARG LEU PRO GLU PRO LEU ALA GLU GLU
SEQRES 3 A 440 SER LEU SER ALA GLN ALA LYS SER VAL LEU THR PHE SER
SEQRES 4 A 440 ASP PHE VAL GLN ASP SER VAL ILE ALA HIS PRO GLU TRP
SEQRES 5 A 440 LEU THR GLU LEU GLU SER GLN PRO PRO GLN ALA ASP GLU
SEQRES 6 A 440 TRP GLN HIS TYR ALA ALA TRP LEU GLN GLU ALA LEU CYS
SEQRES 7 A 440 ASN VAL SER ASP GLU ALA GLY LEU MSE ARG GLU LEU ARG
SEQRES 8 A 440 LEU PHE ARG ARG ARG ILE MSE VAL ARG ILE ALA TRP ALA
SEQRES 9 A 440 GLN THR LEU ALA LEU VAL THR GLU GLU SER ILE LEU GLN
SEQRES 10 A 440 GLN LEU SER TYR LEU ALA GLU THR LEU ILE VAL ALA ALA
SEQRES 11 A 440 ARG ASP TRP LEU TYR ASP ALA CYS CYS ARG GLU TRP GLY
SEQRES 12 A 440 THR PRO CYS ASN ALA GLN GLY GLU ALA GLN PRO LEU LEU
SEQRES 13 A 440 ILE LEU GLY MSE GLY LYS LEU GLY GLY GLY GLU LEU ASN
SEQRES 14 A 440 PHE SER SER ASP ILE ASP LEU ILE PHE ALA TRP PRO GLU
SEQRES 15 A 440 HIS GLY CYS THR GLN GLY GLY ARG ARG GLU LEU ASP ASN
SEQRES 16 A 440 ALA GLN PHE PHE THR ARG MSE GLY GLN ARG LEU ILE LYS
SEQRES 17 A 440 VAL LEU ASP GLN PRO THR GLN ASP GLY PHE VAL TYR ARG
SEQRES 18 A 440 VAL ASP MSE ARG LEU ARG PRO PHE GLY GLU SER GLY PRO
SEQRES 19 A 440 LEU VAL LEU SER PHE ALA ALA LEU GLU ASP TYR TYR GLN
SEQRES 20 A 440 GLU GLN GLY ARG ASP TRP GLU ARG TYR ALA MSE VAL LYS
SEQRES 21 A 440 ALA ARG ILE MSE GLY ASP SER GLU GLY VAL TYR ALA ASN
SEQRES 22 A 440 GLU LEU ARG ALA MSE LEU ARG PRO PHE VAL PHE ARG ARG
SEQRES 23 A 440 TYR ILE ASP PHE SER VAL ILE GLN SER LEU ARG ASN MSE
SEQRES 24 A 440 LYS GLY MSE ILE ALA ARG GLU VAL ARG ARG ARG GLY LEU
SEQRES 25 A 440 THR ASP ASN ILE LYS LEU GLY ALA GLY GLY ILE ARG GLU
SEQRES 26 A 440 ILE GLU PHE ILE VAL GLN VAL PHE GLN LEU ILE ARG GLY
SEQRES 27 A 440 GLY ARG GLU PRO SER LEU GLN SER ARG SER LEU LEU PRO
SEQRES 28 A 440 THR LEU SER ALA ILE ALA GLU LEU HIS LEU LEU SER GLU
SEQRES 29 A 440 ASN ASP ALA GLU GLN LEU ARG VAL ALA TYR LEU PHE LEU
SEQRES 30 A 440 ARG ARG LEU GLU ASN LEU LEU GLN SER ILE ASN ASP GLU
SEQRES 31 A 440 GLN THR GLN THR LEU PRO SER ASP GLU LEU ASN ARG ALA
SEQRES 32 A 440 ARG LEU ALA TRP ALA MSE ASP PHE ALA ASP TRP PRO GLN
SEQRES 33 A 440 LEU THR GLY ALA LEU THR ALA HIS MSE THR ASN VAL ARG
SEQRES 34 A 440 ARG VAL PHE ASN GLU LEU ILE GLY ASP ASP GLU
MODRES 1V4A MSE A 1 MET SELENOMETHIONINE
MODRES 1V4A MSE A 87 MET SELENOMETHIONINE
MODRES 1V4A MSE A 98 MET SELENOMETHIONINE
MODRES 1V4A MSE A 160 MET SELENOMETHIONINE
MODRES 1V4A MSE A 202 MET SELENOMETHIONINE
MODRES 1V4A MSE A 224 MET SELENOMETHIONINE
MODRES 1V4A MSE A 258 MET SELENOMETHIONINE
MODRES 1V4A MSE A 264 MET SELENOMETHIONINE
MODRES 1V4A MSE A 278 MET SELENOMETHIONINE
MODRES 1V4A MSE A 299 MET SELENOMETHIONINE
MODRES 1V4A MSE A 302 MET SELENOMETHIONINE
MODRES 1V4A MSE A 409 MET SELENOMETHIONINE
MODRES 1V4A MSE A 425 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 87 8
HET MSE A 98 8
HET MSE A 160 8
HET MSE A 202 8
HET MSE A 224 8
HET MSE A 258 8
HET MSE A 264 8
HET MSE A 278 8
HET MSE A 299 8
HET MSE A 302 8
HET MSE A 409 8
HET MSE A 425 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 13(C5 H11 N O2 SE)
FORMUL 2 HOH *171(H2 O)
HELIX 1 1 SER A 5 GLU A 17 1 13
HELIX 2 2 ALA A 24 LEU A 28 5 5
HELIX 3 3 SER A 29 SER A 39 1 11
HELIX 4 4 SER A 39 HIS A 49 1 11
HELIX 5 5 PRO A 50 GLN A 59 1 10
HELIX 6 6 GLN A 62 GLN A 67 5 6
HELIX 7 7 HIS A 68 LEU A 77 1 10
HELIX 8 8 ASP A 82 LEU A 107 1 26
HELIX 9 9 THR A 111 TRP A 142 1 32
HELIX 10 10 MSE A 160 GLY A 165 1 6
HELIX 11 11 ASP A 194 GLN A 212 1 19
HELIX 12 12 PHE A 229 GLY A 233 5 5
HELIX 13 13 PHE A 239 GLY A 250 1 12
HELIX 14 14 ARG A 251 VAL A 259 1 9
HELIX 15 15 GLY A 269 PHE A 284 1 16
HELIX 16 16 ASP A 289 GLY A 311 1 23
HELIX 17 17 GLY A 322 GLY A 338 1 17
HELIX 18 18 GLU A 341 GLN A 345 5 5
HELIX 19 19 SER A 348 LEU A 359 1 12
HELIX 20 20 SER A 363 SER A 386 1 24
HELIX 21 21 ASP A 398 MSE A 409 1 12
HELIX 22 22 ASP A 413 LEU A 435 1 23
SHEET 1 A 2 ASN A 147 ALA A 148 0
SHEET 2 A 2 GLU A 151 ALA A 152 -1 O GLU A 151 N ALA A 148
SHEET 1 B 3 VAL A 222 ASP A 223 0
SHEET 2 B 3 ILE A 174 TRP A 180 1 N ILE A 174 O ASP A 223
SHEET 3 B 3 VAL A 236 SER A 238 1 O LEU A 237 N TRP A 180
SHEET 1 C 4 VAL A 222 ASP A 223 0
SHEET 2 C 4 ILE A 174 TRP A 180 1 N ILE A 174 O ASP A 223
SHEET 3 C 4 LEU A 156 GLY A 159 -1 N LEU A 156 O ALA A 179
SHEET 4 C 4 ARG A 262 ILE A 263 -1 O ARG A 262 N GLY A 159
LINK C MSE A 1 N LYS A 2 1555 1555 1.33
LINK C LEU A 86 N MSE A 87 1555 1555 1.33
LINK C MSE A 87 N ARG A 88 1555 1555 1.33
LINK C ILE A 97 N MSE A 98 1555 1555 1.33
LINK C MSE A 98 N VAL A 99 1555 1555 1.33
LINK C GLY A 159 N MSE A 160 1555 1555 1.33
LINK C MSE A 160 N GLY A 161 1555 1555 1.33
LINK C ARG A 201 N MSE A 202 1555 1555 1.33
LINK C MSE A 202 N GLY A 203 1555 1555 1.33
LINK C ASP A 223 N MSE A 224 1555 1555 1.33
LINK C MSE A 224 N ARG A 225 1555 1555 1.33
LINK C ALA A 257 N MSE A 258 1555 1555 1.33
LINK C MSE A 258 N VAL A 259 1555 1555 1.33
LINK C ILE A 263 N MSE A 264 1555 1555 1.33
LINK C MSE A 264 N GLY A 265 1555 1555 1.33
LINK C ALA A 277 N MSE A 278 1555 1555 1.33
LINK C MSE A 278 N LEU A 279 1555 1555 1.33
LINK C ASN A 298 N MSE A 299 1555 1555 1.33
LINK C MSE A 299 N LYS A 300 1555 1555 1.33
LINK C GLY A 301 N MSE A 302 1555 1555 1.33
LINK C MSE A 302 N ILE A 303 1555 1555 1.33
LINK C ALA A 408 N MSE A 409 1555 1555 1.33
LINK C MSE A 409 N ASP A 410 1555 1555 1.34
LINK C HIS A 424 N MSE A 425 1555 1555 1.33
LINK C MSE A 425 N THR A 426 1555 1555 1.33
CISPEP 1 GLU A 21 PRO A 22 0 -2.03
CRYST1 116.836 116.836 67.744 90.00 90.00 120.00 P 32 2 1 6
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 0.008559 0.004942 0.000000 0.00000
SCALE2 0.000000 0.009883 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014761 0.00000
HETATM 1 N MSE A 1 102.224 67.255 -4.414 1.00 66.99 N
HETATM 2 CA MSE A 1 102.817 67.483 -3.067 1.00 65.32 C
HETATM 3 C MSE A 1 103.037 68.974 -2.810 1.00 64.25 C
HETATM 4 O MSE A 1 104.033 69.547 -3.249 1.00 64.75 O
HETATM 5 CB MSE A 1 104.142 66.731 -2.948 1.00 66.73 C
HETATM 6 CG MSE A 1 104.843 66.905 -1.602 1.00 67.17 C
HETATM 7 SE MSE A 1 105.998 65.566 -1.242 1.00 67.17 SE
HETATM 8 CE MSE A 1 106.942 65.485 -2.794 1.00 66.29 C
(ATOM LINES ARE NOT SHOWN.)
END
