HEADER LIGASE 02-DEC-97 11AS
TITLE ASPARAGINE SYNTHETASE MUTANT C51A, C315A COMPLEXED WITH L-
TITLE 2 ASPARAGINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ASPARAGINE SYNTHETASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 6.3.1.1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K12;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K-12;
SOURCE 5 GENE: ASNA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PUC18;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PUNAD37 CYS-FREE;
SOURCE 11 EXPRESSION_SYSTEM_GENE: ASNA
KEYWDS LIGASE, ASPARAGINE SYNTHETASE, NITROGEN FIXATION
EXPDTA X-RAY DIFFRACTION
AUTHOR T.NAKATSU,H.KATO,J.ODA
REVDAT 3 24-FEB-09 11AS 1 VERSN
REVDAT 2 16-FEB-99 11AS 3 SOURCE COMPND REMARK TITLE
REVDAT 2 2 3 HETATM KEYWDS
REVDAT 1 30-DEC-98 11AS 0
JRNL AUTH T.NAKATSU,H.KATO,J.ODA
JRNL TITL CRYSTAL STRUCTURE OF ASPARAGINE SYNTHETASE REVEALS
JRNL TITL 2 A CLOSE EVOLUTIONARY RELATIONSHIP TO CLASS II
JRNL TITL 3 AMINOACYL-TRNA SYNTHETASE.
JRNL REF NAT.STRUCT.BIOL. V. 5 15 1998
JRNL REFN ISSN 1072-8368
JRNL PMID 9437423
JRNL DOI 10.1038/NSB0198-15
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.NAKATSU,H.KATO,J.ODA
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY CRYSTALLOGRAPHIC
REMARK 1 TITL 2 STUDY OF ASPARAGINE SYNTHETASE FROM ESCHERICHIA
REMARK 1 TITL 3 COLI
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 52 604 1996
REMARK 1 REFN ISSN 0907-4449
REMARK 1 REFERENCE 2
REMARK 1 AUTH A.SUGIYAMA,H.KATO,T.NISHIOKA,J.ODA
REMARK 1 TITL OVEREXPRESSION AND PURIFICATION OF ASPARAGINE
REMARK 1 TITL 2 SYNTHETASE FROM ESCHERICHIA COLI
REMARK 1 REF BIOSCI.BIOTECHNOL.BIOCHEM. V. 56 376 1992
REMARK 1 REFN ISSN 0916-8451
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
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) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0010
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 72.2
REMARK 3 NUMBER OF REFLECTIONS : 17421
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 SET) : 0.155
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1715
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 : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.61
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 56.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1438
REMARK 3 BIN R VALUE (WORKING SET) : 0.1810
REMARK 3 BIN FREE R VALUE : 0.3340
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 136
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 : 5118
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 84
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 11.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.20
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) : 0.21
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
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) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.20
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 28.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 2.70
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 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : PARAM19.SOL
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TOPH19.SOL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 11AS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : APR-95
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RUH3R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE(002)
REMARK 200 OPTICS : COLLIMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : PROCESS
REMARK 200 DATA SCALING SOFTWARE : PROCESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17805
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 73.8
REMARK 200 DATA REDUNDANCY : 2.900
REMARK 200 R MERGE (I) : 0.10500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 54.5
REMARK 200 DATA REDUNDANCY IN SHELL : 1.70
REMARK 200 R MERGE FOR SHELL (I) : 0.20000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: PHASES
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN CRYSTALLIZED FROM 45%
REMARK 280 SATURATED AMMONIUM SULFATE, 22 MM ASPARAGINE, 88 MM MGCL2, 10
REMARK 280 %(W/V) GLYCEROL 5 MM 2-MERCAPTOETHANOL, 50 MM HEPES, PH7.5
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 63.10000
REMARK 290 SMTRY3 2 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: 4040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25020 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 LYS A 2
REMARK 465 THR A 3
REMARK 465 MET B 1
REMARK 465 LYS B 2
REMARK 465 THR B 3
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 ARG A 105 NE - CZ - NH1 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG A 185 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG B 10 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG B 39 NE - CZ - NH1 ANGL. DEV. = -3.2 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 PRO A 35 170.72 -54.15
REMARK 500 VAL A 40 103.71 -58.20
REMARK 500 LEU A 48 -139.07 67.11
REMARK 500 VAL A 55 99.98 -63.46
REMARK 500 LEU A 62 76.94 -107.46
REMARK 500 VAL A 70 118.12 -5.95
REMARK 500 LEU A 73 33.00 -91.33
REMARK 500 PRO A 159 167.49 -49.48
REMARK 500 PHE A 160 -23.61 -174.47
REMARK 500 ASP A 163 40.41 -76.39
REMARK 500 GLN A 164 122.19 178.88
REMARK 500 TYR A 177 78.69 -109.47
REMARK 500 ASP A 207 -152.65 -93.06
REMARK 500 TYR A 218 -13.85 -146.49
REMARK 500 GLU A 226 7.96 -67.67
REMARK 500 ALA A 246 -178.43 -60.45
REMARK 500 VAL A 256 148.93 -37.63
REMARK 500 PRO A 288 -167.77 -78.40
REMARK 500 SER A 328 27.77 85.62
REMARK 500 LEU B 48 -106.48 39.06
REMARK 500 GLN B 56 78.35 -103.76
REMARK 500 VAL B 70 129.56 -33.90
REMARK 500 LEU B 73 49.34 -96.14
REMARK 500 ASP B 85 86.49 52.94
REMARK 500 SER B 131 -61.35 -2.44
REMARK 500 TYR B 177 71.19 -119.26
REMARK 500 LEU B 205 -166.45 -103.27
REMARK 500 TYR B 218 -61.94 -148.02
REMARK 500 LEU B 227 1.32 -68.65
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 69 VAL A 70 142.39
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 ARG A 10 0.26 SIDE_CHAIN
REMARK 500 ARG A 21 0.27 SIDE_CHAIN
REMARK 500 ARG A 26 0.20 SIDE_CHAIN
REMARK 500 ARG A 39 0.16 SIDE_CHAIN
REMARK 500 ARG A 78 0.24 SIDE_CHAIN
REMARK 500 ARG A 100 0.13 SIDE_CHAIN
REMARK 500 ARG A 105 0.20 SIDE_CHAIN
REMARK 500 ARG A 121 0.20 SIDE_CHAIN
REMARK 500 ARG A 128 0.19 SIDE_CHAIN
REMARK 500 ARG A 176 0.25 SIDE_CHAIN
REMARK 500 TYR A 177 0.11 SIDE_CHAIN
REMARK 500 ARG A 185 0.25 SIDE_CHAIN
REMARK 500 ARG A 210 0.22 SIDE_CHAIN
REMARK 500 ARG A 214 0.25 SIDE_CHAIN
REMARK 500 ARG A 255 0.26 SIDE_CHAIN
REMARK 500 ARG A 273 0.25 SIDE_CHAIN
REMARK 500 ARG A 284 0.27 SIDE_CHAIN
REMARK 500 ARG A 299 0.26 SIDE_CHAIN
REMARK 500 ARG A 323 0.24 SIDE_CHAIN
REMARK 500 ARG B 10 0.25 SIDE_CHAIN
REMARK 500 ARG B 21 0.26 SIDE_CHAIN
REMARK 500 ARG B 26 0.15 SIDE_CHAIN
REMARK 500 ARG B 39 0.25 SIDE_CHAIN
REMARK 500 ARG B 78 0.25 SIDE_CHAIN
REMARK 500 ARG B 100 0.20 SIDE_CHAIN
REMARK 500 TYR B 113 0.07 SIDE_CHAIN
REMARK 500 ARG B 121 0.23 SIDE_CHAIN
REMARK 500 ARG B 128 0.07 SIDE_CHAIN
REMARK 500 ARG B 176 0.24 SIDE_CHAIN
REMARK 500 TYR B 177 0.09 SIDE_CHAIN
REMARK 500 ARG B 185 0.22 SIDE_CHAIN
REMARK 500 ARG B 187 0.14 SIDE_CHAIN
REMARK 500 ARG B 210 0.24 SIDE_CHAIN
REMARK 500 ARG B 214 0.15 SIDE_CHAIN
REMARK 500 ARG B 255 0.26 SIDE_CHAIN
REMARK 500 ARG B 273 0.23 SIDE_CHAIN
REMARK 500 ARG B 284 0.25 SIDE_CHAIN
REMARK 500 ARG B 323 0.23 SIDE_CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 VAL A 69 12.59
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 ASN A 331
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ASN B 331
DBREF 11AS A 1 330 UNP P00963 ASNA_ECOLI 1 330
DBREF 11AS B 1 330 UNP P00963 ASNA_ECOLI 1 330
SEQADV 11AS ALA A 51 UNP P00963 CYS 51 ENGINEERED
SEQADV 11AS ALA A 315 UNP P00963 CYS 315 ENGINEERED
SEQADV 11AS ALA B 51 UNP P00963 CYS 51 ENGINEERED
SEQADV 11AS ALA B 315 UNP P00963 CYS 315 ENGINEERED
SEQRES 1 A 330 MET LYS THR ALA TYR ILE ALA LYS GLN ARG GLN ILE SER
SEQRES 2 A 330 PHE VAL LYS SER HIS PHE SER ARG GLN LEU GLU GLU ARG
SEQRES 3 A 330 LEU GLY LEU ILE GLU VAL GLN ALA PRO ILE LEU SER ARG
SEQRES 4 A 330 VAL GLY ASP GLY THR GLN ASP ASN LEU SER GLY ALA GLU
SEQRES 5 A 330 LYS ALA VAL GLN VAL LYS VAL LYS ALA LEU PRO ASP ALA
SEQRES 6 A 330 GLN PHE GLU VAL VAL HIS SER LEU ALA LYS TRP LYS ARG
SEQRES 7 A 330 GLN THR LEU GLY GLN HIS ASP PHE SER ALA GLY GLU GLY
SEQRES 8 A 330 LEU TYR THR HIS MET LYS ALA LEU ARG PRO ASP GLU ASP
SEQRES 9 A 330 ARG LEU SER PRO LEU HIS SER VAL TYR VAL ASP GLN TRP
SEQRES 10 A 330 ASP TRP GLU ARG VAL MET GLY ASP GLY GLU ARG GLN PHE
SEQRES 11 A 330 SER THR LEU LYS SER THR VAL GLU ALA ILE TRP ALA GLY
SEQRES 12 A 330 ILE LYS ALA THR GLU ALA ALA VAL SER GLU GLU PHE GLY
SEQRES 13 A 330 LEU ALA PRO PHE LEU PRO ASP GLN ILE HIS PHE VAL HIS
SEQRES 14 A 330 SER GLN GLU LEU LEU SER ARG TYR PRO ASP LEU ASP ALA
SEQRES 15 A 330 LYS GLY ARG GLU ARG ALA ILE ALA LYS ASP LEU GLY ALA
SEQRES 16 A 330 VAL PHE LEU VAL GLY ILE GLY GLY LYS LEU SER ASP GLY
SEQRES 17 A 330 HIS ARG HIS ASP VAL ARG ALA PRO ASP TYR ASP ASP TRP
SEQRES 18 A 330 SER THR PRO SER GLU LEU GLY HIS ALA GLY LEU ASN GLY
SEQRES 19 A 330 ASP ILE LEU VAL TRP ASN PRO VAL LEU GLU ASP ALA PHE
SEQRES 20 A 330 GLU LEU SER SER MET GLY ILE ARG VAL ASP ALA ASP THR
SEQRES 21 A 330 LEU LYS HIS GLN LEU ALA LEU THR GLY ASP GLU ASP ARG
SEQRES 22 A 330 LEU GLU LEU GLU TRP HIS GLN ALA LEU LEU ARG GLY GLU
SEQRES 23 A 330 MET PRO GLN THR ILE GLY GLY GLY ILE GLY GLN SER ARG
SEQRES 24 A 330 LEU THR MET LEU LEU LEU GLN LEU PRO HIS ILE GLY GLN
SEQRES 25 A 330 VAL GLN ALA GLY VAL TRP PRO ALA ALA VAL ARG GLU SER
SEQRES 26 A 330 VAL PRO SER LEU LEU
SEQRES 1 B 330 MET LYS THR ALA TYR ILE ALA LYS GLN ARG GLN ILE SER
SEQRES 2 B 330 PHE VAL LYS SER HIS PHE SER ARG GLN LEU GLU GLU ARG
SEQRES 3 B 330 LEU GLY LEU ILE GLU VAL GLN ALA PRO ILE LEU SER ARG
SEQRES 4 B 330 VAL GLY ASP GLY THR GLN ASP ASN LEU SER GLY ALA GLU
SEQRES 5 B 330 LYS ALA VAL GLN VAL LYS VAL LYS ALA LEU PRO ASP ALA
SEQRES 6 B 330 GLN PHE GLU VAL VAL HIS SER LEU ALA LYS TRP LYS ARG
SEQRES 7 B 330 GLN THR LEU GLY GLN HIS ASP PHE SER ALA GLY GLU GLY
SEQRES 8 B 330 LEU TYR THR HIS MET LYS ALA LEU ARG PRO ASP GLU ASP
SEQRES 9 B 330 ARG LEU SER PRO LEU HIS SER VAL TYR VAL ASP GLN TRP
SEQRES 10 B 330 ASP TRP GLU ARG VAL MET GLY ASP GLY GLU ARG GLN PHE
SEQRES 11 B 330 SER THR LEU LYS SER THR VAL GLU ALA ILE TRP ALA GLY
SEQRES 12 B 330 ILE LYS ALA THR GLU ALA ALA VAL SER GLU GLU PHE GLY
SEQRES 13 B 330 LEU ALA PRO PHE LEU PRO ASP GLN ILE HIS PHE VAL HIS
SEQRES 14 B 330 SER GLN GLU LEU LEU SER ARG TYR PRO ASP LEU ASP ALA
SEQRES 15 B 330 LYS GLY ARG GLU ARG ALA ILE ALA LYS ASP LEU GLY ALA
SEQRES 16 B 330 VAL PHE LEU VAL GLY ILE GLY GLY LYS LEU SER ASP GLY
SEQRES 17 B 330 HIS ARG HIS ASP VAL ARG ALA PRO ASP TYR ASP ASP TRP
SEQRES 18 B 330 SER THR PRO SER GLU LEU GLY HIS ALA GLY LEU ASN GLY
SEQRES 19 B 330 ASP ILE LEU VAL TRP ASN PRO VAL LEU GLU ASP ALA PHE
SEQRES 20 B 330 GLU LEU SER SER MET GLY ILE ARG VAL ASP ALA ASP THR
SEQRES 21 B 330 LEU LYS HIS GLN LEU ALA LEU THR GLY ASP GLU ASP ARG
SEQRES 22 B 330 LEU GLU LEU GLU TRP HIS GLN ALA LEU LEU ARG GLY GLU
SEQRES 23 B 330 MET PRO GLN THR ILE GLY GLY GLY ILE GLY GLN SER ARG
SEQRES 24 B 330 LEU THR MET LEU LEU LEU GLN LEU PRO HIS ILE GLY GLN
SEQRES 25 B 330 VAL GLN ALA GLY VAL TRP PRO ALA ALA VAL ARG GLU SER
SEQRES 26 B 330 VAL PRO SER LEU LEU
HET ASN A 331 9
HET ASN B 331 9
HETNAM ASN ASPARAGINE
FORMUL 3 ASN 2(C4 H8 N2 O3)
FORMUL 5 HOH *84(H2 O)
HELIX 1 1 TYR A 5 LEU A 27 1 23
HELIX 2 2 ALA A 74 GLN A 83 1 10
HELIX 3 3 PHE A 130 GLU A 154 1 25
HELIX 4 4 SER A 170 ARG A 176 1 7
HELIX 5 5 ALA A 182 LEU A 193 1 12
HELIX 6 6 ALA A 258 THR A 268 1 11
HELIX 7 7 GLU A 271 GLU A 275 5 5
HELIX 8 8 GLU A 277 LEU A 283 1 7
HELIX 9 9 GLN A 297 LEU A 305 1 9
HELIX 10 10 ILE A 310 GLN A 312 5 3
HELIX 11 11 ALA A 320 SER A 325 1 6
HELIX 12 12 TYR B 5 ARG B 26 1 22
HELIX 13 13 TRP B 76 GLN B 83 1 8
HELIX 14 14 PHE B 130 PHE B 155 1 26
HELIX 15 15 SER B 170 ARG B 176 1 7
HELIX 16 16 ALA B 182 LEU B 193 1 12
HELIX 17 17 ALA B 258 THR B 268 1 11
HELIX 18 18 GLU B 271 GLU B 275 5 5
HELIX 19 19 GLU B 277 LEU B 283 1 7
HELIX 20 20 GLN B 297 LEU B 304 1 8
HELIX 21 21 ILE B 310 GLN B 312 5 3
HELIX 22 22 ALA B 320 SER B 325 1 6
SHEET 1 A 8 LEU A 29 GLU A 31 0
SHEET 2 A 8 GLY A 91 LEU A 99 1 N GLY A 91 O ILE A 30
SHEET 3 A 8 TYR A 113 VAL A 122 -1 N GLU A 120 O LEU A 92
SHEET 4 A 8 THR A 290 GLY A 296 -1 N ILE A 295 O TRP A 117
SHEET 5 A 8 ASP A 245 ILE A 254 -1 N GLY A 253 O GLY A 292
SHEET 6 A 8 ASN A 233 ASN A 240 -1 N ASN A 240 O ASP A 245
SHEET 7 A 8 ALA A 195 VAL A 199 -1 N LEU A 198 O ASP A 235
SHEET 8 A 8 HIS A 166 HIS A 169 1 N HIS A 166 O PHE A 197
SHEET 1 B 2 LEU A 37 ARG A 39 0
SHEET 2 B 2 PHE A 67 VAL A 69 -1 N GLU A 68 O SER A 38
SHEET 1 C 8 LEU B 29 GLU B 31 0
SHEET 2 C 8 GLY B 91 LEU B 99 1 N GLY B 91 O ILE B 30
SHEET 3 C 8 TYR B 113 VAL B 122 -1 N GLU B 120 O LEU B 92
SHEET 4 C 8 THR B 290 GLY B 296 -1 N ILE B 295 O TRP B 117
SHEET 5 C 8 ASP B 245 ILE B 254 -1 N GLY B 253 O GLY B 292
SHEET 6 C 8 ASN B 233 ASN B 240 -1 N ASN B 240 O ASP B 245
SHEET 7 C 8 ALA B 195 VAL B 199 -1 N LEU B 198 O ASP B 235
SHEET 8 C 8 HIS B 166 HIS B 169 1 N HIS B 166 O PHE B 197
SHEET 1 D 2 LEU B 37 ARG B 39 0
SHEET 2 D 2 PHE B 67 VAL B 69 -1 N GLU B 68 O SER B 38
SITE 1 AC1 10 ASP A 46 SER A 72 ALA A 74 LYS A 77
SITE 2 AC1 10 ARG A 100 GLN A 116 ASP A 118 TYR A 218
SITE 3 AC1 10 SER A 251 ARG A 255
SITE 1 AC2 8 ASP B 46 SER B 72 LYS B 77 ASP B 118
SITE 2 AC2 8 TYR B 218 SER B 251 ARG B 255 GLY B 293
CRYST1 52.900 126.200 52.780 90.00 105.34 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 0.018904 0.000000 0.005186 0.00000
SCALE2 0.000000 0.007924 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019647 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
