HEADER HYDROLASE 07-MAY-97 3RLA
TITLE ALTERING THE BINUCLEAR MANGANESE CLUSTER OF ARGINASE DIMINISHES
TITLE 2 THERMOSTABILITY AND CATALYTIC FUNCTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ARGINASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 EC: 3.5.3.1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 CELL_LINE: BL21;
SOURCE 6 ORGAN: LIVER;
SOURCE 7 CELLULAR_LOCATION: CYTOPLASM;
SOURCE 8 GENE: PARGR-2;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 11 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 13 EXPRESSION_SYSTEM_PLASMID: PRSET C;
SOURCE 14 EXPRESSION_SYSTEM_GENE: PARG-X
KEYWDS HYDROLASE, UREA CYCLE, ARGININE METABOLISM
EXPDTA X-RAY DIFFRACTION
AUTHOR L.R.SCOLNICK,Z.F.KANYO,D.W.CHRISTIANSON
REVDAT 5 03-APR-24 3RLA 1 REMARK
REVDAT 4 28-FEB-24 3RLA 1 REMARK
REVDAT 3 03-NOV-21 3RLA 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 3RLA 1 VERSN
REVDAT 1 13-MAY-98 3RLA 0
JRNL AUTH L.R.SCOLNICK,Z.F.KANYO,R.C.CAVALLI,D.E.ASH,D.W.CHRISTIANSON
JRNL TITL ALTERING THE BINUCLEAR MANGANESE CLUSTER OF ARGINASE
JRNL TITL 2 DIMINISHES THERMOSTABILITY AND CATALYTIC FUNCTION.
JRNL REF BIOCHEMISTRY V. 36 10558 1997
JRNL REFN ISSN 0006-2960
JRNL PMID 9265637
JRNL DOI 10.1021/BI970800V
REMARK 2
REMARK 2 RESOLUTION. 2.54 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) : 2.54
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.1000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 74.0
REMARK 3 NUMBER OF REFLECTIONS : 24212
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) : 0.194
REMARK 3 FREE R VALUE : 0.282
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.000
REMARK 3 FREE R VALUE TEST SET COUNT : 694
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.000
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) : 2.54
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.65
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 79.50
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3245
REMARK 3 BIN R VALUE (WORKING SET) : 0.4200
REMARK 3 BIN FREE R VALUE : 0.5000
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 2.40
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 102
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.005
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7164
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 39
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 50.00
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) : 0.25
REMARK 3 LOW RESOLUTION CUTOFF (A) : 12.0
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) : 1.700
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.600
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 : RESTRAINTS
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 : PARAM-LRS.MAY96
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TOPH-LRS.MAY96
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT CORRECTION USED
REMARK 4
REMARK 4 3RLA 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_1000179132.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : JAN-95
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 8.5
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 RUH2R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : YALE MIRRORS
REMARK 200 OPTICS : YALE
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS II
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26381
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 8.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 74.0
REMARK 200 DATA REDUNDANCY : 2.500
REMARK 200 R MERGE (I) : 0.10500
REMARK 200 R SYM (I) : 0.10500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.54
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.60
REMARK 200 COMPLETENESS FOR SHELL (%) : 79.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
REMARK 200 R MERGE FOR SHELL (I) : 0.40000
REMARK 200 R SYM FOR SHELL (I) : 0.40000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: RAT LIVER ARGINASE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12 - 18% PEG 8000, 50 MM BICINE PH =
REMARK 280 8.5, 0.05% AZIDE, 1 MM MNCL2, PH 8.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
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
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 76.93333
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 38.46667
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6310 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -60.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 SER A 2
REMARK 465 SER A 3
REMARK 465 LYS A 4
REMARK 465 PRO A 5
REMARK 465 LYS A 320
REMARK 465 PRO A 321
REMARK 465 PRO A 322
REMARK 465 LYS A 323
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 SER B 3
REMARK 465 LYS B 4
REMARK 465 PRO B 5
REMARK 465 LYS B 320
REMARK 465 PRO B 321
REMARK 465 PRO B 322
REMARK 465 LYS B 323
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 SER C 3
REMARK 465 LYS C 4
REMARK 465 PRO C 5
REMARK 465 LYS C 320
REMARK 465 PRO C 321
REMARK 465 PRO C 322
REMARK 465 LYS C 323
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ASN A 101 CB CG OD1 ND2
REMARK 470 LEU A 319 O
REMARK 470 ASN B 101 CB CG OD1 ND2
REMARK 470 LEU B 319 O
REMARK 470 ASN C 101 CB CG OD1 ND2
REMARK 470 LEU C 319 O
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 B 273 CA - CB - CG ANGL. DEV. = 14.8 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 SER A 16 14.21 -146.99
REMARK 500 ARG A 21 105.68 -57.49
REMARK 500 GLU A 42 5.58 -67.74
REMARK 500 THR A 43 -167.65 -100.36
REMARK 500 GLN A 65 -75.42 67.36
REMARK 500 ASN A 90 20.47 -79.54
REMARK 500 PRO A 157 -159.88 -54.15
REMARK 500 PRO A 167 108.44 -42.93
REMARK 500 ARG A 180 8.80 -153.20
REMARK 500 ASP A 181 71.09 -153.29
REMARK 500 PRO B 14 57.97 -68.53
REMARK 500 SER B 16 13.61 -146.26
REMARK 500 GLU B 42 3.90 -68.08
REMARK 500 GLN B 65 -70.84 65.61
REMARK 500 ASP B 117 31.34 -96.86
REMARK 500 PRO B 157 -160.98 -50.41
REMARK 500 PRO B 167 105.16 -44.79
REMARK 500 ARG B 180 0.82 -152.29
REMARK 500 SER C 16 11.90 -141.28
REMARK 500 GLN C 65 -72.85 69.11
REMARK 500 ASN C 90 20.39 -76.63
REMARK 500 ILE C 105 -71.34 -54.85
REMARK 500 PRO C 157 -160.38 -51.18
REMARK 500 PRO C 160 106.86 -59.54
REMARK 500 PRO C 167 105.49 -42.05
REMARK 500 ARG C 180 4.36 -151.81
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 C 176 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 MN A 500 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 124 OD2
REMARK 620 2 ASP A 128 OD2 99.0
REMARK 620 3 ASP A 232 OD2 84.4 145.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 501 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 124 OD1
REMARK 620 2 HIS A 126 ND1 97.9
REMARK 620 3 ASP A 232 OD2 82.3 176.2
REMARK 620 4 ASP A 234 OD2 125.3 91.8 91.2
REMARK 620 5 ASP A 234 OD1 73.9 90.0 93.6 52.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 502 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 124 OD2
REMARK 620 2 ASP B 128 OD2 95.4
REMARK 620 3 ASP B 232 OD2 76.8 136.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 503 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 124 OD1
REMARK 620 2 HIS B 126 ND1 94.9
REMARK 620 3 ASP B 232 OD2 76.9 170.3
REMARK 620 4 ASP B 234 OD2 123.0 96.3 92.6
REMARK 620 5 ASP B 234 OD1 66.9 94.4 87.1 56.6
REMARK 620 6 HOH B 504 O 135.9 98.4 84.5 97.2 152.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN C 504 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 124 OD2
REMARK 620 2 ASP C 128 OD2 97.2
REMARK 620 3 ASP C 232 OD2 77.9 129.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN C 505 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 124 OD1
REMARK 620 2 HIS C 126 ND1 104.3
REMARK 620 3 ASP C 232 OD2 79.4 173.6
REMARK 620 4 ASP C 234 OD2 118.5 100.6 81.8
REMARK 620 5 ASP C 234 OD1 67.2 101.7 84.5 53.0
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: MNA
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: BI-MANGANESE NUCLEAR BINDING SITE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: MNB
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: BI-MANGANESE NUCLEAR BINDING SITE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: MNC
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: BI-MANGANESE NUCLEAR BINDING SITE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 505
DBREF 3RLA A 1 323 UNP P07824 ARGI1_RAT 1 323
DBREF 3RLA B 1 323 UNP P07824 ARGI1_RAT 1 323
DBREF 3RLA C 1 323 UNP P07824 ARGI1_RAT 1 323
SEQADV 3RLA ASN A 101 UNP P07824 HIS 101 ENGINEERED MUTATION
SEQADV 3RLA ASN B 101 UNP P07824 HIS 101 ENGINEERED MUTATION
SEQADV 3RLA ASN C 101 UNP P07824 HIS 101 ENGINEERED MUTATION
SEQRES 1 A 323 MET SER SER LYS PRO LYS PRO ILE GLU ILE ILE GLY ALA
SEQRES 2 A 323 PRO PHE SER LYS GLY GLN PRO ARG GLY GLY VAL GLU LYS
SEQRES 3 A 323 GLY PRO ALA ALA LEU ARG LYS ALA GLY LEU VAL GLU LYS
SEQRES 4 A 323 LEU LYS GLU THR GLU TYR ASN VAL ARG ASP HIS GLY ASP
SEQRES 5 A 323 LEU ALA PHE VAL ASP VAL PRO ASN ASP SER PRO PHE GLN
SEQRES 6 A 323 ILE VAL LYS ASN PRO ARG SER VAL GLY LYS ALA ASN GLU
SEQRES 7 A 323 GLN LEU ALA ALA VAL VAL ALA GLU THR GLN LYS ASN GLY
SEQRES 8 A 323 THR ILE SER VAL VAL LEU GLY GLY ASP ASN SER MET ALA
SEQRES 9 A 323 ILE GLY SER ILE SER GLY HIS ALA ARG VAL HIS PRO ASP
SEQRES 10 A 323 LEU CYS VAL ILE TRP VAL ASP ALA HIS THR ASP ILE ASN
SEQRES 11 A 323 THR PRO LEU THR THR SER SER GLY ASN LEU HIS GLY GLN
SEQRES 12 A 323 PRO VAL ALA PHE LEU LEU LYS GLU LEU LYS GLY LYS PHE
SEQRES 13 A 323 PRO ASP VAL PRO GLY PHE SER TRP VAL THR PRO CYS ILE
SEQRES 14 A 323 SER ALA LYS ASP ILE VAL TYR ILE GLY LEU ARG ASP VAL
SEQRES 15 A 323 ASP PRO GLY GLU HIS TYR ILE ILE LYS THR LEU GLY ILE
SEQRES 16 A 323 LYS TYR PHE SER MET THR GLU VAL ASP LYS LEU GLY ILE
SEQRES 17 A 323 GLY LYS VAL MET GLU GLU THR PHE SER TYR LEU LEU GLY
SEQRES 18 A 323 ARG LYS LYS ARG PRO ILE HIS LEU SER PHE ASP VAL ASP
SEQRES 19 A 323 GLY LEU ASP PRO VAL PHE THR PRO ALA THR GLY THR PRO
SEQRES 20 A 323 VAL VAL GLY GLY LEU SER TYR ARG GLU GLY LEU TYR ILE
SEQRES 21 A 323 THR GLU GLU ILE TYR LYS THR GLY LEU LEU SER GLY LEU
SEQRES 22 A 323 ASP ILE MET GLU VAL ASN PRO THR LEU GLY LYS THR PRO
SEQRES 23 A 323 GLU GLU VAL THR ARG THR VAL ASN THR ALA VAL ALA LEU
SEQRES 24 A 323 THR LEU SER CYS PHE GLY THR LYS ARG GLU GLY ASN HIS
SEQRES 25 A 323 LYS PRO GLU THR ASP TYR LEU LYS PRO PRO LYS
SEQRES 1 B 323 MET SER SER LYS PRO LYS PRO ILE GLU ILE ILE GLY ALA
SEQRES 2 B 323 PRO PHE SER LYS GLY GLN PRO ARG GLY GLY VAL GLU LYS
SEQRES 3 B 323 GLY PRO ALA ALA LEU ARG LYS ALA GLY LEU VAL GLU LYS
SEQRES 4 B 323 LEU LYS GLU THR GLU TYR ASN VAL ARG ASP HIS GLY ASP
SEQRES 5 B 323 LEU ALA PHE VAL ASP VAL PRO ASN ASP SER PRO PHE GLN
SEQRES 6 B 323 ILE VAL LYS ASN PRO ARG SER VAL GLY LYS ALA ASN GLU
SEQRES 7 B 323 GLN LEU ALA ALA VAL VAL ALA GLU THR GLN LYS ASN GLY
SEQRES 8 B 323 THR ILE SER VAL VAL LEU GLY GLY ASP ASN SER MET ALA
SEQRES 9 B 323 ILE GLY SER ILE SER GLY HIS ALA ARG VAL HIS PRO ASP
SEQRES 10 B 323 LEU CYS VAL ILE TRP VAL ASP ALA HIS THR ASP ILE ASN
SEQRES 11 B 323 THR PRO LEU THR THR SER SER GLY ASN LEU HIS GLY GLN
SEQRES 12 B 323 PRO VAL ALA PHE LEU LEU LYS GLU LEU LYS GLY LYS PHE
SEQRES 13 B 323 PRO ASP VAL PRO GLY PHE SER TRP VAL THR PRO CYS ILE
SEQRES 14 B 323 SER ALA LYS ASP ILE VAL TYR ILE GLY LEU ARG ASP VAL
SEQRES 15 B 323 ASP PRO GLY GLU HIS TYR ILE ILE LYS THR LEU GLY ILE
SEQRES 16 B 323 LYS TYR PHE SER MET THR GLU VAL ASP LYS LEU GLY ILE
SEQRES 17 B 323 GLY LYS VAL MET GLU GLU THR PHE SER TYR LEU LEU GLY
SEQRES 18 B 323 ARG LYS LYS ARG PRO ILE HIS LEU SER PHE ASP VAL ASP
SEQRES 19 B 323 GLY LEU ASP PRO VAL PHE THR PRO ALA THR GLY THR PRO
SEQRES 20 B 323 VAL VAL GLY GLY LEU SER TYR ARG GLU GLY LEU TYR ILE
SEQRES 21 B 323 THR GLU GLU ILE TYR LYS THR GLY LEU LEU SER GLY LEU
SEQRES 22 B 323 ASP ILE MET GLU VAL ASN PRO THR LEU GLY LYS THR PRO
SEQRES 23 B 323 GLU GLU VAL THR ARG THR VAL ASN THR ALA VAL ALA LEU
SEQRES 24 B 323 THR LEU SER CYS PHE GLY THR LYS ARG GLU GLY ASN HIS
SEQRES 25 B 323 LYS PRO GLU THR ASP TYR LEU LYS PRO PRO LYS
SEQRES 1 C 323 MET SER SER LYS PRO LYS PRO ILE GLU ILE ILE GLY ALA
SEQRES 2 C 323 PRO PHE SER LYS GLY GLN PRO ARG GLY GLY VAL GLU LYS
SEQRES 3 C 323 GLY PRO ALA ALA LEU ARG LYS ALA GLY LEU VAL GLU LYS
SEQRES 4 C 323 LEU LYS GLU THR GLU TYR ASN VAL ARG ASP HIS GLY ASP
SEQRES 5 C 323 LEU ALA PHE VAL ASP VAL PRO ASN ASP SER PRO PHE GLN
SEQRES 6 C 323 ILE VAL LYS ASN PRO ARG SER VAL GLY LYS ALA ASN GLU
SEQRES 7 C 323 GLN LEU ALA ALA VAL VAL ALA GLU THR GLN LYS ASN GLY
SEQRES 8 C 323 THR ILE SER VAL VAL LEU GLY GLY ASP ASN SER MET ALA
SEQRES 9 C 323 ILE GLY SER ILE SER GLY HIS ALA ARG VAL HIS PRO ASP
SEQRES 10 C 323 LEU CYS VAL ILE TRP VAL ASP ALA HIS THR ASP ILE ASN
SEQRES 11 C 323 THR PRO LEU THR THR SER SER GLY ASN LEU HIS GLY GLN
SEQRES 12 C 323 PRO VAL ALA PHE LEU LEU LYS GLU LEU LYS GLY LYS PHE
SEQRES 13 C 323 PRO ASP VAL PRO GLY PHE SER TRP VAL THR PRO CYS ILE
SEQRES 14 C 323 SER ALA LYS ASP ILE VAL TYR ILE GLY LEU ARG ASP VAL
SEQRES 15 C 323 ASP PRO GLY GLU HIS TYR ILE ILE LYS THR LEU GLY ILE
SEQRES 16 C 323 LYS TYR PHE SER MET THR GLU VAL ASP LYS LEU GLY ILE
SEQRES 17 C 323 GLY LYS VAL MET GLU GLU THR PHE SER TYR LEU LEU GLY
SEQRES 18 C 323 ARG LYS LYS ARG PRO ILE HIS LEU SER PHE ASP VAL ASP
SEQRES 19 C 323 GLY LEU ASP PRO VAL PHE THR PRO ALA THR GLY THR PRO
SEQRES 20 C 323 VAL VAL GLY GLY LEU SER TYR ARG GLU GLY LEU TYR ILE
SEQRES 21 C 323 THR GLU GLU ILE TYR LYS THR GLY LEU LEU SER GLY LEU
SEQRES 22 C 323 ASP ILE MET GLU VAL ASN PRO THR LEU GLY LYS THR PRO
SEQRES 23 C 323 GLU GLU VAL THR ARG THR VAL ASN THR ALA VAL ALA LEU
SEQRES 24 C 323 THR LEU SER CYS PHE GLY THR LYS ARG GLU GLY ASN HIS
SEQRES 25 C 323 LYS PRO GLU THR ASP TYR LEU LYS PRO PRO LYS
HET MN A 500 1
HET MN A 501 1
HET MN B 502 1
HET MN B 503 1
HET MN C 504 1
HET MN C 505 1
HETNAM MN MANGANESE (II) ION
FORMUL 4 MN 6(MN 2+)
FORMUL 10 HOH *39(H2 O)
HELIX 1 1 VAL A 24 LYS A 33 5 10
HELIX 2 2 LEU A 36 LYS A 41 1 6
HELIX 3 3 PRO A 70 LYS A 89 1 20
HELIX 4 4 ASN A 101 ALA A 112 5 12
HELIX 5 5 LEU A 140 GLY A 142 5 3
HELIX 6 6 PRO A 144 PHE A 147 5 4
HELIX 7 7 ALA A 171 ASP A 173 5 3
HELIX 8 8 PRO A 184 THR A 192 1 9
HELIX 9 9 MET A 200 LEU A 206 1 7
HELIX 10 10 ILE A 208 LEU A 220 1 13
HELIX 11 11 VAL A 233 GLY A 235 5 3
HELIX 12 12 TYR A 254 THR A 267 1 14
HELIX 13 13 PRO A 280 LEU A 282 5 3
HELIX 14 14 PRO A 286 CYS A 303 1 18
HELIX 15 15 VAL B 24 LYS B 33 5 10
HELIX 16 16 LEU B 36 LYS B 41 1 6
HELIX 17 17 PRO B 70 LYS B 89 1 20
HELIX 18 18 ASN B 101 ALA B 112 5 12
HELIX 19 19 LEU B 140 GLY B 142 5 3
HELIX 20 20 PRO B 144 LEU B 148 1 5
HELIX 21 21 ALA B 171 ASP B 173 5 3
HELIX 22 22 PRO B 184 THR B 192 1 9
HELIX 23 23 MET B 200 LEU B 220 1 21
HELIX 24 24 VAL B 233 GLY B 235 5 3
HELIX 25 25 TYR B 254 THR B 267 1 14
HELIX 26 26 PRO B 280 LEU B 282 5 3
HELIX 27 27 PRO B 286 CYS B 303 1 18
HELIX 28 28 VAL C 24 LYS C 33 5 10
HELIX 29 29 LEU C 36 LYS C 41 1 6
HELIX 30 30 PRO C 70 LYS C 89 1 20
HELIX 31 31 ASN C 101 VAL C 114 5 14
HELIX 32 32 LEU C 140 GLY C 142 5 3
HELIX 33 33 PRO C 144 PHE C 147 5 4
HELIX 34 34 ALA C 171 ASP C 173 5 3
HELIX 35 35 PRO C 184 THR C 192 1 9
HELIX 36 36 MET C 200 LEU C 220 1 21
HELIX 37 37 VAL C 233 GLY C 235 5 3
HELIX 38 38 TYR C 254 THR C 267 1 14
HELIX 39 39 PRO C 280 LEU C 282 5 3
HELIX 40 40 PRO C 286 CYS C 303 1 18
SHEET 1 A 8 ASN A 46 ASP A 49 0
SHEET 2 A 8 PRO A 7 GLY A 12 1 N ILE A 8 O ASN A 46
SHEET 3 A 8 THR A 92 LEU A 97 1 N ILE A 93 O PRO A 7
SHEET 4 A 8 LEU A 270 MET A 276 1 N LEU A 273 O SER A 94
SHEET 5 A 8 ILE A 227 ASP A 232 1 N ILE A 227 O SER A 271
SHEET 6 A 8 CYS A 119 VAL A 123 1 N CYS A 119 O HIS A 228
SHEET 7 A 8 ILE A 174 LEU A 179 1 N VAL A 175 O VAL A 120
SHEET 8 A 8 LYS A 196 SER A 199 1 N LYS A 196 O TYR A 176
SHEET 1 B 8 ASN B 46 ASP B 49 0
SHEET 2 B 8 PRO B 7 GLY B 12 1 N ILE B 8 O ASN B 46
SHEET 3 B 8 ILE B 93 LEU B 97 1 N ILE B 93 O GLU B 9
SHEET 4 B 8 LEU B 270 MET B 276 1 N LEU B 273 O SER B 94
SHEET 5 B 8 ILE B 227 ASP B 232 1 N ILE B 227 O SER B 271
SHEET 6 B 8 CYS B 119 VAL B 123 1 N CYS B 119 O HIS B 228
SHEET 7 B 8 ILE B 174 LEU B 179 1 N VAL B 175 O VAL B 120
SHEET 8 B 8 LYS B 196 SER B 199 1 N LYS B 196 O TYR B 176
SHEET 1 C 8 VAL C 47 ASP C 49 0
SHEET 2 C 8 PRO C 7 GLY C 12 1 N ILE C 8 O ARG C 48
SHEET 3 C 8 THR C 92 LEU C 97 1 N ILE C 93 O PRO C 7
SHEET 4 C 8 LEU C 270 MET C 276 1 N LEU C 273 O SER C 94
SHEET 5 C 8 ILE C 227 ASP C 232 1 N ILE C 227 O SER C 271
SHEET 6 C 8 CYS C 119 VAL C 123 1 N CYS C 119 O HIS C 228
SHEET 7 C 8 ILE C 174 LEU C 179 1 N VAL C 175 O VAL C 120
SHEET 8 C 8 LYS C 196 SER C 199 1 N LYS C 196 O TYR C 176
LINK OD2 ASP A 124 MN MN A 500 1555 1555 1.92
LINK OD1 ASP A 124 MN MN A 501 1555 1555 2.12
LINK ND1 HIS A 126 MN MN A 501 1555 1555 2.53
LINK OD2 ASP A 128 MN MN A 500 1555 1555 2.07
LINK OD2 ASP A 232 MN MN A 500 1555 1555 2.32
LINK OD2 ASP A 232 MN MN A 501 1555 1555 2.32
LINK OD2 ASP A 234 MN MN A 501 1555 1555 2.24
LINK OD1 ASP A 234 MN MN A 501 1555 1555 2.62
LINK OD2 ASP B 124 MN MN B 502 1555 1555 2.02
LINK OD1 ASP B 124 MN MN B 503 1555 1555 2.31
LINK ND1 HIS B 126 MN MN B 503 1555 1555 2.37
LINK OD2 ASP B 128 MN MN B 502 1555 1555 2.15
LINK OD2 ASP B 232 MN MN B 502 1555 1555 2.51
LINK OD2 ASP B 232 MN MN B 503 1555 1555 2.29
LINK OD2 ASP B 234 MN MN B 503 1555 1555 2.11
LINK OD1 ASP B 234 MN MN B 503 1555 1555 2.50
LINK MN MN B 503 O HOH B 504 1555 1555 2.57
LINK OD2 ASP C 124 MN MN C 504 1555 1555 2.16
LINK OD1 ASP C 124 MN MN C 505 1555 1555 2.31
LINK ND1 HIS C 126 MN MN C 505 1555 1555 2.28
LINK OD2 ASP C 128 MN MN C 504 1555 1555 2.13
LINK OD2 ASP C 232 MN MN C 504 1555 1555 2.76
LINK OD2 ASP C 232 MN MN C 505 1555 1555 2.65
LINK OD2 ASP C 234 MN MN C 505 1555 1555 2.29
LINK OD1 ASP C 234 MN MN C 505 1555 1555 2.60
CISPEP 1 GLY A 98 GLY A 99 0 -0.02
CISPEP 2 GLY B 98 GLY B 99 0 0.22
CISPEP 3 GLY C 98 GLY C 99 0 0.16
SITE 1 MNA 6 ASN A 101 ASP A 124 HIS A 126 ASP A 128
SITE 2 MNA 6 ASP A 232 ASP A 234
SITE 1 MNB 6 ASN B 101 ASP B 124 HIS B 126 ASP B 128
SITE 2 MNB 6 ASP B 232 ASP B 234
SITE 1 MNC 6 ASN C 101 ASP C 124 HIS C 126 ASP C 128
SITE 2 MNC 6 ASP C 232 ASP C 234
SITE 1 AC1 4 ASP A 124 ASP A 128 ASP A 232 MN A 501
SITE 1 AC2 5 ASP A 124 HIS A 126 ASP A 232 ASP A 234
SITE 2 AC2 5 MN A 500
SITE 1 AC3 4 TRP B 122 ASP B 124 ASP B 128 ASP B 232
SITE 1 AC4 5 ASP B 124 HIS B 126 ASP B 232 ASP B 234
SITE 2 AC4 5 HOH B 504
SITE 1 AC5 4 TRP C 122 ASP C 124 ASP C 128 ASP C 232
SITE 1 AC6 4 ASP C 124 HIS C 126 ASP C 232 ASP C 234
CRYST1 89.000 89.000 115.400 90.00 90.00 120.00 P 32 9
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 0.011236 0.006487 0.000000 0.00000
SCALE2 0.000000 0.012974 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008666 0.00000
MTRIX1 1 -0.420945 -0.852193 0.310761 -0.01375 1
MTRIX2 1 0.844137 -0.493426 -0.209675 51.70329 1
MTRIX3 1 0.332021 0.174063 0.927073 0.59379 1
MTRIX1 2 -0.439303 0.845288 0.304141 -44.10607 1
MTRIX2 2 -0.847093 -0.502493 0.173016 25.85707 1
MTRIX3 2 0.299077 -0.181630 0.936784 9.31568 1
(ATOM LINES ARE NOT SHOWN.)
END