HEADER LIGASE 12-JAN-97 1NHT
TITLE ENTRAPMENT OF 6-THIOPHOSPHORYL-IMP IN THE ACTIVE SITE OF CRYSTALLINE
TITLE 2 ADENYLOSUCCINATE SYNTHETASE FROM ESCHERICHIA COLI DATA COLLECTED AT
TITLE 3 100K
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADENYLOSUCCINATE SYNTHETASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 6.3.4.4
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 STRAIN: PUR A STRAIN H1238;
SOURCE 5 ATCC: COLI GENETIC STOCK CENTER, STRAIN NUMBER 5408;
SOURCE 6 OTHER_DETAILS: A GIFT FROM DR. B. BACHMAN, GENETIC CENTER, YALE
SOURCE 7 UNIVERSITY
KEYWDS LIGASE, SYNTHETASE, PURINE NUCLEOTIDE BIOSYNTHESIS, GTP-HYDROLYSING
KEYWDS 2 ENZYMES
EXPDTA X-RAY DIFFRACTION
AUTHOR B.W.POLAND,C.A.BRUNS,H.J.FROMM,R.B.HONZATKO
REVDAT 4 14-FEB-24 1NHT 1 REMARK LINK
REVDAT 3 27-OCT-10 1NHT 1 FORMUL HET HETATM HETNAM
REVDAT 2 24-FEB-09 1NHT 1 VERSN
REVDAT 1 08-OCT-97 1NHT 0
JRNL AUTH B.W.POLAND,C.BRUNS,H.J.FROMM,R.B.HONZATKO
JRNL TITL ENTRAPMENT OF 6-THIOPHOSPHORYL-IMP IN THE ACTIVE SITE OF
JRNL TITL 2 CRYSTALLINE ADENYLOSUCCINATE SYNTHETASE FROM ESCHERICHIA
JRNL TITL 3 COLI.
JRNL REF J.BIOL.CHEM. V. 272 15200 1997
JRNL REFN ISSN 0021-9258
JRNL PMID 9182542
JRNL DOI 10.1074/JBC.272.24.15200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.M.SILVA,B.W.POLAND,C.R.HOFFMAN,H.J.FROMM,R.B.HONZATKO
REMARK 1 TITL REFINED CRYSTAL STRUCTURES OF UNLIGATED ADENYLOSUCCINATE
REMARK 1 TITL 2 SYNTHETASE FROM ESCHERICHIA COLI
REMARK 1 REF J.MOL.BIOL. V. 254 431 1995
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 2
REMARK 1 AUTH B.W.POLAND,M.M.SILVA,M.A.SERRA,Y.CHO,K.H.KIM,E.M.HARRIS,
REMARK 1 AUTH 2 R.B.HONZATKO
REMARK 1 TITL CRYSTAL STRUCTURE OF ADENYLOSUCCINATE SYNTHETASE FROM
REMARK 1 TITL 2 ESCHERICHIA COLI. EVIDENCE FOR CONVERGENT EVOLUTION OF
REMARK 1 TITL 3 GTP-BINDING DOMAINS
REMARK 1 REF J.BIOL.CHEM. V. 268 25334 1993
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 5.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 19932
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.206
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3321
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 64
REMARK 3 SOLVENT ATOMS : 454
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.30
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.013
REMARK 3 BOND ANGLES (DEGREES) : 1.890
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.630
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THERE ARE TWO REGIONS THAT ARE DISORDERED AT POSITIONS
REMARK 3 121 - 130, 298 - 303 AND ONE RESIDUE 416 THAT DIVERGE FROM
REMARK 3 THE DNA SEQUENCE GIVEN IN PIR:A61592. RESIDUE 416 IS
REMARK 3 GLYCINE IN THE ENTRY.
REMARK 4
REMARK 4 1NHT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000175295.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-MAY-96
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : SIEMENS-NICOLET X100
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XENGEN
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22201
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 4.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : 0.07900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 105.43333
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 52.71667
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 52.71667
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 105.43333
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 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 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 -0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 105.43333
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 VAL A 385 HG1 THR A 415 1.34
REMARK 500 OD2 ASP A 351 HH12 ARG A 353 1.39
REMARK 500 HH12 ARG A 32 O HIS A 53 1.42
REMARK 500 O ASP A 195 HG SER A 199 1.42
REMARK 500 O GLY A 225 HG1 THR A 243 1.43
REMARK 500 H2 GLY A 1 O ALA A 431 1.43
REMARK 500 O GLY A 384 HZ1 LYS A 386 1.44
REMARK 500 O ARG A 388 H LEU A 391 1.45
REMARK 500 HH TYR A 261 OD2 ASP A 411 1.46
REMARK 500 O LEU A 172 H ALA A 178 1.47
REMARK 500 HZ3 LYS A 18 OG1 THR A 422 1.51
REMARK 500 H VAL A 341 O MET A 375 1.51
REMARK 500 O ILE A 402 HG1 THR A 406 1.52
REMARK 500 H2 HOH A 545 O HOH A 641 1.52
REMARK 500 HH21 ARG A 426 O ASP A 430 1.53
REMARK 500 H1 HOH A 717 O HOH A 811 1.53
REMARK 500 HH TYR A 269 OE2 GLU A 296 1.53
REMARK 500 HG1 THR A 239 O3A PGS A 440 1.53
REMARK 500 O HOH A 596 H1 HOH A 747 1.54
REMARK 500 H TYR A 347 O VAL A 355 1.54
REMARK 500 O GLU A 403 H GLY A 407 1.54
REMARK 500 O ILE A 45 H GLU A 48 1.55
REMARK 500 O GLU A 14 HG1 THR A 330 1.55
REMARK 500 O HOH A 755 H2 HOH A 772 1.56
REMARK 500 HZ3 LYS A 16 O2P PGS A 440 1.56
REMARK 500 O HOH A 651 H1 HOH A 891 1.57
REMARK 500 O HOH A 594 H1 HOH A 630 1.57
REMARK 500 O VAL A 5 H LEU A 263 1.58
REMARK 500 O HOH A 626 H1 HOH A 774 1.58
REMARK 500 O GLY A 233 H TYR A 235 1.58
REMARK 500 OD2 ASP A 336 H THR A 382 1.59
REMARK 500 O HOH A 515 H1 HOH A 666 1.59
REMARK 500 H2 HOH A 525 O HOH A 948 1.59
REMARK 500 O HOH A 566 H2 HOH A 605 1.59
REMARK 500 H1 HOH A 530 O HOH A 786 1.59
REMARK 500 H1 HOH A 506 O HOH A 813 1.59
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 HH21 ARG A 257 O SER A 323 6555 1.50
REMARK 500 H2 HOH A 549 O HOH A 829 6555 1.53
REMARK 500 O HOH A 608 H2 HOH A 888 6555 1.54
REMARK 500 O HOH A 704 H2 HOH A 943 2664 1.58
REMARK 500
REMARK 500 REMARK: NULL
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 LEU A 7 CA - CB - CG ANGL. DEV. = 16.8 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 GLN A 10 -121.60 -111.62
REMARK 500 HIS A 53 -70.71 -118.92
REMARK 500 SER A 57 11.27 -69.01
REMARK 500 ARG A 121 -7.85 -53.63
REMARK 500 ARG A 131 -167.66 -65.20
REMARK 500 PHE A 152 -103.13 -61.90
REMARK 500 ASP A 153 98.45 -49.54
REMARK 500 TYR A 175 -73.51 -81.16
REMARK 500 GLN A 224 -156.89 44.33
REMARK 500 LEU A 227 3.05 -65.29
REMARK 500 THR A 234 60.44 -69.27
REMARK 500 SER A 240 23.34 -78.19
REMARK 500 ALA A 245 -8.14 -46.63
REMARK 500 VAL A 248 -72.23 -61.52
REMARK 500 SER A 252 -42.22 -132.67
REMARK 500 LYS A 267 10.80 -69.46
REMARK 500 ALA A 268 -21.31 70.84
REMARK 500 PHE A 278 70.93 -158.33
REMARK 500 ASN A 295 61.31 37.53
REMARK 500 THR A 300 -40.96 -134.39
REMARK 500 LEU A 324 158.59 -43.58
REMARK 500 ALA A 361 122.99 144.15
REMARK 500 ALA A 362 -66.31 -24.59
REMARK 500 ASP A 364 11.86 -64.95
REMARK 500 LYS A 366 -25.49 -38.79
REMARK 500 TYR A 372 -160.54 -67.73
REMARK 500 GLU A 373 79.22 -173.28
REMARK 500 TRP A 378 124.29 -171.41
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 PHE A 327 0.07 SIDE CHAIN
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 435 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 13 OD1
REMARK 620 2 GLY A 40 O 150.6
REMARK 620 3 GDP A 432 O1B 99.5 98.6
REMARK 620 4 GDP A 432 O2A 99.9 99.0 101.1
REMARK 620 5 HDA A 437 O 77.1 77.7 159.4 99.5
REMARK 620 6 PGS A 440 O3P 71.1 89.6 80.2 171.0 79.6
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: GNS
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: THESE RESIDUES MAKE UP THE GUANINE NUCLEOTIDE
REMARK 800 BINDING SITE ON ADENYLOSUCCINATE SYNTHETASE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: IMP
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: THESE RESIDUES MAKE UP THE GUANINE NUCLEOTIDE
REMARK 800 BINDING SITE ON ADENYLOSUCCINATE SYNTHETASE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: ASP
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: THESE RESIDUES MAKE UP THE GUANINE NUCLEOTIDE
REMARK 800 BINDING SITE ON ADENYLOSUCCINATE SYNTHETASE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 435
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 432
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HDA A 437
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGS A 440
DBREF 1NHT A 1 431 UNP P0A7D4 PURA_ECOLI 1 431
SEQRES 1 A 431 GLY ASN ASN VAL VAL VAL LEU GLY THR GLN TRP GLY ASP
SEQRES 2 A 431 GLU GLY LYS GLY LYS ILE VAL ASP LEU LEU THR GLU ARG
SEQRES 3 A 431 ALA LYS TYR VAL VAL ARG TYR GLN GLY GLY HIS ASN ALA
SEQRES 4 A 431 GLY HIS THR LEU VAL ILE ASN GLY GLU LYS THR VAL LEU
SEQRES 5 A 431 HIS LEU ILE PRO SER GLY ILE LEU ARG GLU ASN VAL THR
SEQRES 6 A 431 SER ILE ILE GLY ASN GLY VAL VAL LEU SER PRO ALA ALA
SEQRES 7 A 431 LEU MET LYS GLU MET LYS GLU LEU GLU ASP ARG GLY ILE
SEQRES 8 A 431 PRO VAL ARG GLU ARG LEU LEU LEU SER GLU ALA CYS PRO
SEQRES 9 A 431 LEU ILE LEU ASP TYR HIS VAL ALA LEU ASP ASN ALA ARG
SEQRES 10 A 431 GLU LYS ALA ARG GLY ALA LYS ALA ILE GLY THR THR GLY
SEQRES 11 A 431 ARG GLY ILE GLY PRO ALA TYR GLU ASP LYS VAL ALA ARG
SEQRES 12 A 431 ARG GLY LEU ARG VAL GLY ASP LEU PHE ASP LYS GLU THR
SEQRES 13 A 431 PHE ALA GLU LYS LEU LYS GLU VAL MET GLU TYR HIS ASN
SEQRES 14 A 431 PHE GLN LEU VAL ASN TYR TYR LYS ALA GLU ALA VAL ASP
SEQRES 15 A 431 TYR GLN LYS VAL LEU ASP ASP THR MET ALA VAL ALA ASP
SEQRES 16 A 431 ILE LEU THR SER MET VAL VAL ASP VAL SER ASP LEU LEU
SEQRES 17 A 431 ASP GLN ALA ARG GLN ARG GLY ASP PHE VAL MET PHE GLU
SEQRES 18 A 431 GLY ALA GLN GLY THR LEU LEU ASP ILE ASP HIS GLY THR
SEQRES 19 A 431 TYR PRO TYR VAL THR SER SER ASN THR THR ALA GLY GLY
SEQRES 20 A 431 VAL ALA THR GLY SER GLY LEU GLY PRO ARG TYR VAL ASP
SEQRES 21 A 431 TYR VAL LEU GLY ILE LEU LYS ALA TYR SER THR ARG VAL
SEQRES 22 A 431 GLY ALA GLY PRO PHE PRO THR GLU LEU PHE ASP GLU THR
SEQRES 23 A 431 GLY GLU PHE LEU CYS LYS GLN GLY ASN GLU PHE GLY ALA
SEQRES 24 A 431 THR THR GLY ARG ARG ARG ARG THR GLY TRP LEU ASP THR
SEQRES 25 A 431 VAL ALA VAL ARG ARG ALA VAL GLN LEU ASN SER LEU SER
SEQRES 26 A 431 GLY PHE CYS LEU THR LYS LEU ASP VAL LEU ASP GLY LEU
SEQRES 27 A 431 LYS GLU VAL LYS LEU CYS VAL ALA TYR ARG MET PRO ASP
SEQRES 28 A 431 GLY ARG GLU VAL THR THR THR PRO LEU ALA ALA ASP ASP
SEQRES 29 A 431 TRP LYS GLY VAL GLU PRO ILE TYR GLU THR MET PRO GLY
SEQRES 30 A 431 TRP SER GLU SER THR PHE GLY VAL LYS ASP ARG SER GLY
SEQRES 31 A 431 LEU PRO GLN ALA ALA LEU ASN TYR ILE LYS ARG ILE GLU
SEQRES 32 A 431 GLU LEU THR GLY VAL PRO ILE ASP ILE ILE SER THR GLY
SEQRES 33 A 431 PRO ASP ARG THR GLU THR MET ILE LEU ARG ASP PRO PHE
SEQRES 34 A 431 ASP ALA
HET MG A 435 1
HET GDP A 432 40
HET HDA A 437 9
HET PGS A 440 37
HETNAM MG MAGNESIUM ION
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
HETNAM HDA HADACIDIN
HETNAM PGS 2-DEAZO-6-THIOPHOSPHATE GUANOSINE-5'-MONOPHOSPHATE
FORMUL 2 MG MG 2+
FORMUL 3 GDP C10 H15 N5 O11 P2
FORMUL 4 HDA C3 H5 N O4
FORMUL 5 PGS C10 H15 N4 O10 P2 S 1+
FORMUL 6 HOH *454(H2 O)
HELIX 1 1 LYS A 16 ARG A 26 1 11
HELIX 2 2 PRO A 76 ASP A 88 1 13
HELIX 3 3 VAL A 93 ARG A 96 1 4
HELIX 4 4 ASP A 108 ALA A 120 1 13
HELIX 5 5 GLY A 122 LYS A 124 5 3
HELIX 6 6 ILE A 133 ALA A 142 1 10
HELIX 7 7 VAL A 148 LEU A 151 5 4
HELIX 8 8 LYS A 154 ASN A 174 1 21
HELIX 9 9 TYR A 183 MET A 200 1 18
HELIX 10 10 VAL A 204 ARG A 214 1 11
HELIX 11 11 THR A 226 LEU A 228 5 3
HELIX 12 12 ALA A 245 SER A 252 5 8
HELIX 13 13 PRO A 256 TYR A 258 5 3
HELIX 14 14 GLU A 285 GLN A 293 1 9
HELIX 15 15 THR A 312 ASN A 322 1 11
HELIX 16 16 LEU A 332 LEU A 335 5 4
HELIX 17 17 ALA A 362 TRP A 365 5 4
HELIX 18 18 ARG A 388 GLY A 390 5 3
HELIX 19 19 GLN A 393 THR A 406 1 14
SHEET 1 A 9 THR A 422 ILE A 424 0
SHEET 2 A 9 ILE A 410 SER A 414 -1 N ILE A 413 O MET A 423
SHEET 3 A 9 GLY A 326 LEU A 329 1 N PHE A 327 O ASP A 411
SHEET 4 A 9 TYR A 261 LEU A 266 1 N GLY A 264 O GLY A 326
SHEET 5 A 9 ASN A 3 GLY A 8 1 N VAL A 5 O TYR A 261
SHEET 6 A 9 VAL A 218 GLU A 221 1 N VAL A 218 O VAL A 4
SHEET 7 A 9 TYR A 29 ARG A 32 1 N TYR A 29 O MET A 219
SHEET 8 A 9 THR A 65 ILE A 68 1 N THR A 65 O VAL A 30
SHEET 9 A 9 LEU A 97 LEU A 99 1 N LEU A 98 O SER A 66
SHEET 1 B 2 LEU A 43 ILE A 45 0
SHEET 2 B 2 GLU A 48 THR A 50 -1 N THR A 50 O LEU A 43
SHEET 1 C 2 VAL A 73 SER A 75 0
SHEET 2 C 2 PRO A 104 ILE A 106 1 N PRO A 104 O LEU A 74
SHEET 1 D 2 SER A 270 ARG A 272 0
SHEET 2 D 2 ARG A 306 GLY A 308 -1 N GLY A 308 O SER A 270
SHEET 1 E 2 GLU A 340 LYS A 342 0
SHEET 2 E 2 THR A 374 PRO A 376 -1 N MET A 375 O VAL A 341
SHEET 1 F 2 ALA A 346 ARG A 348 0
SHEET 2 F 2 GLU A 369 ILE A 371 -1 N ILE A 371 O ALA A 346
LINK OD1 ASP A 13 MG MG A 435 1555 1555 2.81
LINK O GLY A 40 MG MG A 435 1555 1555 2.09
LINK O1B GDP A 432 MG MG A 435 1555 1555 1.82
LINK O2A GDP A 432 MG MG A 435 1555 1555 1.79
LINK MG MG A 435 O HDA A 437 1555 1555 2.02
LINK MG MG A 435 O3P PGS A 440 1555 1555 2.18
CISPEP 1 TYR A 235 PRO A 236 0 0.05
SITE 1 GNS 13 ASP A 13 GLU A 14 GLY A 15 LYS A 16
SITE 2 GNS 13 GLY A 17 LYS A 18 LYS A 331 LEU A 332
SITE 3 GNS 13 ASP A 333 SER A 414 THR A 415 GLY A 416
SITE 4 GNS 13 PRO A 417
SITE 1 IMP 6 ASN A 38 THR A 129 ARG A 143 GLN A 224
SITE 2 IMP 6 THR A 239 VAL A 273
SITE 1 ASP 3 ARG A 305 THR A 301 ARG A 303
SITE 1 AC1 5 ASP A 13 GLY A 40 GDP A 432 HDA A 437
SITE 2 AC1 5 PGS A 440
SITE 1 AC2 21 ASP A 13 GLU A 14 GLY A 15 LYS A 16
SITE 2 AC2 21 GLY A 17 GLY A 40 HIS A 41 THR A 42
SITE 3 AC2 21 ARG A 305 LYS A 331 ASP A 333 SER A 414
SITE 4 AC2 21 GLY A 416 PRO A 417 MG A 435 HDA A 437
SITE 5 AC2 21 PGS A 440 HOH A 502 HOH A 616 HOH A 646
SITE 6 AC2 21 HOH A 951
SITE 1 AC3 13 ASP A 13 ASN A 38 GLY A 40 THR A 129
SITE 2 AC3 13 GLY A 298 ALA A 299 THR A 300 THR A 301
SITE 3 AC3 13 ARG A 303 ARG A 305 GDP A 432 MG A 435
SITE 4 AC3 13 PGS A 440
SITE 1 AC4 26 TRP A 11 GLY A 12 ASP A 13 LYS A 16
SITE 2 AC4 26 ASN A 38 ALA A 39 GLY A 40 HIS A 41
SITE 3 AC4 26 GLY A 127 THR A 128 THR A 129 ARG A 143
SITE 4 AC4 26 ALA A 223 GLN A 224 VAL A 238 THR A 239
SITE 5 AC4 26 VAL A 273 GLY A 274 ARG A 303 GDP A 432
SITE 6 AC4 26 MG A 435 HDA A 437 HOH A 636 HOH A 699
SITE 7 AC4 26 HOH A 716 HOH A 732
CRYST1 80.540 80.540 158.150 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 0.012416 0.007168 0.000000 0.00000
SCALE2 0.000000 0.014337 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006323 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
