HEADER TRANSFERASE 05-APR-05 1ZA2
TITLE STRUCTURE OF WILD-TYPE E. COLI ASPARTATE TRANSCARBAMOYLASE IN THE
TITLE 2 PRESENCE OF CTP, CARBAMOYL PHOSPHATE AT 2.50 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ASPARTATE CARBAMOYLTRANSFERASE CATALYTIC CHAIN;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: ASPARTATE TRANSCARBAMYLASE, ATCASE;
COMPND 5 EC: 2.1.3.2;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: ASPARTATE CARBAMOYLTRANSFERASE REGULATORY CHAIN;
COMPND 9 CHAIN: B, D;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: PYRB;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: EK1104;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PEK54;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 12 ORGANISM_TAXID: 562;
SOURCE 13 GENE: PYRI;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: EK1104;
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PEK54
KEYWDS ORDERED SUBSTRATE BINDING, COOPERATIVITY, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.WANG,K.A.STIEGLITZ,J.P.CARDIA,E.R.KANTROWITZ
REVDAT 6 23-AUG-23 1ZA2 1 REMARK SEQADV LINK
REVDAT 5 16-NOV-11 1ZA2 1 HETATM
REVDAT 4 13-JUL-11 1ZA2 1 VERSN
REVDAT 3 24-FEB-09 1ZA2 1 VERSN
REVDAT 2 13-DEC-05 1ZA2 1 JRNL
REVDAT 1 07-JUN-05 1ZA2 0
JRNL AUTH J.WANG,K.A.STIEGLITZ,J.P.CARDIA,E.R.KANTROWITZ
JRNL TITL STRUCTURAL BASIS FOR ORDERED SUBSTRATE BINDING AND
JRNL TITL 2 COOPERATIVITY IN ASPARTATE TRANSCARBAMOYLASE
JRNL REF PROC.NATL.ACAD.SCI.USA V. 102 8881 2005
JRNL REFN ISSN 0027-8424
JRNL PMID 15951418
JRNL DOI 10.1073/PNAS.0503742102
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
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 : 40371
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) : 0.197
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 4037
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 : 7084
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 93
REMARK 3 SOLVENT ATOMS : 381
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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) : NULL
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) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 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: NULL
REMARK 4
REMARK 4 1ZA2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-APR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032487.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-AUG-04
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 5.7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTAM Q315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42599
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 9.000
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 36.7000
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) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.10
REMARK 200 R MERGE FOR SHELL (I) : 0.44700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1TU0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 40 MM CITRIC ACID, 3 MM SODIUM AZIDE,
REMARK 280 1MM 2-MERCAPTOETHANOL, 1MM CTP, 0.2MM EDTA, PH 5.7,
REMARK 280 MICRODIALYSIS, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3 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
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-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 -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 0.00000
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 0.00000
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 0.00000
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 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: DODECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 36510 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 100930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -133.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 121.44200
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 60.72100
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 105.17186
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 373 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 374 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 396 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 420 LIES ON A SPECIAL POSITION.
REMARK 375 HOH C 411 LIES ON A SPECIAL POSITION.
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 B 1
REMARK 465 THR B 2
REMARK 465 HIS B 3
REMARK 465 ASP B 4
REMARK 465 ASN B 5
REMARK 465 LYS B 6
REMARK 465 LEU B 7
REMARK 465 GLN B 8
REMARK 465 VAL B 9
REMARK 465 MET D 1
REMARK 465 THR D 2
REMARK 465 HIS D 3
REMARK 465 ASP D 4
REMARK 465 ASN D 5
REMARK 465 LYS D 6
REMARK 465 LEU D 7
REMARK 465 GLN D 8
REMARK 465 VAL D 9
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 NA NA A 311 NA NA A 311 2655 0.80
REMARK 500 O HOH C 361 O HOH C 361 2655 1.86
REMARK 500 O HOH A 456 O HOH A 457 3665 2.14
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 81 N - CA - C ANGL. DEV. = -16.9 DEGREES
REMARK 500 PRO C 36 C - N - CA ANGL. DEV. = 10.2 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 SER A 52 138.94 -175.10
REMARK 500 ASN A 132 -87.01 -92.85
REMARK 500 HIS A 134 59.89 -166.13
REMARK 500 GLN A 231 88.75 -60.27
REMARK 500 ALA A 245 -18.69 -44.12
REMARK 500 LEU A 267 160.29 65.61
REMARK 500 VAL A 270 -74.44 -136.82
REMARK 500 ALA A 295 -60.42 102.04
REMARK 500 ARG A 306 -101.87 -41.05
REMARK 500 LEU A 308 -178.74 -56.41
REMARK 500 VAL A 309 14.05 177.91
REMARK 500 ALA B 11 84.82 -162.96
REMARK 500 ILE B 12 149.16 -29.74
REMARK 500 GLU B 37 57.09 -95.33
REMARK 500 GLU B 52 -47.24 -139.03
REMARK 500 TYR B 89 -7.73 57.40
REMARK 500 VAL B 91 70.71 -68.68
REMARK 500 VAL B 92 -75.86 -46.46
REMARK 500 ASN B 105 -45.35 69.06
REMARK 500 ARG B 130 -146.60 -158.03
REMARK 500 ALA B 131 88.78 -43.19
REMARK 500 TYR B 140 -75.54 -84.94
REMARK 500 HIS C 41 -7.25 82.06
REMARK 500 SER C 52 139.06 -176.89
REMARK 500 THR C 53 -62.30 -109.99
REMARK 500 ASP C 75 -168.16 -165.02
REMARK 500 ALA C 77 35.09 -152.89
REMARK 500 SER C 80 -43.53 166.09
REMARK 500 LYS C 84 -143.88 14.13
REMARK 500 GLU C 86 75.89 31.11
REMARK 500 ALA C 101 147.85 -170.04
REMARK 500 ASN C 132 -92.47 -92.74
REMARK 500 HIS C 134 56.60 -166.08
REMARK 500 ALA C 220 -10.36 -48.94
REMARK 500 PRO C 237 -35.40 -38.17
REMARK 500 ALA C 245 -28.74 -34.26
REMARK 500 LEU C 267 156.74 65.59
REMARK 500 VAL C 270 -80.10 -119.20
REMARK 500 LYS D 13 -98.46 -72.59
REMARK 500 LYS D 34 63.90 30.94
REMARK 500 GLU D 37 49.90 -90.08
REMARK 500 MET D 53 11.99 -166.59
REMARK 500 ILE D 86 115.91 1.40
REMARK 500 VAL D 91 83.15 -64.99
REMARK 500 VAL D 92 -85.31 -49.25
REMARK 500 ASN D 105 -52.14 61.06
REMARK 500 ALA D 131 119.26 67.96
REMARK 500 ASN D 132 -39.36 92.65
REMARK 500 GLU D 142 1.05 85.35
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 NA A 311 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 323 O
REMARK 620 2 HOH A 379 O 95.8
REMARK 620 3 HOH A 379 O 98.5 126.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 154 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 109 SG
REMARK 620 2 CYS B 114 SG 114.1
REMARK 620 3 CYS B 138 SG 111.0 106.4
REMARK 620 4 CYS B 141 SG 101.9 113.4 110.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 154 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 109 SG
REMARK 620 2 CYS D 114 SG 116.1
REMARK 620 3 CYS D 138 SG 111.1 106.4
REMARK 620 4 CYS D 141 SG 95.6 110.2 117.6
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 311
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CTP B 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CTP D 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CP A 312
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CP C 311
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CP A 313
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CP C 312
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1TU0 RELATED DB: PDB
REMARK 900 THE CATALYTIC CHAIN E50A MUTANT OF E. COLI ASPARTATE
REMARK 900 TRANSCARBAMOYLASE IN THE PRESENCE OF PHOSPHONOACETAMIDE
REMARK 900 RELATED ID: 1ZA1 RELATED DB: PDB
REMARK 900 STRUCTURE OF WILD-TYPE E. COLI ASPARTATE TRANSCARBAMOYLASE IN THE
REMARK 900 PRESENCE OF CTP AT 2.20 A RESOLUTION
DBREF 1ZA2 A 1 310 UNP P00479 PYRB_ECOLI 1 310
DBREF 1ZA2 C 1 310 UNP P00479 PYRB_ECOLI 1 310
DBREF 1ZA2 B 2 153 UNP P00478 PYRI_ECOLI 1 152
DBREF 1ZA2 D 2 153 UNP P00478 PYRI_ECOLI 1 152
SEQADV 1ZA2 MET B 1 UNP P00478 INITIATING METHIONINE
SEQADV 1ZA2 MET D 1 UNP P00478 INITIATING METHIONINE
SEQRES 1 A 310 ALA ASN PRO LEU TYR GLN LYS HIS ILE ILE SER ILE ASN
SEQRES 2 A 310 ASP LEU SER ARG ASP ASP LEU ASN LEU VAL LEU ALA THR
SEQRES 3 A 310 ALA ALA LYS LEU LYS ALA ASN PRO GLN PRO GLU LEU LEU
SEQRES 4 A 310 LYS HIS LYS VAL ILE ALA SER CYS PHE PHE GLU ALA SER
SEQRES 5 A 310 THR ARG THR ARG LEU SER PHE GLU THR SER MET HIS ARG
SEQRES 6 A 310 LEU GLY ALA SER VAL VAL GLY PHE SER ASP SER ALA ASN
SEQRES 7 A 310 THR SER LEU GLY LYS LYS GLY GLU THR LEU ALA ASP THR
SEQRES 8 A 310 ILE SER VAL ILE SER THR TYR VAL ASP ALA ILE VAL MET
SEQRES 9 A 310 ARG HIS PRO GLN GLU GLY ALA ALA ARG LEU ALA THR GLU
SEQRES 10 A 310 PHE SER GLY ASN VAL PRO VAL LEU ASN ALA GLY ASP GLY
SEQRES 11 A 310 SER ASN GLN HIS PRO THR GLN THR LEU LEU ASP LEU PHE
SEQRES 12 A 310 THR ILE GLN GLU THR GLN GLY ARG LEU ASP ASN LEU HIS
SEQRES 13 A 310 VAL ALA MET VAL GLY ASP LEU LYS TYR GLY ARG THR VAL
SEQRES 14 A 310 HIS SER LEU THR GLN ALA LEU ALA LYS PHE ASP GLY ASN
SEQRES 15 A 310 ARG PHE TYR PHE ILE ALA PRO ASP ALA LEU ALA MET PRO
SEQRES 16 A 310 GLN TYR ILE LEU ASP MET LEU ASP GLU LYS GLY ILE ALA
SEQRES 17 A 310 TRP SER LEU HIS SER SER ILE GLU GLU VAL MET ALA GLU
SEQRES 18 A 310 VAL ASP ILE LEU TYR MET THR ARG VAL GLN LYS GLU ARG
SEQRES 19 A 310 LEU ASP PRO SER GLU TYR ALA ASN VAL LYS ALA GLN PHE
SEQRES 20 A 310 VAL LEU ARG ALA SER ASP LEU HIS ASN ALA LYS ALA ASN
SEQRES 21 A 310 MET LYS VAL LEU HIS PRO LEU PRO ARG VAL ASP GLU ILE
SEQRES 22 A 310 ALA THR ASP VAL ASP LYS THR PRO HIS ALA TRP TYR PHE
SEQRES 23 A 310 GLN GLN ALA GLY ASN GLY ILE PHE ALA ARG GLN ALA LEU
SEQRES 24 A 310 LEU ALA LEU VAL LEU ASN ARG ASP LEU VAL LEU
SEQRES 1 B 153 MET THR HIS ASP ASN LYS LEU GLN VAL GLU ALA ILE LYS
SEQRES 2 B 153 ARG GLY THR VAL ILE ASP HIS ILE PRO ALA GLN ILE GLY
SEQRES 3 B 153 PHE LYS LEU LEU SER LEU PHE LYS LEU THR GLU THR ASP
SEQRES 4 B 153 GLN ARG ILE THR ILE GLY LEU ASN LEU PRO SER GLY GLU
SEQRES 5 B 153 MET GLY ARG LYS ASP LEU ILE LYS ILE GLU ASN THR PHE
SEQRES 6 B 153 LEU SER GLU ASP GLN VAL ASP GLN LEU ALA LEU TYR ALA
SEQRES 7 B 153 PRO GLN ALA THR VAL ASN ARG ILE ASP ASN TYR GLU VAL
SEQRES 8 B 153 VAL GLY LYS SER ARG PRO SER LEU PRO GLU ARG ILE ASP
SEQRES 9 B 153 ASN VAL LEU VAL CYS PRO ASN SER ASN CYS ILE SER HIS
SEQRES 10 B 153 ALA GLU PRO VAL SER SER SER PHE ALA VAL ARG LYS ARG
SEQRES 11 B 153 ALA ASN ASP ILE ALA LEU LYS CYS LYS TYR CYS GLU LYS
SEQRES 12 B 153 GLU PHE SER HIS ASN VAL VAL LEU ALA ASN
SEQRES 1 C 310 ALA ASN PRO LEU TYR GLN LYS HIS ILE ILE SER ILE ASN
SEQRES 2 C 310 ASP LEU SER ARG ASP ASP LEU ASN LEU VAL LEU ALA THR
SEQRES 3 C 310 ALA ALA LYS LEU LYS ALA ASN PRO GLN PRO GLU LEU LEU
SEQRES 4 C 310 LYS HIS LYS VAL ILE ALA SER CYS PHE PHE GLU ALA SER
SEQRES 5 C 310 THR ARG THR ARG LEU SER PHE GLU THR SER MET HIS ARG
SEQRES 6 C 310 LEU GLY ALA SER VAL VAL GLY PHE SER ASP SER ALA ASN
SEQRES 7 C 310 THR SER LEU GLY LYS LYS GLY GLU THR LEU ALA ASP THR
SEQRES 8 C 310 ILE SER VAL ILE SER THR TYR VAL ASP ALA ILE VAL MET
SEQRES 9 C 310 ARG HIS PRO GLN GLU GLY ALA ALA ARG LEU ALA THR GLU
SEQRES 10 C 310 PHE SER GLY ASN VAL PRO VAL LEU ASN ALA GLY ASP GLY
SEQRES 11 C 310 SER ASN GLN HIS PRO THR GLN THR LEU LEU ASP LEU PHE
SEQRES 12 C 310 THR ILE GLN GLU THR GLN GLY ARG LEU ASP ASN LEU HIS
SEQRES 13 C 310 VAL ALA MET VAL GLY ASP LEU LYS TYR GLY ARG THR VAL
SEQRES 14 C 310 HIS SER LEU THR GLN ALA LEU ALA LYS PHE ASP GLY ASN
SEQRES 15 C 310 ARG PHE TYR PHE ILE ALA PRO ASP ALA LEU ALA MET PRO
SEQRES 16 C 310 GLN TYR ILE LEU ASP MET LEU ASP GLU LYS GLY ILE ALA
SEQRES 17 C 310 TRP SER LEU HIS SER SER ILE GLU GLU VAL MET ALA GLU
SEQRES 18 C 310 VAL ASP ILE LEU TYR MET THR ARG VAL GLN LYS GLU ARG
SEQRES 19 C 310 LEU ASP PRO SER GLU TYR ALA ASN VAL LYS ALA GLN PHE
SEQRES 20 C 310 VAL LEU ARG ALA SER ASP LEU HIS ASN ALA LYS ALA ASN
SEQRES 21 C 310 MET LYS VAL LEU HIS PRO LEU PRO ARG VAL ASP GLU ILE
SEQRES 22 C 310 ALA THR ASP VAL ASP LYS THR PRO HIS ALA TRP TYR PHE
SEQRES 23 C 310 GLN GLN ALA GLY ASN GLY ILE PHE ALA ARG GLN ALA LEU
SEQRES 24 C 310 LEU ALA LEU VAL LEU ASN ARG ASP LEU VAL LEU
SEQRES 1 D 153 MET THR HIS ASP ASN LYS LEU GLN VAL GLU ALA ILE LYS
SEQRES 2 D 153 ARG GLY THR VAL ILE ASP HIS ILE PRO ALA GLN ILE GLY
SEQRES 3 D 153 PHE LYS LEU LEU SER LEU PHE LYS LEU THR GLU THR ASP
SEQRES 4 D 153 GLN ARG ILE THR ILE GLY LEU ASN LEU PRO SER GLY GLU
SEQRES 5 D 153 MET GLY ARG LYS ASP LEU ILE LYS ILE GLU ASN THR PHE
SEQRES 6 D 153 LEU SER GLU ASP GLN VAL ASP GLN LEU ALA LEU TYR ALA
SEQRES 7 D 153 PRO GLN ALA THR VAL ASN ARG ILE ASP ASN TYR GLU VAL
SEQRES 8 D 153 VAL GLY LYS SER ARG PRO SER LEU PRO GLU ARG ILE ASP
SEQRES 9 D 153 ASN VAL LEU VAL CYS PRO ASN SER ASN CYS ILE SER HIS
SEQRES 10 D 153 ALA GLU PRO VAL SER SER SER PHE ALA VAL ARG LYS ARG
SEQRES 11 D 153 ALA ASN ASP ILE ALA LEU LYS CYS LYS TYR CYS GLU LYS
SEQRES 12 D 153 GLU PHE SER HIS ASN VAL VAL LEU ALA ASN
HET NA A 311 1
HET CP A 312 8
HET CP A 313 8
HET ZN B 154 1
HET CTP B 155 29
HET CP C 311 8
HET CP C 312 8
HET ZN D 154 1
HET CTP D 155 29
HETNAM NA SODIUM ION
HETNAM CP PHOSPHORIC ACID MONO(FORMAMIDE)ESTER
HETNAM ZN ZINC ION
HETNAM CTP CYTIDINE-5'-TRIPHOSPHATE
FORMUL 5 NA NA 1+
FORMUL 6 CP 4(C H4 N O5 P)
FORMUL 8 ZN 2(ZN 2+)
FORMUL 9 CTP 2(C9 H16 N3 O14 P3)
FORMUL 14 HOH *381(H2 O)
HELIX 1 1 SER A 11 LEU A 15 5 5
HELIX 2 2 SER A 16 ASN A 33 1 18
HELIX 3 3 THR A 53 LEU A 66 1 14
HELIX 4 4 THR A 79 LYS A 84 1 6
HELIX 5 5 THR A 87 SER A 96 1 10
HELIX 6 6 GLY A 110 GLU A 117 1 8
HELIX 7 7 HIS A 134 GLY A 150 1 17
HELIX 8 8 GLY A 166 ALA A 177 1 12
HELIX 9 9 PRO A 189 ALA A 193 5 5
HELIX 10 10 PRO A 195 LYS A 205 1 11
HELIX 11 11 VAL A 218 VAL A 222 5 5
HELIX 12 12 GLN A 231 LEU A 235 5 5
HELIX 13 13 ASP A 236 LYS A 244 1 9
HELIX 14 14 ALA A 245 PHE A 247 5 3
HELIX 15 15 ARG A 250 HIS A 255 5 6
HELIX 16 16 ALA A 274 ASP A 278 5 5
HELIX 17 17 TRP A 284 ASN A 291 1 8
HELIX 18 18 GLY A 292 ASN A 305 1 14
HELIX 19 19 ILE B 25 PHE B 33 1 9
HELIX 20 20 SER B 67 GLN B 73 1 7
HELIX 21 21 HIS B 147 ALA B 152 1 6
HELIX 22 22 SER C 11 LEU C 15 5 5
HELIX 23 23 SER C 16 ASN C 33 1 18
HELIX 24 24 THR C 53 LEU C 66 1 14
HELIX 25 25 THR C 87 SER C 96 1 10
HELIX 26 26 GLY C 110 GLU C 117 1 8
HELIX 27 27 HIS C 134 GLY C 150 1 17
HELIX 28 28 GLY C 166 ALA C 177 1 12
HELIX 29 29 PRO C 189 ALA C 193 5 5
HELIX 30 30 PRO C 195 LYS C 205 1 11
HELIX 31 31 SER C 214 MET C 219 1 6
HELIX 32 32 ALA C 220 VAL C 222 5 3
HELIX 33 33 GLN C 231 LEU C 235 5 5
HELIX 34 34 ASP C 236 LYS C 244 1 9
HELIX 35 35 ALA C 245 PHE C 247 5 3
HELIX 36 36 ARG C 250 ALA C 257 5 8
HELIX 37 37 ALA C 274 ASP C 278 5 5
HELIX 38 38 TRP C 284 ASN C 305 1 22
HELIX 39 39 ILE D 25 PHE D 33 1 9
HELIX 40 40 SER D 67 GLN D 73 1 7
HELIX 41 41 HIS D 147 LEU D 151 1 5
SHEET 1 A 4 SER A 69 PHE A 73 0
SHEET 2 A 4 VAL A 43 PHE A 48 1 N SER A 46 O VAL A 71
SHEET 3 A 4 ALA A 101 HIS A 106 1 O VAL A 103 N CYS A 47
SHEET 4 A 4 VAL A 124 ASP A 129 1 O ALA A 127 N MET A 104
SHEET 1 B 5 TRP A 209 LEU A 211 0
SHEET 2 B 5 ARG A 183 ILE A 187 1 N PHE A 186 O SER A 210
SHEET 3 B 5 HIS A 156 VAL A 160 1 N MET A 159 O ILE A 187
SHEET 4 B 5 ILE A 224 MET A 227 1 O TYR A 226 N ALA A 158
SHEET 5 B 5 LYS A 262 LEU A 264 1 O LEU A 264 N MET A 227
SHEET 1 C 9 LYS B 94 SER B 95 0
SHEET 2 C 9 THR B 82 ILE B 86 -1 N VAL B 83 O SER B 95
SHEET 3 C 9 GLY B 15 PRO B 22 -1 N VAL B 17 O ASN B 84
SHEET 4 C 9 ARG B 55 GLU B 62 -1 O ILE B 59 N ILE B 18
SHEET 5 C 9 ILE B 42 PRO B 49 -1 N GLY B 45 O LEU B 58
SHEET 6 C 9 ILE D 42 PRO D 49 -1 O ILE D 44 N ILE B 44
SHEET 7 C 9 ARG D 55 GLU D 62 -1 O LYS D 56 N LEU D 48
SHEET 8 C 9 GLY D 15 PRO D 22 -1 N THR D 16 O ILE D 61
SHEET 9 C 9 THR D 82 ASN D 84 -1 O THR D 82 N ASP D 19
SHEET 1 D 4 ARG B 102 ASP B 104 0
SHEET 2 D 4 SER B 124 ARG B 130 -1 O PHE B 125 N ILE B 103
SHEET 3 D 4 ASP B 133 CYS B 138 -1 O LYS B 137 N ALA B 126
SHEET 4 D 4 GLU B 144 SER B 146 -1 O PHE B 145 N LEU B 136
SHEET 1 E 4 SER C 69 PHE C 73 0
SHEET 2 E 4 VAL C 43 PHE C 48 1 N ILE C 44 O SER C 69
SHEET 3 E 4 ALA C 101 HIS C 106 1 O VAL C 103 N CYS C 47
SHEET 4 E 4 VAL C 124 ASP C 129 1 O LEU C 125 N ILE C 102
SHEET 1 F 5 ALA C 208 HIS C 212 0
SHEET 2 F 5 ARG C 183 ILE C 187 1 N PHE C 184 O ALA C 208
SHEET 3 F 5 HIS C 156 VAL C 160 1 N VAL C 157 O ARG C 183
SHEET 4 F 5 ILE C 224 MET C 227 1 O TYR C 226 N ALA C 158
SHEET 5 F 5 LYS C 262 LEU C 264 1 O LEU C 264 N MET C 227
SHEET 1 G 4 ARG D 102 ASP D 104 0
SHEET 2 G 4 SER D 124 LYS D 129 -1 O PHE D 125 N ILE D 103
SHEET 3 G 4 ILE D 134 CYS D 138 -1 O ALA D 135 N ARG D 128
SHEET 4 G 4 GLU D 144 SER D 146 -1 O PHE D 145 N LEU D 136
LINK NA NA A 311 O HOH A 323 1555 1555 2.99
LINK NA NA A 311 O HOH A 379 1555 1555 2.20
LINK NA NA A 311 O HOH A 379 1555 3665 2.28
LINK SG CYS B 109 ZN ZN B 154 1555 1555 2.35
LINK SG CYS B 114 ZN ZN B 154 1555 1555 2.33
LINK SG CYS B 138 ZN ZN B 154 1555 1555 2.33
LINK SG CYS B 141 ZN ZN B 154 1555 1555 2.35
LINK SG CYS D 109 ZN ZN D 154 1555 1555 2.35
LINK SG CYS D 114 ZN ZN D 154 1555 1555 2.35
LINK SG CYS D 138 ZN ZN D 154 1555 1555 2.38
LINK SG CYS D 141 ZN ZN D 154 1555 1555 2.37
CISPEP 1 LEU A 267 PRO A 268 0 -0.16
CISPEP 2 LEU C 267 PRO C 268 0 0.29
SITE 1 AC1 4 CYS B 109 CYS B 114 CYS B 138 CYS B 141
SITE 1 AC2 4 CYS D 109 CYS D 114 CYS D 138 CYS D 141
SITE 1 AC3 2 HOH A 323 HOH A 379
SITE 1 AC4 10 ALA B 11 ILE B 12 ASP B 19 HIS B 20
SITE 2 AC4 10 LYS B 60 ASN B 84 ILE B 86 TYR B 89
SITE 3 AC4 10 VAL B 91 LYS B 94
SITE 1 AC5 10 ALA D 11 ILE D 12 VAL D 17 ASP D 19
SITE 2 AC5 10 HIS D 20 LYS D 60 ASN D 84 TYR D 89
SITE 3 AC5 10 VAL D 91 LYS D 94
SITE 1 AC6 12 SER A 52 THR A 53 ARG A 54 THR A 55
SITE 2 AC6 12 SER A 80 ARG A 105 HIS A 134 GLN A 137
SITE 3 AC6 12 PRO A 266 LEU A 267 HOH A 336 HOH A 457
SITE 1 AC7 12 SER C 52 THR C 53 ARG C 54 THR C 55
SITE 2 AC7 12 THR C 79 ARG C 105 HIS C 134 GLN C 137
SITE 3 AC7 12 PRO C 266 LEU C 267 HOH C 325 HOH C 337
SITE 1 AC8 7 TYR A 165 GLY A 166 ARG A 167 THR A 168
SITE 2 AC8 7 GLN A 231 HOH A 350 HOH A 409
SITE 1 AC9 4 LYS C 83 GLY C 166 ARG C 167 THR C 168
CRYST1 121.442 121.442 142.547 90.00 90.00 120.00 P 3 2 1 12
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 0.008234 0.004754 0.000000 0.00000
SCALE2 0.000000 0.009508 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007015 0.00000
(ATOM LINES ARE NOT SHOWN.)
END