HEADER TRANSFERASE 09-JUL-97 1ECC
TITLE ESCHERICHIA COLI GLUTAMINE PHOSPHORIBOSYLPYROPHOSPHATE (PRPP)
TITLE 2 AMIDOTRANSFERASE COMPLEXED WITH MN-CPRPP AND 5-OXO-NORLEUCINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAMINE PHOSPHORIBOSYLPYROPHOSPHATE AMIDOTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.4.2.14;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: PURF;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PT7F1
KEYWDS TRANSFERASE, GLUTAMINE AMIDOTRANSFERASE, PURINE BIOSYNTHESIS,
KEYWDS 2 GLYCOSYLTRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.M.KRAHN,J.L.SMITH
REVDAT 3 09-AUG-23 1ECC 1 REMARK LINK
REVDAT 2 24-FEB-09 1ECC 1 VERSN
REVDAT 1 15-APR-98 1ECC 0
JRNL AUTH J.M.KRAHN,J.H.KIM,M.R.BURNS,R.J.PARRY,H.ZALKIN,J.L.SMITH
JRNL TITL COUPLED FORMATION OF AN AMIDOTRANSFERASE INTERDOMAIN AMMONIA
JRNL TITL 2 CHANNEL AND A PHOSPHORIBOSYLTRANSFERASE ACTIVE SITE.
JRNL REF BIOCHEMISTRY V. 36 11061 1997
JRNL REFN ISSN 0006-2960
JRNL PMID 9333323
JRNL DOI 10.1021/BI9714114
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.8
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1000000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 88.3
REMARK 3 NUMBER OF REFLECTIONS : 35343
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM, FROM ENTIRE DATA SET
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.265
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1679
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 : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.49
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2517
REMARK 3 BIN R VALUE (WORKING SET) : 0.2950
REMARK 3 BIN FREE R VALUE : 0.3500
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 127
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 : 7732
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 69
REMARK 3 SOLVENT ATOMS : 291
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 42.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.46000
REMARK 3 B22 (A**2) : 1.46000
REMARK 3 B33 (A**2) : -2.92000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.27
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) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 1.970
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.470
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) : 1.500 ; 1.574
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.000 ; 2.636
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.000 ; 2.420
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.500 ; 3.780
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 : PARAM11X.DNA
REMARK 3 PARAMETER FILE 3 : PARAM11.WAT
REMARK 3 PARAMETER FILE 4 : PRPP.PAR
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TOPH11.DNA
REMARK 3 TOPOLOGY FILE 3 : TOPH11.WAT
REMARK 3 TOPOLOGY FILE 4 : CPRPP.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: ADDITIONAL TOPOLOGY/PARAMETER FILES FOR
REMARK 3 THE CYS/ONL LINKAGE WERE USED, WHICH HAVE A NOMENCLATURE
REMARK 3 DIFFERENT FROM THE ONL RESIDUE IN THIS ENTRY.
REMARK 4
REMARK 4 1ECC 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_1000173002.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-AUG-96
REMARK 200 TEMPERATURE (KELVIN) : 110.0
REMARK 200 PH : 5.8
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 RUH2R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : MSC DOUBLE MIRROR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL (DENZO)
REMARK 200 DATA SCALING SOFTWARE : HKL, SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27331
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.3
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.03600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 60.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.17200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR 3.8
REMARK 200 STARTING MODEL: PDB ENTRY 1ECF
REMARK 200
REMARK 200 REMARK: A SINGLE GAT DOMAIN (249 RESIDUES) WAS USED AS THE PROBE
REMARK 200 MODEL DUE TO ALLOSTERIC DIFFERENCES BETWEEN THIS STRUCTURE AND
REMARK 200 THAT OF 1ECF.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.42MM CPRPP, 25MM MNCL2, 40MM BIS
REMARK 280 -TRIS PH 5.8, 3.2% 2-PROPANOL, 7.5% PEG-3350
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 154.40000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 39.10000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 39.10000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 231.60000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 39.10000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 39.10000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 77.20000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 39.10000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 39.10000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 231.60000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 39.10000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 39.10000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 77.20000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 154.40000
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: TETRAMERIC
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 350 BIOMT1 2 0.000000 -1.000000 0.000000 78.20000
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 78.20000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 154.40000
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 ASN A 493
REMARK 465 GLU A 494
REMARK 465 VAL A 495
REMARK 465 GLU A 496
REMARK 465 ASN A 497
REMARK 465 LEU A 498
REMARK 465 GLU A 499
REMARK 465 MET A 500
REMARK 465 HIS A 501
REMARK 465 ASN A 502
REMARK 465 GLU A 503
REMARK 465 GLY A 504
REMARK 465 ASN B 493
REMARK 465 GLU B 494
REMARK 465 VAL B 495
REMARK 465 GLU B 496
REMARK 465 ASN B 497
REMARK 465 LEU B 498
REMARK 465 GLU B 499
REMARK 465 MET B 500
REMARK 465 HIS B 501
REMARK 465 ASN B 502
REMARK 465 GLU B 503
REMARK 465 GLY B 504
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 TYR A 94 -30.01 65.04
REMARK 500 PHE A 115 -77.25 -80.68
REMARK 500 HIS A 144 26.87 -68.82
REMARK 500 TYR A 145 124.81 -6.52
REMARK 500 HIS A 176 -60.55 -120.37
REMARK 500 PRO A 184 -9.99 -52.61
REMARK 500 ASP A 198 -153.55 -153.11
REMARK 500 ASN A 200 -49.11 -141.15
REMARK 500 LEU A 221 -76.08 -102.09
REMARK 500 TYR A 258 -49.49 -148.68
REMARK 500 GLU A 291 -47.81 -28.22
REMARK 500 ASP A 292 23.13 -73.99
REMARK 500 VAL A 370 -71.09 -122.87
REMARK 500 ALA A 385 3.46 -69.65
REMARK 500 ASN A 450 80.10 -157.14
REMARK 500 PRO B 11 121.78 -39.94
REMARK 500 TYR B 94 -35.38 79.24
REMARK 500 ASP B 140 4.43 -68.88
REMARK 500 HIS B 176 -61.40 -125.88
REMARK 500 LEU B 190 120.98 -170.66
REMARK 500 GLU B 199 92.32 -42.83
REMARK 500 ASN B 200 -18.22 118.76
REMARK 500 ARG B 222 176.65 173.85
REMARK 500 ARG B 241 139.05 -177.44
REMARK 500 TYR B 258 -41.30 -137.90
REMARK 500 LEU B 293 137.94 -32.94
REMARK 500 VAL B 370 -84.54 -123.36
REMARK 500 ASN B 450 89.21 -152.87
REMARK 500 CYS B 458 43.84 -144.61
REMARK 500 THR B 467 0.50 -68.91
REMARK 500 LYS B 468 -63.20 68.16
REMARK 500 ASP B 469 -12.90 -40.82
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 TYR A 145 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 A WELL ORDERED MN++ EXISTS AT A LATTICE CONTACT. THIS
REMARK 600 METAL IS LIGATED TO GLU B 449, ASP B 471, AND WATERS
REMARK 600 HOH A 507, HOH A 508, HOH B 507, AND HOH B 508.
REMARK 600 LIGATION TO ASP B 471 IS TO A SYMMETRY-EQUIVALENT RESIDUE.
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 MN A 506 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PCP A 505 O1
REMARK 620 2 PCP A 505 O2 77.4
REMARK 620 3 PCP A 505 O3 85.5 76.3
REMARK 620 4 PCP A 505 O1B 91.5 94.5 170.8
REMARK 620 5 HOH A2378 O 170.8 94.7 97.3 84.4
REMARK 620 6 HOH A2379 O 87.7 159.0 88.0 100.7 101.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B2449 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 449 OE2
REMARK 620 2 ASP B 471 OD1 123.4
REMARK 620 3 HOH B2543 O 80.1 61.6
REMARK 620 4 HOH B2597 O 86.6 107.4 62.4
REMARK 620 5 HOH B2598 O 88.0 78.9 120.4 173.3
REMARK 620 6 HOH B2599 O 149.8 62.2 78.3 64.7 121.3
REMARK 620 7 HOH B2600 O 96.0 137.6 150.4 88.2 88.5 92.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 506 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PCP B 505 O1
REMARK 620 2 PCP B 505 O2 73.6
REMARK 620 3 PCP B 505 O3 81.3 77.3
REMARK 620 4 PCP B 505 O1B 86.5 94.2 166.7
REMARK 620 5 HOH B2451 O 168.5 98.2 105.1 86.2
REMARK 620 6 HOH B2452 O 96.2 168.3 95.7 90.8 92.7
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: NTA
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NTN AMIDOTRANSFERASE ACTIVE SITE. THE ACTIVE
REMARK 800 SITE IN THIS STRUCTURE CONTAINS THE PRODUCT OF COVALENT
REMARK 800 INACTIVATION BY THE GLUTAMINE ANALOGUE DON.
REMARK 800
REMARK 800 SITE_IDENTIFIER: PRT
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: PHOSPHORIBOSYL TRANSFERASE ACTIVE SITE. THE
REMARK 800 ACTIVE SITE IN THIS STRUCTURE CONTAINS CPRPP, A CARBOCYCLIC PRPP
REMARK 800 ANALOGUE. ASP 366 AND ASP 367 FUNCTION AS METAL LIGANDS, AND ARE
REMARK 800 THE HALLMARK OF PRTASE ENZYMES. MG++ IS THE PRIMARY BIOLOGICALLY
REMARK 800 FUNCTIONAL METAL ION. MN++ IS PRESENT IN THIS STRUCTURE, AND
REMARK 800 DEMONSTRATES A COORDINATION GEOMETRY VERY SIMILAR TO TYPICAL MG++
REMARK 800 COORDINATIONS.
REMARK 800
REMARK 800 SITE_IDENTIFIER: NTB
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NTN AMIDOTRANSFERASE ACTIVE SITE. THE ACTIVE
REMARK 800 SITE IN THIS STRUCTURE CONTAINS THE PRODUCT OF COVALENT
REMARK 800 INACTIVATION BY THE GLUTAMINE ANALOGUE DON.
REMARK 800
REMARK 800 SITE_IDENTIFIER: PRB
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: PHOSPHORIBOSYL TRANSFERASE ACTIVE SITE. THE
REMARK 800 ACTIVE SITE IN THIS STRUCTURE CONTAINS CPRPP, A CARBOCYCLIC PRPP
REMARK 800 ANALOGUE. ASP 366 AND ASP 367 FUNCTION AS METAL LIGANDS, AND ARE
REMARK 800 THE HALLMARK OF PRTASE ENZYMES. MG++ IS THE PRIMARY BIOLOGICALLY
REMARK 800 FUNCTIONAL METAL ION. MN++ IS PRESENT IN THIS STRUCTURE, AND
REMARK 800 DEMONSTRATES A COORDINATION GEOMETRY VERY SIMILAR TO TYPICAL MG++
REMARK 800 COORDINATIONS.
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 1449
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 2376
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 2449
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ONL A 2377
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PCP A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ONL B 2450
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PCP B 505
DBREF 1ECC A 1 504 UNP P00496 PUR1_ECOLI 1 504
DBREF 1ECC B 1 504 UNP P00496 PUR1_ECOLI 1 504
SEQRES 1 A 504 CYS GLY ILE VAL GLY ILE ALA GLY VAL MET PRO VAL ASN
SEQRES 2 A 504 GLN SER ILE TYR ASP ALA LEU THR VAL LEU GLN HIS ARG
SEQRES 3 A 504 GLY GLN ASP ALA ALA GLY ILE ILE THR ILE ASP ALA ASN
SEQRES 4 A 504 ASN CYS PHE ARG LEU ARG LYS ALA ASN GLY LEU VAL SER
SEQRES 5 A 504 ASP VAL PHE GLU ALA ARG HIS MET GLN ARG LEU GLN GLY
SEQRES 6 A 504 ASN MET GLY ILE GLY HIS VAL ARG TYR PRO THR ALA GLY
SEQRES 7 A 504 SER SER SER ALA SER GLU ALA GLN PRO PHE TYR VAL ASN
SEQRES 8 A 504 SER PRO TYR GLY ILE THR LEU ALA HIS ASN GLY ASN LEU
SEQRES 9 A 504 THR ASN ALA HIS GLU LEU ARG LYS LYS LEU PHE GLU GLU
SEQRES 10 A 504 LYS ARG ARG HIS ILE ASN THR THR SER ASP SER GLU ILE
SEQRES 11 A 504 LEU LEU ASN ILE PHE ALA SER GLU LEU ASP ASN PHE ARG
SEQRES 12 A 504 HIS TYR PRO LEU GLU ALA ASP ASN ILE PHE ALA ALA ILE
SEQRES 13 A 504 ALA ALA THR ASN ARG LEU ILE ARG GLY ALA TYR ALA CYS
SEQRES 14 A 504 VAL ALA MET ILE ILE GLY HIS GLY MET VAL ALA PHE ARG
SEQRES 15 A 504 ASP PRO ASN GLY ILE ARG PRO LEU VAL LEU GLY LYS ARG
SEQRES 16 A 504 ASP ILE ASP GLU ASN ARG THR GLU TYR MET VAL ALA SER
SEQRES 17 A 504 GLU SER VAL ALA LEU ASP THR LEU GLY PHE ASP PHE LEU
SEQRES 18 A 504 ARG ASP VAL ALA PRO GLY GLU ALA ILE TYR ILE THR GLU
SEQRES 19 A 504 GLU GLY GLN LEU PHE THR ARG GLN CYS ALA ASP ASN PRO
SEQRES 20 A 504 VAL SER ASN PRO CYS LEU PHE GLU TYR VAL TYR PHE ALA
SEQRES 21 A 504 ARG PRO ASP SER PHE ILE ASP LYS ILE SER VAL TYR SER
SEQRES 22 A 504 ALA ARG VAL ASN MET GLY THR LYS LEU GLY GLU LYS ILE
SEQRES 23 A 504 ALA ARG GLU TRP GLU ASP LEU ASP ILE ASP VAL VAL ILE
SEQRES 24 A 504 PRO ILE PRO GLU THR SER CYS ASP ILE ALA LEU GLU ILE
SEQRES 25 A 504 ALA ARG ILE LEU GLY LYS PRO TYR ARG GLN GLY PHE VAL
SEQRES 26 A 504 LYS ASN ARG TYR VAL GLY ARG THR PHE ILE MET PRO GLY
SEQRES 27 A 504 GLN GLN LEU ARG ARG LYS SER VAL ARG ARG LYS LEU ASN
SEQRES 28 A 504 ALA ASN ARG ALA GLU PHE ARG ASP LYS ASN VAL LEU LEU
SEQRES 29 A 504 VAL ASP ASP SER ILE VAL ARG GLY THR THR SER GLU GLN
SEQRES 30 A 504 ILE ILE GLU MET ALA ARG GLU ALA GLY ALA LYS LYS VAL
SEQRES 31 A 504 TYR LEU ALA SER ALA ALA PRO GLU ILE ARG PHE PRO ASN
SEQRES 32 A 504 VAL TYR GLY ILE ASP MET PRO SER ALA THR GLU LEU ILE
SEQRES 33 A 504 ALA HIS GLY ARG GLU VAL ASP GLU ILE ARG GLN ILE ILE
SEQRES 34 A 504 GLY ALA ASP GLY LEU ILE PHE GLN ASP LEU ASN ASP LEU
SEQRES 35 A 504 ILE ASP ALA VAL ARG ALA GLU ASN PRO ASP ILE GLN GLN
SEQRES 36 A 504 PHE GLU CYS SER VAL PHE ASN GLY VAL TYR VAL THR LYS
SEQRES 37 A 504 ASP VAL ASP GLN GLY TYR LEU ASP PHE LEU ASP THR LEU
SEQRES 38 A 504 ARG ASN ASP ASP ALA LYS ALA VAL GLN ARG GLN ASN GLU
SEQRES 39 A 504 VAL GLU ASN LEU GLU MET HIS ASN GLU GLY
SEQRES 1 B 504 CYS GLY ILE VAL GLY ILE ALA GLY VAL MET PRO VAL ASN
SEQRES 2 B 504 GLN SER ILE TYR ASP ALA LEU THR VAL LEU GLN HIS ARG
SEQRES 3 B 504 GLY GLN ASP ALA ALA GLY ILE ILE THR ILE ASP ALA ASN
SEQRES 4 B 504 ASN CYS PHE ARG LEU ARG LYS ALA ASN GLY LEU VAL SER
SEQRES 5 B 504 ASP VAL PHE GLU ALA ARG HIS MET GLN ARG LEU GLN GLY
SEQRES 6 B 504 ASN MET GLY ILE GLY HIS VAL ARG TYR PRO THR ALA GLY
SEQRES 7 B 504 SER SER SER ALA SER GLU ALA GLN PRO PHE TYR VAL ASN
SEQRES 8 B 504 SER PRO TYR GLY ILE THR LEU ALA HIS ASN GLY ASN LEU
SEQRES 9 B 504 THR ASN ALA HIS GLU LEU ARG LYS LYS LEU PHE GLU GLU
SEQRES 10 B 504 LYS ARG ARG HIS ILE ASN THR THR SER ASP SER GLU ILE
SEQRES 11 B 504 LEU LEU ASN ILE PHE ALA SER GLU LEU ASP ASN PHE ARG
SEQRES 12 B 504 HIS TYR PRO LEU GLU ALA ASP ASN ILE PHE ALA ALA ILE
SEQRES 13 B 504 ALA ALA THR ASN ARG LEU ILE ARG GLY ALA TYR ALA CYS
SEQRES 14 B 504 VAL ALA MET ILE ILE GLY HIS GLY MET VAL ALA PHE ARG
SEQRES 15 B 504 ASP PRO ASN GLY ILE ARG PRO LEU VAL LEU GLY LYS ARG
SEQRES 16 B 504 ASP ILE ASP GLU ASN ARG THR GLU TYR MET VAL ALA SER
SEQRES 17 B 504 GLU SER VAL ALA LEU ASP THR LEU GLY PHE ASP PHE LEU
SEQRES 18 B 504 ARG ASP VAL ALA PRO GLY GLU ALA ILE TYR ILE THR GLU
SEQRES 19 B 504 GLU GLY GLN LEU PHE THR ARG GLN CYS ALA ASP ASN PRO
SEQRES 20 B 504 VAL SER ASN PRO CYS LEU PHE GLU TYR VAL TYR PHE ALA
SEQRES 21 B 504 ARG PRO ASP SER PHE ILE ASP LYS ILE SER VAL TYR SER
SEQRES 22 B 504 ALA ARG VAL ASN MET GLY THR LYS LEU GLY GLU LYS ILE
SEQRES 23 B 504 ALA ARG GLU TRP GLU ASP LEU ASP ILE ASP VAL VAL ILE
SEQRES 24 B 504 PRO ILE PRO GLU THR SER CYS ASP ILE ALA LEU GLU ILE
SEQRES 25 B 504 ALA ARG ILE LEU GLY LYS PRO TYR ARG GLN GLY PHE VAL
SEQRES 26 B 504 LYS ASN ARG TYR VAL GLY ARG THR PHE ILE MET PRO GLY
SEQRES 27 B 504 GLN GLN LEU ARG ARG LYS SER VAL ARG ARG LYS LEU ASN
SEQRES 28 B 504 ALA ASN ARG ALA GLU PHE ARG ASP LYS ASN VAL LEU LEU
SEQRES 29 B 504 VAL ASP ASP SER ILE VAL ARG GLY THR THR SER GLU GLN
SEQRES 30 B 504 ILE ILE GLU MET ALA ARG GLU ALA GLY ALA LYS LYS VAL
SEQRES 31 B 504 TYR LEU ALA SER ALA ALA PRO GLU ILE ARG PHE PRO ASN
SEQRES 32 B 504 VAL TYR GLY ILE ASP MET PRO SER ALA THR GLU LEU ILE
SEQRES 33 B 504 ALA HIS GLY ARG GLU VAL ASP GLU ILE ARG GLN ILE ILE
SEQRES 34 B 504 GLY ALA ASP GLY LEU ILE PHE GLN ASP LEU ASN ASP LEU
SEQRES 35 B 504 ILE ASP ALA VAL ARG ALA GLU ASN PRO ASP ILE GLN GLN
SEQRES 36 B 504 PHE GLU CYS SER VAL PHE ASN GLY VAL TYR VAL THR LYS
SEQRES 37 B 504 ASP VAL ASP GLN GLY TYR LEU ASP PHE LEU ASP THR LEU
SEQRES 38 B 504 ARG ASN ASP ASP ALA LYS ALA VAL GLN ARG GLN ASN GLU
SEQRES 39 B 504 VAL GLU ASN LEU GLU MET HIS ASN GLU GLY
HET MN A 506 1
HET MN A2376 1
HET ONL A2377 10
HET PCP A 505 22
HET MN B 506 1
HET MN B1449 1
HET MN B2449 1
HET ONL B2450 10
HET PCP B 505 22
HETNAM MN MANGANESE (II) ION
HETNAM ONL 5-OXO-L-NORLEUCINE
HETNAM PCP 1-ALPHA-PYROPHOSPHORYL-2-ALPHA,3-ALPHA-DIHYDROXY-4-
HETNAM 2 PCP BETA-CYCLOPENTANE-METHANOL-5-PHOSPHATE
HETSYN PCP CARBOXYLIC PRPP; CPRPP
FORMUL 3 MN 5(MN 2+)
FORMUL 5 ONL 2(C6 H11 N O3)
FORMUL 6 PCP 2(C6 H15 O13 P3)
FORMUL 12 HOH *291(H2 O)
HELIX 1 1 ASN A 13 VAL A 22 1 10
HELIX 2 2 GLN A 24 ARG A 26 5 3
HELIX 3 3 VAL A 51 VAL A 54 1 4
HELIX 4 4 ALA A 57 ARG A 62 1 6
HELIX 5 5 ALA A 82 GLU A 84 5 3
HELIX 6 6 ALA A 107 GLU A 116 1 10
HELIX 7 7 ASP A 127 ASN A 141 1 15
HELIX 8 8 ALA A 149 LEU A 162 1 14
HELIX 9 9 SER A 210 LEU A 216 5 7
HELIX 10 10 LEU A 253 VAL A 257 1 5
HELIX 11 11 VAL A 271 GLU A 289 1 19
HELIX 12 12 CYS A 306 ILE A 315 1 10
HELIX 13 13 GLN A 339 LYS A 349 1 11
HELIX 14 14 ARG A 354 GLU A 356 5 3
HELIX 15 15 THR A 373 GLU A 384 1 12
HELIX 16 16 ALA A 412 GLU A 414 5 3
HELIX 17 17 VAL A 422 ILE A 429 1 8
HELIX 18 18 LEU A 439 GLU A 449 1 11
HELIX 19 19 SER A 459 ASN A 462 1 4
HELIX 20 20 GLN A 472 ARG A 482 1 11
HELIX 21 21 ASP A 484 GLN A 490 1 7
HELIX 22 22 ASN B 13 VAL B 22 1 10
HELIX 23 23 GLN B 24 ARG B 26 5 3
HELIX 24 24 VAL B 51 VAL B 54 1 4
HELIX 25 25 ALA B 57 ARG B 62 1 6
HELIX 26 26 ALA B 82 GLU B 84 5 3
HELIX 27 27 ALA B 107 GLU B 116 1 10
HELIX 28 28 ASP B 127 ASN B 141 1 15
HELIX 29 29 ALA B 149 LEU B 162 1 14
HELIX 30 30 SER B 210 LEU B 216 1 7
HELIX 31 31 LEU B 253 VAL B 257 1 5
HELIX 32 32 VAL B 271 GLU B 289 1 19
HELIX 33 33 CYS B 306 LEU B 316 1 11
HELIX 34 34 GLN B 339 LYS B 349 1 11
HELIX 35 35 ARG B 354 GLU B 356 5 3
HELIX 36 36 THR B 373 GLU B 384 1 12
HELIX 37 37 ALA B 412 GLU B 414 5 3
HELIX 38 38 VAL B 422 ILE B 429 1 8
HELIX 39 39 LEU B 439 GLU B 449 1 11
HELIX 40 40 SER B 459 ASN B 462 1 4
HELIX 41 41 GLN B 472 ARG B 482 1 11
HELIX 42 42 ASP B 484 GLN B 490 1 7
SHEET 1 A 7 ASP A 219 ASP A 223 0
SHEET 2 A 7 VAL A 191 ASP A 196 -1 N LYS A 194 O ASP A 219
SHEET 3 A 7 THR A 202 ALA A 207 -1 N ALA A 207 O VAL A 191
SHEET 4 A 7 GLY A 2 ALA A 7 -1 N ALA A 7 O TYR A 204
SHEET 5 A 7 MET A 67 ARG A 73 -1 N VAL A 72 O GLY A 2
SHEET 6 A 7 ALA A 30 ILE A 36 -1 N ILE A 36 O MET A 67
SHEET 7 A 7 PHE A 42 ASN A 48 -1 N ALA A 47 O ALA A 31
SHEET 1 B 6 PHE A 88 VAL A 90 0
SHEET 2 B 6 ILE A 96 LEU A 104 -1 N LEU A 98 O PHE A 88
SHEET 3 B 6 GLY A 165 ILE A 173 -1 N MET A 172 O THR A 97
SHEET 4 B 6 GLY A 177 ARG A 182 -1 N PHE A 181 O CYS A 169
SHEET 5 B 6 GLU A 228 THR A 233 -1 N ILE A 232 O MET A 178
SHEET 6 B 6 LEU A 238 GLN A 242 -1 N ARG A 241 O ALA A 229
SHEET 1 C 4 VAL A 297 PRO A 300 0
SHEET 2 C 4 ASN A 361 ASP A 366 1 N LEU A 363 O VAL A 297
SHEET 3 C 4 LYS A 389 SER A 394 1 N LYS A 389 O VAL A 362
SHEET 4 C 4 GLY A 433 PHE A 436 1 N GLY A 433 O LEU A 392
SHEET 1 D 2 PHE A 324 LYS A 326 0
SHEET 2 D 2 LEU A 350 ALA A 352 -1 N ASN A 351 O VAL A 325
SHEET 1 E 7 ASP B 219 ASP B 223 0
SHEET 2 E 7 VAL B 191 ASP B 198 -1 N LYS B 194 O ASP B 219
SHEET 3 E 7 ARG B 201 ALA B 207 -1 N ALA B 207 O VAL B 191
SHEET 4 E 7 GLY B 2 ALA B 7 -1 N ALA B 7 O TYR B 204
SHEET 5 E 7 MET B 67 ARG B 73 -1 N VAL B 72 O GLY B 2
SHEET 6 E 7 ALA B 30 ILE B 36 -1 N ILE B 36 O MET B 67
SHEET 7 E 7 PHE B 42 ASN B 48 -1 N ALA B 47 O ALA B 31
SHEET 1 F 6 PHE B 88 VAL B 90 0
SHEET 2 F 6 ILE B 96 LEU B 104 -1 N LEU B 98 O PHE B 88
SHEET 3 F 6 GLY B 165 ILE B 173 -1 N MET B 172 O THR B 97
SHEET 4 F 6 GLY B 177 ARG B 182 -1 N PHE B 181 O CYS B 169
SHEET 5 F 6 GLU B 228 THR B 233 -1 N ILE B 232 O MET B 178
SHEET 6 F 6 LEU B 238 GLN B 242 -1 N ARG B 241 O ALA B 229
SHEET 1 G 4 VAL B 297 PRO B 300 0
SHEET 2 G 4 LYS B 360 ASP B 366 1 N LEU B 363 O VAL B 297
SHEET 3 G 4 ALA B 387 SER B 394 1 N LYS B 388 O LYS B 360
SHEET 4 G 4 GLY B 433 PHE B 436 1 N GLY B 433 O LEU B 392
SHEET 1 H 2 PHE B 324 LYS B 326 0
SHEET 2 H 2 LEU B 350 ALA B 352 -1 N ASN B 351 O VAL B 325
LINK SG CYS A 1 CE ONL A2377 1555 1555 1.81
LINK SG CYS B 1 CE ONL B2450 1555 1555 1.79
LINK OE2 GLU A 449 MN MN A2376 1555 1555 2.57
LINK OG1 THR A 480 MN MN B1449 8765 1555 2.22
LINK O1 PCP A 505 MN MN A 506 1555 1555 2.17
LINK O2 PCP A 505 MN MN A 506 1555 1555 2.06
LINK O3 PCP A 505 MN MN A 506 1555 1555 2.14
LINK O1B PCP A 505 MN MN A 506 1555 1555 2.21
LINK MN MN A 506 O HOH A2378 1555 1555 2.18
LINK MN MN A 506 O HOH A2379 1555 1555 2.22
LINK OE2 GLU B 449 MN MN B2449 1555 1555 2.25
LINK OD1 ASP B 471 MN MN B2449 5755 1555 2.69
LINK O1 PCP B 505 MN MN B 506 1555 1555 2.26
LINK O2 PCP B 505 MN MN B 506 1555 1555 2.19
LINK O3 PCP B 505 MN MN B 506 1555 1555 2.19
LINK O1B PCP B 505 MN MN B 506 1555 1555 2.20
LINK MN MN B 506 O HOH B2451 1555 1555 2.35
LINK MN MN B 506 O HOH B2452 1555 1555 2.25
LINK MN MN B2449 O HOH B2543 1555 1555 2.43
LINK MN MN B2449 O HOH B2597 1555 1555 2.44
LINK MN MN B2449 O HOH B2598 1555 1555 2.67
LINK MN MN B2449 O HOH B2599 1555 1555 2.70
LINK MN MN B2449 O HOH B2600 1555 1555 2.59
CISPEP 1 GLN A 86 PRO A 87 0 0.44
CISPEP 2 SER A 92 PRO A 93 0 0.24
CISPEP 3 TYR A 145 PRO A 146 0 -0.15
CISPEP 4 PRO A 302 GLU A 303 0 0.98
CISPEP 5 GLN B 86 PRO B 87 0 -0.90
CISPEP 6 SER B 92 PRO B 93 0 0.15
CISPEP 7 TYR B 145 PRO B 146 0 -0.03
CISPEP 8 PRO B 302 GLU B 303 0 1.66
SITE 1 NTA 1 CYS A 1
SITE 1 PRT 2 ASP A 366 ASP A 367
SITE 1 NTB 1 CYS B 1
SITE 1 PRB 2 ASP B 366 ASP B 367
SITE 1 AC1 5 ASP A 366 ASP A 367 PCP A 505 HOH A2378
SITE 2 AC1 5 HOH A2379
SITE 1 AC2 5 ASP B 366 ASP B 367 PCP B 505 HOH B2451
SITE 2 AC2 5 HOH B2452
SITE 1 AC3 4 ASP A 476 THR A 480 GLU B 376 ILE B 428
SITE 1 AC4 1 GLU A 449
SITE 1 AC5 7 GLU B 449 ASP B 471 HOH B2543 HOH B2597
SITE 2 AC5 7 HOH B2598 HOH B2599 HOH B2600
SITE 1 AC6 11 CYS A 1 ARG A 73 TYR A 74 THR A 76
SITE 2 AC6 11 ALA A 77 GLN A 86 ASN A 101 GLY A 102
SITE 3 AC6 11 ASP A 127 SER A 128 HOH A2402
SITE 1 AC7 22 TYR A 258 GLU A 303 THR A 304 ARG A 332
SITE 2 AC7 22 THR A 333 PHE A 334 LYS A 349 ASP A 366
SITE 3 AC7 22 ASP A 367 SER A 368 ILE A 369 VAL A 370
SITE 4 AC7 22 ARG A 371 GLY A 372 THR A 373 THR A 374
SITE 5 AC7 22 MN A 506 HOH A2378 HOH A2379 HOH A2411
SITE 6 AC7 22 HOH A2431 ARG B 328
SITE 1 AC8 12 CYS B 1 ARG B 73 TYR B 74 THR B 76
SITE 2 AC8 12 ALA B 77 GLN B 86 HIS B 100 ASN B 101
SITE 3 AC8 12 GLY B 102 ASP B 127 SER B 128 HOH B2482
SITE 1 AC9 21 ARG A 328 TYR B 258 GLU B 303 THR B 304
SITE 2 AC9 21 ARG B 332 THR B 333 PHE B 334 LYS B 349
SITE 3 AC9 21 ASP B 366 ASP B 367 SER B 368 VAL B 370
SITE 4 AC9 21 ARG B 371 GLY B 372 THR B 373 THR B 374
SITE 5 AC9 21 MN B 506 HOH B2457 HOH B2460 HOH B2502
SITE 6 AC9 21 HOH B2574
CRYST1 78.200 78.200 308.800 90.00 90.00 90.00 P 43 21 2 16
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 0.012788 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012788 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003238 0.00000
MTRIX1 1 -0.142832 0.840250 0.523047 44.38500 1
MTRIX2 1 0.856486 -0.159910 0.490775 -100.04500 1
MTRIX3 1 0.496014 0.518081 -0.696822 92.62800 1
(ATOM LINES ARE NOT SHOWN.)
END
