HEADER HYDROLASE 19-AUG-11 3THH
TITLE CRYSTAL STRUCTURE OF THE CO2+2-HAI-ABH COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ARGINASE-1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: LIVER-TYPE ARGINASE, TYPE I ARGINASE;
COMPND 5 EC: 3.5.3.1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ARG1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PBS(KS)
KEYWDS ARGINASE FOLD, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.L.D'ANTONIO,D.W.CHRISTIANSON
REVDAT 5 13-SEP-23 3THH 1 REMARK LINK
REVDAT 4 20-NOV-19 3THH 1 LINK
REVDAT 3 26-OCT-11 3THH 1 HET HETNAM HETATM FORMUL
REVDAT 3 2 1 SITE LINK REMARK
REVDAT 2 28-SEP-11 3THH 1 JRNL
REVDAT 1 14-SEP-11 3THH 0
JRNL AUTH E.L.D'ANTONIO,D.W.CHRISTIANSON
JRNL TITL CRYSTAL STRUCTURES OF COMPLEXES WITH COBALT-RECONSTITUTED
JRNL TITL 2 HUMAN ARGINASE I.
JRNL REF BIOCHEMISTRY V. 50 8018 2011
JRNL REFN ISSN 0006-2960
JRNL PMID 21870783
JRNL DOI 10.1021/BI201101T
REMARK 2
REMARK 2 RESOLUTION. 1.85 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) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
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) (%) : 96.8
REMARK 3 NUMBER OF REFLECTIONS : 52538
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) : 0.239
REMARK 3 FREE R VALUE : 0.281
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 5146
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) : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.92
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 80.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3252
REMARK 3 BIN FREE R VALUE : 0.3402
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 456
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 : 4778
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 233
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.28
REMARK 3 ESD FROM SIGMAA (A) : 0.26
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) : 0.32
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.22
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.500
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.900
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
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 3THH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-AUG-11.
REMARK 100 THE DEPOSITION ID IS D_1000067483.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-OCT-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
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) : 0.9795
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : CRYOGENICALLY COOLED DOUBLE
REMARK 200 CRYSTAL MONOCHROMETER WITH
REMARK 200 HORIZONTAL FOCUSING SAGITTAL
REMARK 200 BEND SECOND MONO CRYSTAL WITH 4:
REMARK 200 1 MAGNIFICATION RATIO AND
REMARK 200 VERTICALLY FOCUSING MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52538
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : 0.07800
REMARK 200 R SYM (I) : 0.07800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.5480
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.92
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.4
REMARK 200 DATA REDUNDANCY IN SHELL : 4.30
REMARK 200 R MERGE FOR SHELL (I) : 0.58600
REMARK 200 R SYM FOR SHELL (I) : 0.58600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.324
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 2AEB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AN UNLIGANDED CO2+2-HAI CRYSTAL WAS
REMARK 280 SOAKED IN 20 MM ABH, 5 MM COCL2, 100 MM HEPES, 30% (V/V)
REMARK 280 JEFFAMINE ED-2001 FOR 39 HOURS, PH 7.0, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3
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
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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 8000 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -90.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
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: 7890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -86.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 -0.500000 -0.866025 0.000000 -90.42800
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 -45.21400
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 -78.31295
REMARK 350 BIOMT3 3 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 ALA A 3
REMARK 465 LYS A 4
REMARK 465 SER A 5
REMARK 465 PRO A 320
REMARK 465 PRO A 321
REMARK 465 LYS A 322
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 ALA B 3
REMARK 465 LYS B 4
REMARK 465 SER B 5
REMARK 465 PRO B 320
REMARK 465 PRO B 321
REMARK 465 LYS B 322
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 O HOH B 357 O HOH B 383 2455 2.19
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 -12.57 -141.90
REMARK 500 LYS A 17 1.93 -61.42
REMARK 500 GLU A 44 45.59 -87.22
REMARK 500 ILE A 58 69.20 -117.39
REMARK 500 PRO A 59 -39.39 -38.75
REMARK 500 ASP A 61 74.10 -151.65
REMARK 500 GLN A 65 -103.54 60.43
REMARK 500 ARG A 180 2.62 -153.45
REMARK 500 GLN B 43 -154.65 -95.19
REMARK 500 ASN B 60 78.63 -117.75
REMARK 500 ASP B 61 70.43 -115.55
REMARK 500 GLN B 65 -122.10 73.34
REMARK 500 ASN B 90 22.06 -77.24
REMARK 500 GLN B 143 -0.28 -140.33
REMARK 500 LYS B 153 33.13 -65.66
REMARK 500 ARG B 180 10.57 -157.44
REMARK 500 ASP B 181 80.29 -157.17
REMARK 500 PRO B 226 150.69 -41.28
REMARK 500 PRO B 238 -0.30 -59.12
REMARK 500 PRO B 314 81.61 -67.48
REMARK 500 LEU B 318 -30.40 -144.98
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 CO A 400 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 101 ND1
REMARK 620 2 ASP A 124 OD2 97.3
REMARK 620 3 ASP A 128 OD2 91.4 85.0
REMARK 620 4 ASP A 232 OD2 105.2 79.3 158.4
REMARK 620 5 ABH A 700 O1 164.4 98.2 87.4 80.3
REMARK 620 6 ABH A 700 O2 105.8 156.7 97.5 91.3 59.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CO A 401 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 124 OD1
REMARK 620 2 HIS A 126 ND1 93.6
REMARK 620 3 ASP A 232 OD2 91.4 166.2
REMARK 620 4 ASP A 234 OD1 137.3 98.5 86.3
REMARK 620 5 ASP A 234 OD2 79.0 104.0 89.6 58.4
REMARK 620 6 ABH A 700 O1 102.8 89.6 76.8 118.0 166.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CO B 400 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 101 ND1
REMARK 620 2 ASP B 124 OD2 96.9
REMARK 620 3 ASP B 128 OD2 91.2 90.0
REMARK 620 4 ASP B 232 OD2 102.7 83.8 165.4
REMARK 620 5 ABH B 700 O2 102.2 160.9 88.5 93.0
REMARK 620 6 ABH B 700 O1 163.9 98.9 91.4 76.6 62.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CO B 401 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 124 OD1
REMARK 620 2 HIS B 126 ND1 84.6
REMARK 620 3 ASP B 232 OD2 100.0 169.8
REMARK 620 4 ASP B 234 OD1 136.8 91.8 91.0
REMARK 620 5 ASP B 234 OD2 78.2 101.1 88.8 60.2
REMARK 620 6 ABH B 700 O1 102.8 95.6 74.6 120.3 163.3
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ABH A 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ABH B 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO B 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO B 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3THJ RELATED DB: PDB
REMARK 900 RELATED ID: 3THE RELATED DB: PDB
REMARK 900 SAME PROTEIN BUT IT LACKS THE INHIBITOR ABH AND IT IS AT PH 8.5
REMARK 900 RELATED ID: 3TH7 RELATED DB: PDB
REMARK 900 SAME PROTEIN BUT IT LACKS THE INHIBITOR ABH
REMARK 900 RELATED ID: 3TF3 RELATED DB: PDB
REMARK 900 SAME PROTEIN BUT IT LACKS METAL IONS AND THE INHIBITOR ABH
REMARK 900 RELATED ID: 2AEB RELATED DB: PDB
REMARK 900 SAME PROTEIN COMPLEXED WITH THE INHIBITOR ABH BUT THE METAL IONS
REMARK 900 ARE MN2+
REMARK 900 RELATED ID: 2PHA RELATED DB: PDB
REMARK 900 SAME PROTEIN BUT IT LACKS AN INHIBITOR AND THE METAL IONS ARE MN2+
DBREF 3THH A 1 322 UNP P05089 ARGI1_HUMAN 1 322
DBREF 3THH B 1 322 UNP P05089 ARGI1_HUMAN 1 322
SEQRES 1 A 322 MET SER ALA LYS SER ARG THR ILE GLY ILE ILE GLY ALA
SEQRES 2 A 322 PRO PHE SER LYS GLY GLN PRO ARG GLY GLY VAL GLU GLU
SEQRES 3 A 322 GLY PRO THR VAL LEU ARG LYS ALA GLY LEU LEU GLU LYS
SEQRES 4 A 322 LEU LYS GLU GLN GLU CYS ASP VAL LYS ASP TYR GLY ASP
SEQRES 5 A 322 LEU PRO PHE ALA ASP ILE PRO ASN ASP SER PRO PHE GLN
SEQRES 6 A 322 ILE VAL LYS ASN PRO ARG SER VAL GLY LYS ALA SER GLU
SEQRES 7 A 322 GLN LEU ALA GLY LYS VAL ALA GLU VAL LYS LYS ASN GLY
SEQRES 8 A 322 ARG ILE SER LEU VAL LEU GLY GLY ASP HIS SER LEU ALA
SEQRES 9 A 322 ILE GLY SER ILE SER GLY HIS ALA ARG VAL HIS PRO ASP
SEQRES 10 A 322 LEU GLY VAL ILE TRP VAL ASP ALA HIS THR ASP ILE ASN
SEQRES 11 A 322 THR PRO LEU THR THR THR SER GLY ASN LEU HIS GLY GLN
SEQRES 12 A 322 PRO VAL SER PHE LEU LEU LYS GLU LEU LYS GLY LYS ILE
SEQRES 13 A 322 PRO ASP VAL PRO GLY PHE SER TRP VAL THR PRO CYS ILE
SEQRES 14 A 322 SER ALA LYS ASP ILE VAL TYR ILE GLY LEU ARG ASP VAL
SEQRES 15 A 322 ASP PRO GLY GLU HIS TYR ILE LEU LYS THR LEU GLY ILE
SEQRES 16 A 322 LYS TYR PHE SER MET THR GLU VAL ASP ARG LEU GLY ILE
SEQRES 17 A 322 GLY LYS VAL MET GLU GLU THR LEU SER TYR LEU LEU GLY
SEQRES 18 A 322 ARG LYS LYS ARG PRO ILE HIS LEU SER PHE ASP VAL ASP
SEQRES 19 A 322 GLY LEU ASP PRO SER PHE THR PRO ALA THR GLY THR PRO
SEQRES 20 A 322 VAL VAL GLY GLY LEU THR TYR ARG GLU GLY LEU TYR ILE
SEQRES 21 A 322 THR GLU GLU ILE TYR LYS THR GLY LEU LEU SER GLY LEU
SEQRES 22 A 322 ASP ILE MET GLU VAL ASN PRO SER LEU GLY LYS THR PRO
SEQRES 23 A 322 GLU GLU VAL THR ARG THR VAL ASN THR ALA VAL ALA ILE
SEQRES 24 A 322 THR LEU ALA CYS PHE GLY LEU ALA ARG GLU GLY ASN HIS
SEQRES 25 A 322 LYS PRO ILE ASP TYR LEU ASN PRO PRO LYS
SEQRES 1 B 322 MET SER ALA LYS SER ARG THR ILE GLY ILE ILE GLY ALA
SEQRES 2 B 322 PRO PHE SER LYS GLY GLN PRO ARG GLY GLY VAL GLU GLU
SEQRES 3 B 322 GLY PRO THR VAL LEU ARG LYS ALA GLY LEU LEU GLU LYS
SEQRES 4 B 322 LEU LYS GLU GLN GLU CYS ASP VAL LYS ASP TYR GLY ASP
SEQRES 5 B 322 LEU PRO PHE ALA ASP ILE PRO ASN ASP SER PRO PHE GLN
SEQRES 6 B 322 ILE VAL LYS ASN PRO ARG SER VAL GLY LYS ALA SER GLU
SEQRES 7 B 322 GLN LEU ALA GLY LYS VAL ALA GLU VAL LYS LYS ASN GLY
SEQRES 8 B 322 ARG ILE SER LEU VAL LEU GLY GLY ASP HIS SER LEU ALA
SEQRES 9 B 322 ILE GLY SER ILE SER GLY HIS ALA ARG VAL HIS PRO ASP
SEQRES 10 B 322 LEU GLY VAL ILE TRP VAL ASP ALA HIS THR ASP ILE ASN
SEQRES 11 B 322 THR PRO LEU THR THR THR SER GLY ASN LEU HIS GLY GLN
SEQRES 12 B 322 PRO VAL SER PHE LEU LEU LYS GLU LEU LYS GLY LYS ILE
SEQRES 13 B 322 PRO ASP VAL PRO GLY PHE SER TRP VAL THR PRO CYS ILE
SEQRES 14 B 322 SER ALA LYS ASP ILE VAL TYR ILE GLY LEU ARG ASP VAL
SEQRES 15 B 322 ASP PRO GLY GLU HIS TYR ILE LEU LYS THR LEU GLY ILE
SEQRES 16 B 322 LYS TYR PHE SER MET THR GLU VAL ASP ARG LEU GLY ILE
SEQRES 17 B 322 GLY LYS VAL MET GLU GLU THR LEU SER TYR LEU LEU GLY
SEQRES 18 B 322 ARG LYS LYS ARG PRO ILE HIS LEU SER PHE ASP VAL ASP
SEQRES 19 B 322 GLY LEU ASP PRO SER PHE THR PRO ALA THR GLY THR PRO
SEQRES 20 B 322 VAL VAL GLY GLY LEU THR TYR ARG GLU GLY LEU TYR ILE
SEQRES 21 B 322 THR GLU GLU ILE TYR LYS THR GLY LEU LEU SER GLY LEU
SEQRES 22 B 322 ASP ILE MET GLU VAL ASN PRO SER LEU GLY LYS THR PRO
SEQRES 23 B 322 GLU GLU VAL THR ARG THR VAL ASN THR ALA VAL ALA ILE
SEQRES 24 B 322 THR LEU ALA CYS PHE GLY LEU ALA ARG GLU GLY ASN HIS
SEQRES 25 B 322 LYS PRO ILE ASP TYR LEU ASN PRO PRO LYS
HET CO A 400 1
HET CO A 401 1
HET ABH A 700 13
HET ABH B 700 13
HET CO B 400 1
HET CO B 401 1
HETNAM CO COBALT (II) ION
HETNAM ABH 2(S)-AMINO-6-BORONOHEXANOIC ACID
FORMUL 3 CO 4(CO 2+)
FORMUL 5 ABH 2(C6 H15 B N O5 1-)
FORMUL 9 HOH *233(H2 O)
HELIX 1 1 ARG A 21 GLU A 25 5 5
HELIX 2 2 GLU A 26 LYS A 33 1 8
HELIX 3 3 GLY A 35 GLU A 42 1 8
HELIX 4 4 ASN A 69 ASN A 90 1 22
HELIX 5 5 ASP A 100 SER A 102 5 3
HELIX 6 6 LEU A 103 HIS A 115 1 13
HELIX 7 7 ASN A 139 GLY A 142 5 4
HELIX 8 8 GLN A 143 LEU A 149 1 7
HELIX 9 9 LYS A 150 LYS A 153 5 4
HELIX 10 10 SER A 170 LYS A 172 5 3
HELIX 11 11 ASP A 183 GLY A 194 1 12
HELIX 12 12 SER A 199 GLY A 207 1 9
HELIX 13 13 GLY A 207 LEU A 220 1 14
HELIX 14 14 ASP A 234 LEU A 236 5 3
HELIX 15 15 THR A 253 GLY A 268 1 16
HELIX 16 16 ASN A 279 GLY A 283 5 5
HELIX 17 17 THR A 285 PHE A 304 1 20
HELIX 18 18 ARG B 21 GLU B 25 5 5
HELIX 19 19 GLU B 26 ALA B 34 1 9
HELIX 20 20 GLY B 35 GLN B 43 1 9
HELIX 21 21 ASN B 69 ASN B 90 1 22
HELIX 22 22 ASP B 100 SER B 102 5 3
HELIX 23 23 LEU B 103 ARG B 113 1 11
HELIX 24 24 ASN B 139 GLY B 142 5 4
HELIX 25 25 GLN B 143 LEU B 149 1 7
HELIX 26 26 LYS B 150 LYS B 153 5 4
HELIX 27 27 SER B 170 LYS B 172 5 3
HELIX 28 28 ASP B 183 GLY B 194 1 12
HELIX 29 29 SER B 199 GLY B 207 1 9
HELIX 30 30 GLY B 207 GLY B 221 1 15
HELIX 31 31 ASP B 234 LEU B 236 5 3
HELIX 32 32 THR B 253 GLY B 268 1 16
HELIX 33 33 ASN B 279 GLY B 283 5 5
HELIX 34 34 THR B 285 PHE B 304 1 20
SHEET 1 A 8 ASP A 46 ASP A 52 0
SHEET 2 A 8 THR A 7 GLY A 12 1 N ILE A 10 O TYR A 50
SHEET 3 A 8 ILE A 93 LEU A 97 1 O ILE A 93 N GLY A 9
SHEET 4 A 8 LEU A 270 MET A 276 1 O LEU A 273 N VAL A 96
SHEET 5 A 8 ILE A 227 ASP A 232 1 N LEU A 229 O GLY A 272
SHEET 6 A 8 GLY A 119 VAL A 123 1 N GLY A 119 O HIS A 228
SHEET 7 A 8 ILE A 174 ILE A 177 1 O VAL A 175 N TRP A 122
SHEET 8 A 8 LYS A 196 PHE A 198 1 O PHE A 198 N TYR A 176
SHEET 1 B 8 ASP B 46 ASP B 52 0
SHEET 2 B 8 THR B 7 ALA B 13 1 N ILE B 10 O TYR B 50
SHEET 3 B 8 ILE B 93 GLY B 98 1 O ILE B 93 N GLY B 9
SHEET 4 B 8 LEU B 270 MET B 276 1 O LEU B 273 N VAL B 96
SHEET 5 B 8 ILE B 227 ASP B 232 1 N LEU B 229 O GLY B 272
SHEET 6 B 8 GLY B 119 VAL B 123 1 N GLY B 119 O HIS B 228
SHEET 7 B 8 ILE B 174 ILE B 177 1 O VAL B 175 N TRP B 122
SHEET 8 B 8 LYS B 196 PHE B 198 1 O LYS B 196 N TYR B 176
LINK ND1 HIS A 101 CO CO A 400 1555 1555 2.08
LINK OD2 ASP A 124 CO CO A 400 1555 1555 1.89
LINK OD1 ASP A 124 CO CO A 401 1555 1555 1.95
LINK ND1 HIS A 126 CO CO A 401 1555 1555 2.16
LINK OD2 ASP A 128 CO CO A 400 1555 1555 2.10
LINK OD2 ASP A 232 CO CO A 400 1555 1555 2.14
LINK OD2 ASP A 232 CO CO A 401 1555 1555 2.34
LINK OD1 ASP A 234 CO CO A 401 1555 1555 2.20
LINK OD2 ASP A 234 CO CO A 401 1555 1555 2.31
LINK CO CO A 400 O1 ABH A 700 1555 1555 2.24
LINK CO CO A 400 O2 ABH A 700 1555 1555 2.30
LINK CO CO A 401 O1 ABH A 700 1555 1555 2.20
LINK ND1 HIS B 101 CO CO B 400 1555 1555 2.27
LINK OD2 ASP B 124 CO CO B 400 1555 1555 2.02
LINK OD1 ASP B 124 CO CO B 401 1555 1555 2.18
LINK ND1 HIS B 126 CO CO B 401 1555 1555 2.20
LINK OD2 ASP B 128 CO CO B 400 1555 1555 2.06
LINK OD2 ASP B 232 CO CO B 400 1555 1555 2.17
LINK OD2 ASP B 232 CO CO B 401 1555 1555 2.27
LINK OD1 ASP B 234 CO CO B 401 1555 1555 1.99
LINK OD2 ASP B 234 CO CO B 401 1555 1555 2.36
LINK CO CO B 400 O2 ABH B 700 1555 1555 2.20
LINK CO CO B 400 O1 ABH B 700 1555 1555 2.12
LINK CO CO B 401 O1 ABH B 700 1555 1555 2.12
SITE 1 AC1 6 HIS A 101 ASP A 124 ASP A 128 ASP A 232
SITE 2 AC1 6 CO A 401 ABH A 700
SITE 1 AC2 6 ASP A 124 HIS A 126 ASP A 232 ASP A 234
SITE 2 AC2 6 CO A 400 ABH A 700
SITE 1 AC3 19 HIS A 101 ASP A 124 HIS A 126 ASP A 128
SITE 2 AC3 19 ASN A 130 SER A 137 HIS A 141 ASP A 183
SITE 3 AC3 19 GLU A 186 ASP A 232 ASP A 234 GLU A 277
SITE 4 AC3 19 HOH A 335 HOH A 336 HOH A 342 HOH A 354
SITE 5 AC3 19 CO A 400 CO A 401 HOH A 406
SITE 1 AC4 20 HIS B 101 ASP B 124 HIS B 126 ASP B 128
SITE 2 AC4 20 ASN B 130 SER B 137 HIS B 141 ASP B 183
SITE 3 AC4 20 GLU B 186 ASP B 232 ASP B 234 GLU B 277
SITE 4 AC4 20 HOH B 332 HOH B 338 HOH B 345 HOH B 360
SITE 5 AC4 20 HOH B 369 HOH B 371 CO B 400 CO B 401
SITE 1 AC5 6 HIS B 101 ASP B 124 ASP B 128 ASP B 232
SITE 2 AC5 6 CO B 401 ABH B 700
SITE 1 AC6 6 ASP B 124 HIS B 126 ASP B 232 ASP B 234
SITE 2 AC6 6 CO B 400 ABH B 700
CRYST1 90.428 90.428 69.431 90.00 90.00 120.00 P 3 6
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.011059 0.006385 0.000000 0.00000
SCALE2 0.000000 0.012769 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014403 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
