HEADER HYDROLASE/HYDROLASE INHIBITOR 13-DEC-12 4IE2
TITLE CRYSTAL STRUCTURE OF HUMAN ARGINASE-2 COMPLEXED WITH INHIBITOR 1H
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ARGINASE-2, MITOCHONDRIAL;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: KIDNEY-TYPE ARGINASE, NON-HEPATIC ARGINASE, TYPE II
COMPND 5 ARGINASE;
COMPND 6 EC: 3.5.3.1;
COMPND 7 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: ARG2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET23B
KEYWDS METALLOENZYME, ALPHA/BETA FOLD, HYDROLASE, ARGININE METABOLISM,
KEYWDS 2 MANGANESE, MITOCHONDRION, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.COUSIDO-SIAH,A.MITSCHLER,F.X.RUIZ,P.BECKETT,M.C.VAN ZANDT,M.K.JI,
AUTHOR 2 D.WHITEHOUSE,T.RYDER,E.JAGDMANN,M.ANDREOLI,A.MAZUR,M.PADMANILAYAM,
AUTHOR 3 H.SCHROETER,A.GOLEBIOWSKI,A.PODJARNY
REVDAT 4 20-SEP-23 4IE2 1 REMARK LINK
REVDAT 3 15-NOV-17 4IE2 1 REMARK
REVDAT 2 03-APR-13 4IE2 1 JRNL
REVDAT 1 20-MAR-13 4IE2 0
JRNL AUTH A.GOLEBIOWSKI,R.PAUL BECKETT,M.VAN ZANDT,M.K.JI,
JRNL AUTH 2 D.WHITEHOUSE,T.R.RYDER,E.JAGDMANN,M.ANDREOLI,A.MAZUR,
JRNL AUTH 3 M.PADMANILAYAM,A.COUSIDO-SIAH,A.MITSCHLER,F.X.RUIZ,
JRNL AUTH 4 A.PODJARNY,H.SCHROETER
JRNL TITL 2-SUBSTITUTED-2-AMINO-6-BORONOHEXANOIC ACIDS AS ARGINASE
JRNL TITL 2 INHIBITORS.
JRNL REF BIOORG.MED.CHEM.LETT. V. 23 2027 2013
JRNL REFN ISSN 0960-894X
JRNL PMID 23453840
JRNL DOI 10.1016/J.BMCL.2013.02.024
REMARK 2
REMARK 2 RESOLUTION. 2.21 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV_1144
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.21
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.51
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.880
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 66155
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 3349
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 25.5144 - 6.3382 0.96 2786 141 0.1542 0.1977
REMARK 3 2 6.3382 - 5.0435 0.98 2665 149 0.1621 0.1934
REMARK 3 3 5.0435 - 4.4097 0.98 2620 154 0.1276 0.1743
REMARK 3 4 4.4097 - 4.0082 0.98 2629 133 0.1351 0.1917
REMARK 3 5 4.0082 - 3.7219 0.98 2607 145 0.1474 0.1663
REMARK 3 6 3.7219 - 3.5030 0.98 2588 146 0.1565 0.2029
REMARK 3 7 3.5030 - 3.3280 0.99 2632 131 0.1694 0.2277
REMARK 3 8 3.3280 - 3.1834 0.99 2612 138 0.1860 0.2354
REMARK 3 9 3.1834 - 3.0610 0.99 2626 129 0.1914 0.2663
REMARK 3 10 3.0610 - 2.9556 0.99 2637 119 0.1924 0.2323
REMARK 3 11 2.9556 - 2.8633 0.99 2624 147 0.1934 0.2507
REMARK 3 12 2.8633 - 2.7815 0.99 2618 116 0.1934 0.2640
REMARK 3 13 2.7815 - 2.7084 0.99 2620 126 0.1911 0.2741
REMARK 3 14 2.7084 - 2.6424 1.00 2582 163 0.1906 0.2364
REMARK 3 15 2.6424 - 2.5824 0.99 2625 126 0.1827 0.2475
REMARK 3 16 2.5824 - 2.5275 1.00 2590 153 0.1735 0.2219
REMARK 3 17 2.5275 - 2.4770 1.00 2605 153 0.1747 0.2179
REMARK 3 18 2.4770 - 2.4303 1.00 2569 138 0.1742 0.2130
REMARK 3 19 2.4303 - 2.3869 1.00 2616 146 0.1775 0.2552
REMARK 3 20 2.3869 - 2.3464 1.00 2586 158 0.1820 0.2346
REMARK 3 21 2.3464 - 2.3086 1.00 2600 149 0.1759 0.2295
REMARK 3 22 2.3086 - 2.2731 1.00 2579 135 0.1820 0.2455
REMARK 3 23 2.2731 - 2.2397 1.00 2604 135 0.1934 0.2119
REMARK 3 24 2.2397 - 2.2082 0.99 2586 119 0.2152 0.2834
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.010
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.87
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 7386
REMARK 3 ANGLE : 1.275 10076
REMARK 3 CHIRALITY : 0.167 1155
REMARK 3 PLANARITY : 0.005 1323
REMARK 3 DIHEDRAL : 13.748 2743
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4IE2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JAN-13.
REMARK 100 THE DEPOSITION ID IS D_1000076635.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-JAN-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
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 MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178
REMARK 200 MONOCHROMATOR : DOUBLE MIRRORS MONOCHROMATOR
REMARK 200 OPTICS : OSMIC MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 66565
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.208
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 9.400
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.21
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.29
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 6.60
REMARK 200 R MERGE FOR SHELL (I) : 0.43200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1D3V
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS IN CONDITION H3 FROM SILVER
REMARK 280 BULLET SCREEN (HAMPTON RESEARCH) USING TACSIMATE IN THE
REMARK 280 RESERVOIR, PH 7, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -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 -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 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 64.04700
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 64.04700
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 79.54250
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 64.04700
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 64.04700
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 79.54250
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 64.04700
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 64.04700
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 79.54250
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 64.04700
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 64.04700
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 79.54250
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 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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
REMARK 350 BIOMOLECULE: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 578 LIES ON A SPECIAL POSITION.
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 C1 BME A 404 O1 BME A 406 0.85
REMARK 500 C1 BME B 404 O1 BME B 407 0.95
REMARK 500 C1 BME B 404 C1 BME B 407 1.00
REMARK 500 C2 BME B 404 C2 BME B 407 1.00
REMARK 500 O1 BME B 404 O1 BME B 407 1.13
REMARK 500 C2 BME B 404 C1 BME B 407 1.23
REMARK 500 C1 BME A 404 C1 BME A 406 1.31
REMARK 500 O1 BME A 404 O1 BME A 406 1.33
REMARK 500 C2 BME A 404 C2 BME A 406 1.47
REMARK 500 S2 BME B 404 S2 BME B 407 1.68
REMARK 500 C2 BME B 404 O1 BME B 407 1.78
REMARK 500 C2 BME A 404 C1 BME A 406 1.82
REMARK 500 O1 BME A 404 O HOH A 614 1.85
REMARK 500 C2 BME A 404 O1 BME A 406 1.92
REMARK 500 S2 BME B 404 C2 BME B 407 1.94
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 LEU A 85 -51.02 -150.01
REMARK 500 ARG A 199 -2.43 -155.30
REMARK 500 LEU B 85 -52.30 -146.92
REMARK 500 ARG B 199 -4.20 -155.21
REMARK 500 ASP B 253 1.06 -69.75
REMARK 500 LEU C 85 -49.71 -150.47
REMARK 500 ASP C 143 146.90 -171.39
REMARK 500 ARG C 199 -2.54 -158.37
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 401 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 120 ND1
REMARK 620 2 ASP A 143 OD2 94.9
REMARK 620 3 ASP A 147 OD2 89.5 87.1
REMARK 620 4 ASP A 251 OD2 106.0 83.8 162.6
REMARK 620 5 1EC A 405 O13 169.6 94.4 86.5 79.5
REMARK 620 6 1EC A 405 O11 101.0 163.5 88.8 95.7 69.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 402 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 143 OD1
REMARK 620 2 HIS A 145 ND1 93.9
REMARK 620 3 ASP A 251 OD2 89.9 173.7
REMARK 620 4 ASP A 253 OD2 136.7 93.2 87.4
REMARK 620 5 ASP A 253 OD1 81.3 101.1 84.4 55.4
REMARK 620 6 1EC A 405 O13 91.6 93.5 81.4 130.5 164.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 401 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 120 ND1
REMARK 620 2 ASP B 143 OD2 95.7
REMARK 620 3 ASP B 147 OD2 88.0 86.7
REMARK 620 4 ASP B 251 OD2 101.6 90.2 170.2
REMARK 620 5 1EC B 406 O11 102.8 160.4 87.7 92.3
REMARK 620 6 1EC B 406 O13 169.2 91.6 84.4 86.4 69.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 402 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 143 OD1
REMARK 620 2 HIS B 145 ND1 96.2
REMARK 620 3 ASP B 251 OD2 89.6 170.5
REMARK 620 4 ASP B 253 OD2 132.7 91.2 90.3
REMARK 620 5 ASP B 253 OD1 76.8 99.9 88.6 55.9
REMARK 620 6 1EC B 406 O13 92.3 90.3 82.0 134.5 165.7
REMARK 620 7 1EC B 406 O23 141.5 102.4 68.6 80.7 131.1 54.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN C 402 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 120 ND1
REMARK 620 2 ASP C 143 OD2 94.5
REMARK 620 3 ASP C 147 OD2 84.0 82.8
REMARK 620 4 ASP C 251 OD2 106.8 88.0 166.4
REMARK 620 5 1EC C 404 O11 106.2 158.4 93.1 91.8
REMARK 620 6 1EC C 404 O13 173.9 87.4 90.5 79.0 71.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN C 401 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 143 OD1
REMARK 620 2 HIS C 145 ND1 98.0
REMARK 620 3 ASP C 251 OD2 88.9 170.6
REMARK 620 4 ASP C 253 OD2 131.5 91.1 89.1
REMARK 620 5 ASP C 253 OD1 76.8 102.8 84.9 54.7
REMARK 620 6 1EC C 404 O13 89.2 91.4 82.3 138.4 161.3
REMARK 620 7 1EC C 404 O23 140.3 102.3 68.5 82.1 129.8 56.8
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEN A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1EC A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEN B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1EC B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME B 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEN C 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1EC C 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME C 405
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1D3V RELATED DB: PDB
REMARK 900 RELATED ID: 1PQ3 RELATED DB: PDB
DBREF 4IE2 A 24 329 UNP P78540 ARGI2_HUMAN 24 329
DBREF 4IE2 B 24 329 UNP P78540 ARGI2_HUMAN 24 329
DBREF 4IE2 C 24 329 UNP P78540 ARGI2_HUMAN 24 329
SEQRES 1 A 306 HIS SER VAL ALA VAL ILE GLY ALA PRO PHE SER GLN GLY
SEQRES 2 A 306 GLN LYS ARG LYS GLY VAL GLU HIS GLY PRO ALA ALA ILE
SEQRES 3 A 306 ARG GLU ALA GLY LEU MET LYS ARG LEU SER SER LEU GLY
SEQRES 4 A 306 CYS HIS LEU LYS ASP PHE GLY ASP LEU SER PHE THR PRO
SEQRES 5 A 306 VAL PRO LYS ASP ASP LEU TYR ASN ASN LEU ILE VAL ASN
SEQRES 6 A 306 PRO ARG SER VAL GLY LEU ALA ASN GLN GLU LEU ALA GLU
SEQRES 7 A 306 VAL VAL SER ARG ALA VAL SER ASP GLY TYR SER CYS VAL
SEQRES 8 A 306 THR LEU GLY GLY ASP HIS SER LEU ALA ILE GLY THR ILE
SEQRES 9 A 306 SER GLY HIS ALA ARG HIS CYS PRO ASP LEU CYS VAL VAL
SEQRES 10 A 306 TRP VAL ASP ALA HIS ALA ASP ILE ASN THR PRO LEU THR
SEQRES 11 A 306 THR SER SER GLY ASN LEU HIS GLY GLN PRO VAL SER PHE
SEQRES 12 A 306 LEU LEU ARG GLU LEU GLN ASP LYS VAL PRO GLN LEU PRO
SEQRES 13 A 306 GLY PHE SER TRP ILE LYS PRO CYS ILE SER SER ALA SER
SEQRES 14 A 306 ILE VAL TYR ILE GLY LEU ARG ASP VAL ASP PRO PRO GLU
SEQRES 15 A 306 HIS PHE ILE LEU LYS ASN TYR ASP ILE GLN TYR PHE SER
SEQRES 16 A 306 MET ARG ASP ILE ASP ARG LEU GLY ILE GLN LYS VAL MET
SEQRES 17 A 306 GLU ARG THR PHE ASP LEU LEU ILE GLY LYS ARG GLN ARG
SEQRES 18 A 306 PRO ILE HIS LEU SER PHE ASP ILE ASP ALA PHE ASP PRO
SEQRES 19 A 306 THR LEU ALA PRO ALA THR GLY THR PRO VAL VAL GLY GLY
SEQRES 20 A 306 LEU THR TYR ARG GLU GLY MET TYR ILE ALA GLU GLU ILE
SEQRES 21 A 306 HIS ASN THR GLY LEU LEU SER ALA LEU ASP LEU VAL GLU
SEQRES 22 A 306 VAL ASN PRO GLN LEU ALA THR SER GLU GLU GLU ALA LYS
SEQRES 23 A 306 THR THR ALA ASN LEU ALA VAL ASP VAL ILE ALA SER SER
SEQRES 24 A 306 PHE GLY GLN THR ARG GLU GLY
SEQRES 1 B 306 HIS SER VAL ALA VAL ILE GLY ALA PRO PHE SER GLN GLY
SEQRES 2 B 306 GLN LYS ARG LYS GLY VAL GLU HIS GLY PRO ALA ALA ILE
SEQRES 3 B 306 ARG GLU ALA GLY LEU MET LYS ARG LEU SER SER LEU GLY
SEQRES 4 B 306 CYS HIS LEU LYS ASP PHE GLY ASP LEU SER PHE THR PRO
SEQRES 5 B 306 VAL PRO LYS ASP ASP LEU TYR ASN ASN LEU ILE VAL ASN
SEQRES 6 B 306 PRO ARG SER VAL GLY LEU ALA ASN GLN GLU LEU ALA GLU
SEQRES 7 B 306 VAL VAL SER ARG ALA VAL SER ASP GLY TYR SER CYS VAL
SEQRES 8 B 306 THR LEU GLY GLY ASP HIS SER LEU ALA ILE GLY THR ILE
SEQRES 9 B 306 SER GLY HIS ALA ARG HIS CYS PRO ASP LEU CYS VAL VAL
SEQRES 10 B 306 TRP VAL ASP ALA HIS ALA ASP ILE ASN THR PRO LEU THR
SEQRES 11 B 306 THR SER SER GLY ASN LEU HIS GLY GLN PRO VAL SER PHE
SEQRES 12 B 306 LEU LEU ARG GLU LEU GLN ASP LYS VAL PRO GLN LEU PRO
SEQRES 13 B 306 GLY PHE SER TRP ILE LYS PRO CYS ILE SER SER ALA SER
SEQRES 14 B 306 ILE VAL TYR ILE GLY LEU ARG ASP VAL ASP PRO PRO GLU
SEQRES 15 B 306 HIS PHE ILE LEU LYS ASN TYR ASP ILE GLN TYR PHE SER
SEQRES 16 B 306 MET ARG ASP ILE ASP ARG LEU GLY ILE GLN LYS VAL MET
SEQRES 17 B 306 GLU ARG THR PHE ASP LEU LEU ILE GLY LYS ARG GLN ARG
SEQRES 18 B 306 PRO ILE HIS LEU SER PHE ASP ILE ASP ALA PHE ASP PRO
SEQRES 19 B 306 THR LEU ALA PRO ALA THR GLY THR PRO VAL VAL GLY GLY
SEQRES 20 B 306 LEU THR TYR ARG GLU GLY MET TYR ILE ALA GLU GLU ILE
SEQRES 21 B 306 HIS ASN THR GLY LEU LEU SER ALA LEU ASP LEU VAL GLU
SEQRES 22 B 306 VAL ASN PRO GLN LEU ALA THR SER GLU GLU GLU ALA LYS
SEQRES 23 B 306 THR THR ALA ASN LEU ALA VAL ASP VAL ILE ALA SER SER
SEQRES 24 B 306 PHE GLY GLN THR ARG GLU GLY
SEQRES 1 C 306 HIS SER VAL ALA VAL ILE GLY ALA PRO PHE SER GLN GLY
SEQRES 2 C 306 GLN LYS ARG LYS GLY VAL GLU HIS GLY PRO ALA ALA ILE
SEQRES 3 C 306 ARG GLU ALA GLY LEU MET LYS ARG LEU SER SER LEU GLY
SEQRES 4 C 306 CYS HIS LEU LYS ASP PHE GLY ASP LEU SER PHE THR PRO
SEQRES 5 C 306 VAL PRO LYS ASP ASP LEU TYR ASN ASN LEU ILE VAL ASN
SEQRES 6 C 306 PRO ARG SER VAL GLY LEU ALA ASN GLN GLU LEU ALA GLU
SEQRES 7 C 306 VAL VAL SER ARG ALA VAL SER ASP GLY TYR SER CYS VAL
SEQRES 8 C 306 THR LEU GLY GLY ASP HIS SER LEU ALA ILE GLY THR ILE
SEQRES 9 C 306 SER GLY HIS ALA ARG HIS CYS PRO ASP LEU CYS VAL VAL
SEQRES 10 C 306 TRP VAL ASP ALA HIS ALA ASP ILE ASN THR PRO LEU THR
SEQRES 11 C 306 THR SER SER GLY ASN LEU HIS GLY GLN PRO VAL SER PHE
SEQRES 12 C 306 LEU LEU ARG GLU LEU GLN ASP LYS VAL PRO GLN LEU PRO
SEQRES 13 C 306 GLY PHE SER TRP ILE LYS PRO CYS ILE SER SER ALA SER
SEQRES 14 C 306 ILE VAL TYR ILE GLY LEU ARG ASP VAL ASP PRO PRO GLU
SEQRES 15 C 306 HIS PHE ILE LEU LYS ASN TYR ASP ILE GLN TYR PHE SER
SEQRES 16 C 306 MET ARG ASP ILE ASP ARG LEU GLY ILE GLN LYS VAL MET
SEQRES 17 C 306 GLU ARG THR PHE ASP LEU LEU ILE GLY LYS ARG GLN ARG
SEQRES 18 C 306 PRO ILE HIS LEU SER PHE ASP ILE ASP ALA PHE ASP PRO
SEQRES 19 C 306 THR LEU ALA PRO ALA THR GLY THR PRO VAL VAL GLY GLY
SEQRES 20 C 306 LEU THR TYR ARG GLU GLY MET TYR ILE ALA GLU GLU ILE
SEQRES 21 C 306 HIS ASN THR GLY LEU LEU SER ALA LEU ASP LEU VAL GLU
SEQRES 22 C 306 VAL ASN PRO GLN LEU ALA THR SER GLU GLU GLU ALA LYS
SEQRES 23 C 306 THR THR ALA ASN LEU ALA VAL ASP VAL ILE ALA SER SER
SEQRES 24 C 306 PHE GLY GLN THR ARG GLU GLY
HET MN A 401 1
HET MN A 402 1
HET BEN A 403 9
HET BME A 404 4
HET 1EC A 405 17
HET BME A 406 4
HET MN B 401 1
HET MN B 402 1
HET BEN B 403 9
HET BME B 404 4
HET BME B 405 4
HET 1EC B 406 17
HET BME B 407 4
HET MN C 401 1
HET MN C 402 1
HET BEN C 403 9
HET 1EC C 404 17
HET BME C 405 4
HETNAM MN MANGANESE (II) ION
HETNAM BEN BENZAMIDINE
HETNAM BME BETA-MERCAPTOETHANOL
HETNAM 1EC [(5R)-5-AMINO-5-CARBOXY-8-HYDROXYOCTYL](TRIHYDROXY)
HETNAM 2 1EC BORATE(1-)
FORMUL 4 MN 6(MN 2+)
FORMUL 6 BEN 3(C7 H8 N2)
FORMUL 7 BME 6(C2 H6 O S)
FORMUL 8 1EC 3(C9 H21 B N O6 1-)
FORMUL 22 HOH *610(H2 O)
HELIX 1 1 GLY A 41 GLU A 43 5 3
HELIX 2 2 HIS A 44 ALA A 52 1 9
HELIX 3 3 GLY A 53 LEU A 61 1 9
HELIX 4 4 ASN A 88 ASP A 109 1 22
HELIX 5 5 ASP A 119 SER A 121 5 3
HELIX 6 6 LEU A 122 CYS A 134 1 13
HELIX 7 7 ASN A 158 GLY A 161 5 4
HELIX 8 8 GLN A 162 LEU A 168 1 7
HELIX 9 9 ARG A 169 VAL A 175 5 7
HELIX 10 10 SER A 189 ALA A 191 5 3
HELIX 11 11 ASP A 202 TYR A 212 1 11
HELIX 12 12 MET A 219 GLY A 226 1 8
HELIX 13 13 GLY A 226 GLY A 240 1 15
HELIX 14 14 ASP A 253 PHE A 255 5 3
HELIX 15 15 THR A 272 THR A 286 1 15
HELIX 16 16 ASN A 298 ALA A 302 5 5
HELIX 17 17 SER A 304 PHE A 323 1 20
HELIX 18 18 GLY B 41 GLU B 43 5 3
HELIX 19 19 HIS B 44 ALA B 52 1 9
HELIX 20 20 GLY B 53 LEU B 61 1 9
HELIX 21 21 ASN B 88 ASP B 109 1 22
HELIX 22 22 ASP B 119 SER B 121 5 3
HELIX 23 23 LEU B 122 CYS B 134 1 13
HELIX 24 24 ASN B 158 GLY B 161 5 4
HELIX 25 25 GLN B 162 LEU B 168 1 7
HELIX 26 26 ARG B 169 VAL B 175 5 7
HELIX 27 27 SER B 189 ALA B 191 5 3
HELIX 28 28 ASP B 202 TYR B 212 1 11
HELIX 29 29 MET B 219 GLY B 226 1 8
HELIX 30 30 GLY B 226 GLY B 240 1 15
HELIX 31 31 ASP B 253 PHE B 255 5 3
HELIX 32 32 THR B 272 GLY B 287 1 16
HELIX 33 33 ASN B 298 ALA B 302 5 5
HELIX 34 34 SER B 304 PHE B 323 1 20
HELIX 35 35 GLY C 41 GLU C 43 5 3
HELIX 36 36 HIS C 44 ALA C 52 1 9
HELIX 37 37 GLY C 53 LEU C 61 1 9
HELIX 38 38 ASN C 88 ASP C 109 1 22
HELIX 39 39 ASP C 119 SER C 121 5 3
HELIX 40 40 LEU C 122 CYS C 134 1 13
HELIX 41 41 ASN C 158 GLY C 161 5 4
HELIX 42 42 GLN C 162 LEU C 168 1 7
HELIX 43 43 ARG C 169 VAL C 175 5 7
HELIX 44 44 SER C 189 ALA C 191 5 3
HELIX 45 45 ASP C 202 TYR C 212 1 11
HELIX 46 46 MET C 219 GLY C 226 1 8
HELIX 47 47 GLY C 226 GLY C 240 1 15
HELIX 48 48 ASP C 253 PHE C 255 5 3
HELIX 49 49 THR C 272 GLY C 287 1 16
HELIX 50 50 ASN C 298 ALA C 302 5 5
HELIX 51 51 SER C 304 PHE C 323 1 20
SHEET 1 A 8 HIS A 64 ASP A 70 0
SHEET 2 A 8 SER A 25 ALA A 31 1 N VAL A 26 O HIS A 64
SHEET 3 A 8 SER A 112 GLY A 117 1 O VAL A 114 N ALA A 27
SHEET 4 A 8 LEU A 289 VAL A 295 1 O LEU A 292 N THR A 115
SHEET 5 A 8 ILE A 246 ASP A 251 1 N LEU A 248 O ALA A 291
SHEET 6 A 8 CYS A 138 VAL A 142 1 N VAL A 140 O SER A 249
SHEET 7 A 8 ILE A 193 LEU A 198 1 O VAL A 194 N TRP A 141
SHEET 8 A 8 GLN A 215 SER A 218 1 O PHE A 217 N GLY A 197
SHEET 1 B 8 HIS B 64 ASP B 70 0
SHEET 2 B 8 SER B 25 GLY B 30 1 N VAL B 26 O HIS B 64
SHEET 3 B 8 SER B 112 LEU B 116 1 O VAL B 114 N ALA B 27
SHEET 4 B 8 LEU B 289 VAL B 295 1 O LEU B 292 N CYS B 113
SHEET 5 B 8 ILE B 246 ASP B 251 1 N LEU B 248 O ALA B 291
SHEET 6 B 8 CYS B 138 VAL B 142 1 N VAL B 142 O ASP B 251
SHEET 7 B 8 ILE B 193 LEU B 198 1 O VAL B 194 N TRP B 141
SHEET 8 B 8 GLN B 215 SER B 218 1 O PHE B 217 N GLY B 197
SHEET 1 C 8 HIS C 64 ASP C 70 0
SHEET 2 C 8 SER C 25 GLY C 30 1 N VAL C 26 O HIS C 64
SHEET 3 C 8 SER C 112 LEU C 116 1 O VAL C 114 N ALA C 27
SHEET 4 C 8 LEU C 289 VAL C 295 1 O LEU C 292 N THR C 115
SHEET 5 C 8 ILE C 246 ASP C 251 1 N LEU C 248 O ALA C 291
SHEET 6 C 8 CYS C 138 VAL C 142 1 N VAL C 142 O ASP C 251
SHEET 7 C 8 ILE C 193 LEU C 198 1 O VAL C 194 N TRP C 141
SHEET 8 C 8 GLN C 215 SER C 218 1 O PHE C 217 N GLY C 197
LINK ND1 HIS A 120 MN MN A 401 1555 1555 2.20
LINK OD2 ASP A 143 MN MN A 401 1555 1555 2.06
LINK OD1 ASP A 143 MN MN A 402 1555 1555 2.17
LINK ND1 HIS A 145 MN MN A 402 1555 1555 2.15
LINK OD2 ASP A 147 MN MN A 401 1555 1555 2.09
LINK OD2 ASP A 251 MN MN A 401 1555 1555 2.31
LINK OD2 ASP A 251 MN MN A 402 1555 1555 2.25
LINK OD2 ASP A 253 MN MN A 402 1555 1555 2.23
LINK OD1 ASP A 253 MN MN A 402 1555 1555 2.47
LINK MN MN A 401 O13 1EC A 405 1555 1555 2.22
LINK MN MN A 401 O11 1EC A 405 1555 1555 2.27
LINK MN MN A 402 O13 1EC A 405 1555 1555 2.20
LINK ND1 HIS B 120 MN MN B 401 1555 1555 2.27
LINK OD2 ASP B 143 MN MN B 401 1555 1555 2.05
LINK OD1 ASP B 143 MN MN B 402 1555 1555 2.13
LINK ND1 HIS B 145 MN MN B 402 1555 1555 2.29
LINK OD2 ASP B 147 MN MN B 401 1555 1555 2.09
LINK OD2 ASP B 251 MN MN B 401 1555 1555 2.24
LINK OD2 ASP B 251 MN MN B 402 1555 1555 2.44
LINK OD2 ASP B 253 MN MN B 402 1555 1555 2.18
LINK OD1 ASP B 253 MN MN B 402 1555 1555 2.42
LINK MN MN B 401 O11 1EC B 406 1555 1555 2.23
LINK MN MN B 401 O13 1EC B 406 1555 1555 2.27
LINK MN MN B 402 O13 1EC B 406 1555 1555 2.26
LINK MN MN B 402 O23 1EC B 406 1555 1555 2.69
LINK ND1 HIS C 120 MN MN C 402 1555 1555 2.15
LINK OD1 ASP C 143 MN MN C 401 1555 1555 2.21
LINK OD2 ASP C 143 MN MN C 402 1555 1555 2.16
LINK ND1 HIS C 145 MN MN C 401 1555 1555 2.28
LINK OD2 ASP C 147 MN MN C 402 1555 1555 2.08
LINK OD2 ASP C 251 MN MN C 401 1555 1555 2.27
LINK OD2 ASP C 251 MN MN C 402 1555 1555 2.36
LINK OD2 ASP C 253 MN MN C 401 1555 1555 2.23
LINK OD1 ASP C 253 MN MN C 401 1555 1555 2.52
LINK MN MN C 401 O13 1EC C 404 1555 1555 2.17
LINK MN MN C 401 O23 1EC C 404 1555 1555 2.64
LINK MN MN C 402 O11 1EC C 404 1555 1555 2.08
LINK MN MN C 402 O13 1EC C 404 1555 1555 2.24
CISPEP 1 GLY A 117 GLY A 118 0 3.36
CISPEP 2 GLY B 117 GLY B 118 0 3.31
CISPEP 3 GLY C 117 GLY C 118 0 2.47
SITE 1 AC1 6 HIS A 120 ASP A 143 ASP A 147 ASP A 251
SITE 2 AC1 6 MN A 402 1EC A 405
SITE 1 AC2 6 ASP A 143 HIS A 145 ASP A 251 ASP A 253
SITE 2 AC2 6 MN A 401 1EC A 405
SITE 1 AC3 6 ASN A 83 ASN A 84 LEU A 85 PRO A 151
SITE 2 AC3 6 LEU A 152 THR A 154
SITE 1 AC4 7 HIS A 24 HIS A 284 PHE A 323 BME A 406
SITE 2 AC4 7 HOH A 607 HOH A 614 HOH A 663
SITE 1 AC5 22 HIS A 120 ASP A 143 HIS A 145 ASP A 147
SITE 2 AC5 22 ASN A 149 SER A 156 HIS A 160 ASP A 202
SITE 3 AC5 22 ASP A 251 ASP A 253 THR A 265 GLU A 296
SITE 4 AC5 22 MN A 401 MN A 402 HOH A 502 HOH A 512
SITE 5 AC5 22 HOH A 521 HOH A 522 HOH A 555 HOH A 556
SITE 6 AC5 22 HOH A 674 HOH A 709
SITE 1 AC6 4 LEU A 61 GLY A 62 PHE A 323 BME A 404
SITE 1 AC7 6 HIS B 120 ASP B 143 ASP B 147 ASP B 251
SITE 2 AC7 6 MN B 402 1EC B 406
SITE 1 AC8 6 ASP B 143 HIS B 145 ASP B 251 ASP B 253
SITE 2 AC8 6 MN B 401 1EC B 406
SITE 1 AC9 7 ASN B 83 ASN B 84 LEU B 85 PRO B 151
SITE 2 AC9 7 LEU B 152 THR B 153 THR B 154
SITE 1 BC1 7 HIS B 24 LEU B 61 CYS B 63 HIS B 284
SITE 2 BC1 7 PHE B 323 BME B 407 HOH B 669
SITE 1 BC2 7 PRO A 135 ARG A 169 HIS B 133 CYS B 134
SITE 2 BC2 7 PRO B 135 ASP B 136 PRO B 245
SITE 1 BC3 22 HIS B 120 ASP B 143 HIS B 145 ASP B 147
SITE 2 BC3 22 ASN B 149 SER B 155 SER B 156 HIS B 160
SITE 3 BC3 22 GLY B 161 ASP B 202 ASP B 251 ASP B 253
SITE 4 BC3 22 THR B 265 GLU B 296 MN B 401 MN B 402
SITE 5 BC3 22 HOH B 507 HOH B 511 HOH B 521 HOH B 531
SITE 6 BC3 22 HOH B 536 HOH B 715
SITE 1 BC4 5 VAL B 26 LEU B 61 GLY B 62 PHE B 323
SITE 2 BC4 5 BME B 404
SITE 1 BC5 6 ASP C 143 HIS C 145 ASP C 251 ASP C 253
SITE 2 BC5 6 MN C 402 1EC C 404
SITE 1 BC6 6 HIS C 120 ASP C 143 ASP C 147 ASP C 251
SITE 2 BC6 6 MN C 401 1EC C 404
SITE 1 BC7 6 ASN C 83 ASN C 84 LEU C 85 PRO C 151
SITE 2 BC7 6 LEU C 152 THR C 154
SITE 1 BC8 20 HIS C 120 ASP C 143 HIS C 145 ASP C 147
SITE 2 BC8 20 ASN C 149 SER C 156 HIS C 160 ASP C 202
SITE 3 BC8 20 ASP C 251 ASP C 253 THR C 265 GLU C 296
SITE 4 BC8 20 MN C 401 MN C 402 HOH C 513 HOH C 514
SITE 5 BC8 20 HOH C 519 HOH C 522 HOH C 556 HOH C 617
SITE 1 BC9 4 HIS C 24 CYS C 63 HIS C 284 PHE C 323
CRYST1 128.094 128.094 159.085 90.00 90.00 90.00 P 42 21 2 24
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 0.007807 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007807 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006286 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
