HEADER HYDROLASE 18-AUG-04 1WOG
TITLE CRYSTAL STRUCTURE OF AGMATINASE REVEALS STRUCTURAL CONSERVATION AND
TITLE 2 INHIBITION MECHANISM OF THE UREOHYDROLASE SUPERFAMILY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AGMATINASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 EC: 3.5.3.11;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;
SOURCE 3 ORGANISM_TAXID: 1299;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALPHA/BETA FOLD, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.J.AHN,K.H.KIM,J.LEE,J.-Y.HA,H.H.LEE,D.KIM,H.-J.YOON,A.-R.KWON,
AUTHOR 2 S.W.SUH
REVDAT 4 13-MAR-24 1WOG 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1WOG 1 VERSN
REVDAT 2 07-DEC-04 1WOG 1 JRNL
REVDAT 1 07-SEP-04 1WOG 0
JRNL AUTH H.J.AHN,K.H.KIM,J.LEE,J.-Y.HA,H.H.LEE,D.KIM,H.-J.YOON,
JRNL AUTH 2 A.-R.KWON,S.W.SUH
JRNL TITL CRYSTAL STRUCTURE OF AGMATINASE REVEALS STRUCTURAL
JRNL TITL 2 CONSERVATION AND INHIBITION MECHANISM OF THE UREOHYDROLASE
JRNL TITL 3 SUPERFAMILY
JRNL REF J.BIOL.CHEM. V. 279 50505 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 15355972
JRNL DOI 10.1074/JBC.M409246200
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 16.46
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 3579369.930
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 164248
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) : 0.223
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 16341
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.002
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.91
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 23088
REMARK 3 BIN R VALUE (WORKING SET) : 0.2440
REMARK 3 BIN FREE R VALUE : 0.2730
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 2582
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 : 13722
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 60
REMARK 3 SOLVENT ATOMS : 843
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.14000
REMARK 3 B22 (A**2) : -0.08000
REMARK 3 B33 (A**2) : -2.05000
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) : 0.21
REMARK 3 ESD FROM SIGMAA (A) : 0.14
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) : 0.24
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.17
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.860
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
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 : FLAT MODEL
REMARK 3 KSOL : 0.56
REMARK 3 BSOL : 92.48
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : INH.PARAM
REMARK 3 PARAMETER FILE 5 : CIS_PEPTIDE.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WOG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-AUG-04.
REMARK 100 THE DEPOSITION ID IS D_1000023813.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-NOV-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 6B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : DOUBLE MIRROR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MACSCIENCE DIP100
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 180589
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.91
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3000, SODIUM PHOSPHATE CITRATE,
REMARK 280 NACL, PH 4.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-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 40.88450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 84.42700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 65.71800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 84.42700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 40.88450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 65.71800
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 29590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 51120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -160.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
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 MET B 1
REMARK 465 SER B 2
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 MET D 1
REMARK 465 SER D 2
REMARK 465 MET E 1
REMARK 465 SER E 2
REMARK 465 MET F 1
REMARK 465 SER F 2
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 ASP A 39 19.66 -140.97
REMARK 500 PHE A 44 -100.67 -136.22
REMARK 500 LEU A 91 -137.33 53.30
REMARK 500 ASP A 210 87.87 -160.42
REMARK 500 ALA B 16 19.34 58.55
REMARK 500 PHE B 44 -99.17 -140.81
REMARK 500 LEU B 91 -132.01 54.02
REMARK 500 GLU B 92 63.88 38.21
REMARK 500 ASP B 210 93.87 -161.37
REMARK 500 ASP C 39 20.15 -141.09
REMARK 500 PHE C 44 -100.59 -140.53
REMARK 500 LEU C 91 -137.59 54.67
REMARK 500 ASP C 210 94.85 -161.06
REMARK 500 ALA D 16 18.86 58.34
REMARK 500 PHE D 44 -104.52 -138.57
REMARK 500 LEU D 91 -137.80 53.49
REMARK 500 ASP D 210 84.61 -155.27
REMARK 500 HIS D 303 47.20 -145.01
REMARK 500 PHE E 44 -102.01 -143.44
REMARK 500 LEU E 91 -135.65 57.07
REMARK 500 ASP E 210 87.95 -152.21
REMARK 500 PHE F 44 -98.96 -139.10
REMARK 500 LEU F 91 -135.13 52.46
REMARK 500 SER F 243 78.14 -117.43
REMARK 500 HIS F 303 6.38 -152.59
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 A1601 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 121 ND1
REMARK 620 2 ASP A 143 OD2 94.8
REMARK 620 3 ASP A 147 OD2 85.1 92.8
REMARK 620 4 ASP A 229 OD2 103.6 89.1 170.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A1602 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 143 OD1
REMARK 620 2 HIS A 145 ND1 96.5
REMARK 620 3 ASP A 229 OD2 84.6 166.7
REMARK 620 4 ASP A 231 OD1 83.0 100.8 92.5
REMARK 620 5 ASP A 231 OD2 140.5 94.9 92.6 57.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B1603 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 121 ND1
REMARK 620 2 ASP B 143 OD2 93.2
REMARK 620 3 ASP B 147 OD2 88.0 85.2
REMARK 620 4 ASP B 229 OD2 101.9 92.6 170.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B1604 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 143 OD1
REMARK 620 2 HIS B 145 ND1 92.3
REMARK 620 3 ASP B 229 OD2 86.2 169.2
REMARK 620 4 ASP B 231 OD1 82.3 95.4 95.0
REMARK 620 5 ASP B 231 OD2 139.8 91.4 96.7 57.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN C1605 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 121 ND1
REMARK 620 2 ASP C 143 OD2 97.6
REMARK 620 3 ASP C 147 OD2 86.1 86.6
REMARK 620 4 ASP C 229 OD2 105.1 90.2 168.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN C1606 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 143 OD1
REMARK 620 2 HIS C 145 ND1 91.9
REMARK 620 3 ASP C 229 OD2 85.9 169.8
REMARK 620 4 ASP C 231 OD1 83.4 96.8 92.9
REMARK 620 5 ASP C 231 OD2 139.5 92.2 95.9 56.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN D1607 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 121 ND1
REMARK 620 2 ASP D 143 OD2 95.7
REMARK 620 3 ASP D 147 OD2 89.7 87.9
REMARK 620 4 ASP D 229 OD2 103.6 90.4 166.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN D1608 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 143 OD1
REMARK 620 2 HIS D 145 ND1 95.1
REMARK 620 3 ASP D 229 OD2 85.1 166.6
REMARK 620 4 ASP D 231 OD1 83.5 101.5 91.9
REMARK 620 5 ASP D 231 OD2 141.9 91.6 96.5 58.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN E1609 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS E 121 ND1
REMARK 620 2 ASP E 143 OD2 95.8
REMARK 620 3 ASP E 147 OD2 84.2 83.1
REMARK 620 4 ASP E 229 OD2 104.8 93.1 170.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN E1610 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 143 OD1
REMARK 620 2 HIS E 145 ND1 91.0
REMARK 620 3 ASP E 229 OD2 85.0 169.7
REMARK 620 4 ASP E 231 OD1 82.2 98.3 90.7
REMARK 620 5 ASP E 231 OD2 139.6 95.9 93.3 57.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN F1611 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS F 121 ND1
REMARK 620 2 ASP F 143 OD2 97.3
REMARK 620 3 ASP F 147 OD2 90.0 82.4
REMARK 620 4 ASP F 229 OD2 104.1 91.6 165.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN F1612 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 143 OD1
REMARK 620 2 HIS F 145 ND1 92.3
REMARK 620 3 ASP F 229 OD2 86.2 171.7
REMARK 620 4 ASP F 231 OD1 81.1 96.2 91.7
REMARK 620 5 ASP F 231 OD2 139.3 91.6 94.9 58.2
REMARK 620 N 1 2 3 4
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 1601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 1602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 1603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 1604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 1605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 1606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN D 1607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN D 1608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 1609
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 1610
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN F 1611
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN F 1612
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 16D A 1401
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 16D B 1402
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 16D C 1403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 16D D 1404
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 16D E 1405
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 16D F 1406
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1WOH RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITHOUT LIGAND
REMARK 900 RELATED ID: 1WOI RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH MANGANESE (II) ION
DBREF 1WOG A 1 304 UNP Q9RZ04 Q9RZ04_DEIRA 1 304
DBREF 1WOG B 1 304 UNP Q9RZ04 Q9RZ04_DEIRA 1 304
DBREF 1WOG C 1 304 UNP Q9RZ04 Q9RZ04_DEIRA 1 304
DBREF 1WOG D 1 304 UNP Q9RZ04 Q9RZ04_DEIRA 1 304
DBREF 1WOG E 1 304 UNP Q9RZ04 Q9RZ04_DEIRA 1 304
DBREF 1WOG F 1 304 UNP Q9RZ04 Q9RZ04_DEIRA 1 304
SEQADV 1WOG LEU A 305 UNP Q9RZ04 CLONING ARTIFACT
SEQADV 1WOG LEU B 305 UNP Q9RZ04 CLONING ARTIFACT
SEQADV 1WOG LEU C 305 UNP Q9RZ04 CLONING ARTIFACT
SEQADV 1WOG LEU D 305 UNP Q9RZ04 CLONING ARTIFACT
SEQADV 1WOG LEU E 305 UNP Q9RZ04 CLONING ARTIFACT
SEQADV 1WOG LEU F 305 UNP Q9RZ04 CLONING ARTIFACT
SEQRES 1 A 305 MET SER GLY PRO ALA HIS LEU PRO TYR GLY GLY ILE PRO
SEQRES 2 A 305 THR PHE ALA ARG ALA PRO LEU VAL GLN PRO ASP GLY ASP
SEQRES 3 A 305 TRP GLN ALA ASP VAL ALA ALA LEU GLY VAL PRO PHE ASP
SEQRES 4 A 305 ILE ALA LEU GLY PHE ARG PRO GLY ALA ARG PHE ALA PRO
SEQRES 5 A 305 ARG ALA LEU ARG GLU ALA SER LEU ARG SER VAL PRO PRO
SEQRES 6 A 305 PHE THR GLY LEU ASP GLY LYS THR ARG LEU GLN GLY VAL
SEQRES 7 A 305 THR PHE ALA ASP ALA GLY ASP VAL ILE LEU PRO SER LEU
SEQRES 8 A 305 GLU PRO GLN LEU ALA HIS ASP ARG ILE THR GLU ALA ALA
SEQRES 9 A 305 ARG GLN VAL ARG GLY ARG CYS ARG VAL PRO VAL PHE LEU
SEQRES 10 A 305 GLY GLY ASP HIS SER VAL SER TYR PRO LEU LEU ARG ALA
SEQRES 11 A 305 PHE ALA ASP VAL PRO ASP LEU HIS VAL VAL GLN LEU ASP
SEQRES 12 A 305 ALA HIS LEU ASP PHE THR ASP THR ARG ASN ASP THR LYS
SEQRES 13 A 305 TRP SER ASN SER SER PRO PHE ARG ARG ALA CYS GLU ALA
SEQRES 14 A 305 LEU PRO ASN LEU VAL HIS ILE THR THR VAL GLY LEU ARG
SEQRES 15 A 305 GLY LEU ARG PHE ASP PRO GLU ALA VAL ALA ALA ALA ARG
SEQRES 16 A 305 ALA ARG GLY HIS THR ILE ILE PRO MET ASP ASP VAL THR
SEQRES 17 A 305 ALA ASP LEU ALA GLY VAL LEU ALA GLN LEU PRO ARG GLY
SEQRES 18 A 305 GLN ASN VAL TYR PHE SER VAL ASP VAL ASP GLY PHE ASP
SEQRES 19 A 305 PRO ALA VAL ILE PRO GLY THR SER SER PRO GLU PRO ASP
SEQRES 20 A 305 GLY LEU THR TYR ALA GLN GLY MET LYS ILE LEU ALA ALA
SEQRES 21 A 305 ALA ALA ALA ASN ASN THR VAL VAL GLY LEU ASP LEU VAL
SEQRES 22 A 305 GLU LEU ALA PRO ASN LEU ASP PRO THR GLY ARG SER GLU
SEQRES 23 A 305 LEU LEU MET ALA ARG LEU VAL MET GLU THR LEU CYS GLU
SEQRES 24 A 305 VAL PHE ASP HIS VAL LEU
SEQRES 1 B 305 MET SER GLY PRO ALA HIS LEU PRO TYR GLY GLY ILE PRO
SEQRES 2 B 305 THR PHE ALA ARG ALA PRO LEU VAL GLN PRO ASP GLY ASP
SEQRES 3 B 305 TRP GLN ALA ASP VAL ALA ALA LEU GLY VAL PRO PHE ASP
SEQRES 4 B 305 ILE ALA LEU GLY PHE ARG PRO GLY ALA ARG PHE ALA PRO
SEQRES 5 B 305 ARG ALA LEU ARG GLU ALA SER LEU ARG SER VAL PRO PRO
SEQRES 6 B 305 PHE THR GLY LEU ASP GLY LYS THR ARG LEU GLN GLY VAL
SEQRES 7 B 305 THR PHE ALA ASP ALA GLY ASP VAL ILE LEU PRO SER LEU
SEQRES 8 B 305 GLU PRO GLN LEU ALA HIS ASP ARG ILE THR GLU ALA ALA
SEQRES 9 B 305 ARG GLN VAL ARG GLY ARG CYS ARG VAL PRO VAL PHE LEU
SEQRES 10 B 305 GLY GLY ASP HIS SER VAL SER TYR PRO LEU LEU ARG ALA
SEQRES 11 B 305 PHE ALA ASP VAL PRO ASP LEU HIS VAL VAL GLN LEU ASP
SEQRES 12 B 305 ALA HIS LEU ASP PHE THR ASP THR ARG ASN ASP THR LYS
SEQRES 13 B 305 TRP SER ASN SER SER PRO PHE ARG ARG ALA CYS GLU ALA
SEQRES 14 B 305 LEU PRO ASN LEU VAL HIS ILE THR THR VAL GLY LEU ARG
SEQRES 15 B 305 GLY LEU ARG PHE ASP PRO GLU ALA VAL ALA ALA ALA ARG
SEQRES 16 B 305 ALA ARG GLY HIS THR ILE ILE PRO MET ASP ASP VAL THR
SEQRES 17 B 305 ALA ASP LEU ALA GLY VAL LEU ALA GLN LEU PRO ARG GLY
SEQRES 18 B 305 GLN ASN VAL TYR PHE SER VAL ASP VAL ASP GLY PHE ASP
SEQRES 19 B 305 PRO ALA VAL ILE PRO GLY THR SER SER PRO GLU PRO ASP
SEQRES 20 B 305 GLY LEU THR TYR ALA GLN GLY MET LYS ILE LEU ALA ALA
SEQRES 21 B 305 ALA ALA ALA ASN ASN THR VAL VAL GLY LEU ASP LEU VAL
SEQRES 22 B 305 GLU LEU ALA PRO ASN LEU ASP PRO THR GLY ARG SER GLU
SEQRES 23 B 305 LEU LEU MET ALA ARG LEU VAL MET GLU THR LEU CYS GLU
SEQRES 24 B 305 VAL PHE ASP HIS VAL LEU
SEQRES 1 C 305 MET SER GLY PRO ALA HIS LEU PRO TYR GLY GLY ILE PRO
SEQRES 2 C 305 THR PHE ALA ARG ALA PRO LEU VAL GLN PRO ASP GLY ASP
SEQRES 3 C 305 TRP GLN ALA ASP VAL ALA ALA LEU GLY VAL PRO PHE ASP
SEQRES 4 C 305 ILE ALA LEU GLY PHE ARG PRO GLY ALA ARG PHE ALA PRO
SEQRES 5 C 305 ARG ALA LEU ARG GLU ALA SER LEU ARG SER VAL PRO PRO
SEQRES 6 C 305 PHE THR GLY LEU ASP GLY LYS THR ARG LEU GLN GLY VAL
SEQRES 7 C 305 THR PHE ALA ASP ALA GLY ASP VAL ILE LEU PRO SER LEU
SEQRES 8 C 305 GLU PRO GLN LEU ALA HIS ASP ARG ILE THR GLU ALA ALA
SEQRES 9 C 305 ARG GLN VAL ARG GLY ARG CYS ARG VAL PRO VAL PHE LEU
SEQRES 10 C 305 GLY GLY ASP HIS SER VAL SER TYR PRO LEU LEU ARG ALA
SEQRES 11 C 305 PHE ALA ASP VAL PRO ASP LEU HIS VAL VAL GLN LEU ASP
SEQRES 12 C 305 ALA HIS LEU ASP PHE THR ASP THR ARG ASN ASP THR LYS
SEQRES 13 C 305 TRP SER ASN SER SER PRO PHE ARG ARG ALA CYS GLU ALA
SEQRES 14 C 305 LEU PRO ASN LEU VAL HIS ILE THR THR VAL GLY LEU ARG
SEQRES 15 C 305 GLY LEU ARG PHE ASP PRO GLU ALA VAL ALA ALA ALA ARG
SEQRES 16 C 305 ALA ARG GLY HIS THR ILE ILE PRO MET ASP ASP VAL THR
SEQRES 17 C 305 ALA ASP LEU ALA GLY VAL LEU ALA GLN LEU PRO ARG GLY
SEQRES 18 C 305 GLN ASN VAL TYR PHE SER VAL ASP VAL ASP GLY PHE ASP
SEQRES 19 C 305 PRO ALA VAL ILE PRO GLY THR SER SER PRO GLU PRO ASP
SEQRES 20 C 305 GLY LEU THR TYR ALA GLN GLY MET LYS ILE LEU ALA ALA
SEQRES 21 C 305 ALA ALA ALA ASN ASN THR VAL VAL GLY LEU ASP LEU VAL
SEQRES 22 C 305 GLU LEU ALA PRO ASN LEU ASP PRO THR GLY ARG SER GLU
SEQRES 23 C 305 LEU LEU MET ALA ARG LEU VAL MET GLU THR LEU CYS GLU
SEQRES 24 C 305 VAL PHE ASP HIS VAL LEU
SEQRES 1 D 305 MET SER GLY PRO ALA HIS LEU PRO TYR GLY GLY ILE PRO
SEQRES 2 D 305 THR PHE ALA ARG ALA PRO LEU VAL GLN PRO ASP GLY ASP
SEQRES 3 D 305 TRP GLN ALA ASP VAL ALA ALA LEU GLY VAL PRO PHE ASP
SEQRES 4 D 305 ILE ALA LEU GLY PHE ARG PRO GLY ALA ARG PHE ALA PRO
SEQRES 5 D 305 ARG ALA LEU ARG GLU ALA SER LEU ARG SER VAL PRO PRO
SEQRES 6 D 305 PHE THR GLY LEU ASP GLY LYS THR ARG LEU GLN GLY VAL
SEQRES 7 D 305 THR PHE ALA ASP ALA GLY ASP VAL ILE LEU PRO SER LEU
SEQRES 8 D 305 GLU PRO GLN LEU ALA HIS ASP ARG ILE THR GLU ALA ALA
SEQRES 9 D 305 ARG GLN VAL ARG GLY ARG CYS ARG VAL PRO VAL PHE LEU
SEQRES 10 D 305 GLY GLY ASP HIS SER VAL SER TYR PRO LEU LEU ARG ALA
SEQRES 11 D 305 PHE ALA ASP VAL PRO ASP LEU HIS VAL VAL GLN LEU ASP
SEQRES 12 D 305 ALA HIS LEU ASP PHE THR ASP THR ARG ASN ASP THR LYS
SEQRES 13 D 305 TRP SER ASN SER SER PRO PHE ARG ARG ALA CYS GLU ALA
SEQRES 14 D 305 LEU PRO ASN LEU VAL HIS ILE THR THR VAL GLY LEU ARG
SEQRES 15 D 305 GLY LEU ARG PHE ASP PRO GLU ALA VAL ALA ALA ALA ARG
SEQRES 16 D 305 ALA ARG GLY HIS THR ILE ILE PRO MET ASP ASP VAL THR
SEQRES 17 D 305 ALA ASP LEU ALA GLY VAL LEU ALA GLN LEU PRO ARG GLY
SEQRES 18 D 305 GLN ASN VAL TYR PHE SER VAL ASP VAL ASP GLY PHE ASP
SEQRES 19 D 305 PRO ALA VAL ILE PRO GLY THR SER SER PRO GLU PRO ASP
SEQRES 20 D 305 GLY LEU THR TYR ALA GLN GLY MET LYS ILE LEU ALA ALA
SEQRES 21 D 305 ALA ALA ALA ASN ASN THR VAL VAL GLY LEU ASP LEU VAL
SEQRES 22 D 305 GLU LEU ALA PRO ASN LEU ASP PRO THR GLY ARG SER GLU
SEQRES 23 D 305 LEU LEU MET ALA ARG LEU VAL MET GLU THR LEU CYS GLU
SEQRES 24 D 305 VAL PHE ASP HIS VAL LEU
SEQRES 1 E 305 MET SER GLY PRO ALA HIS LEU PRO TYR GLY GLY ILE PRO
SEQRES 2 E 305 THR PHE ALA ARG ALA PRO LEU VAL GLN PRO ASP GLY ASP
SEQRES 3 E 305 TRP GLN ALA ASP VAL ALA ALA LEU GLY VAL PRO PHE ASP
SEQRES 4 E 305 ILE ALA LEU GLY PHE ARG PRO GLY ALA ARG PHE ALA PRO
SEQRES 5 E 305 ARG ALA LEU ARG GLU ALA SER LEU ARG SER VAL PRO PRO
SEQRES 6 E 305 PHE THR GLY LEU ASP GLY LYS THR ARG LEU GLN GLY VAL
SEQRES 7 E 305 THR PHE ALA ASP ALA GLY ASP VAL ILE LEU PRO SER LEU
SEQRES 8 E 305 GLU PRO GLN LEU ALA HIS ASP ARG ILE THR GLU ALA ALA
SEQRES 9 E 305 ARG GLN VAL ARG GLY ARG CYS ARG VAL PRO VAL PHE LEU
SEQRES 10 E 305 GLY GLY ASP HIS SER VAL SER TYR PRO LEU LEU ARG ALA
SEQRES 11 E 305 PHE ALA ASP VAL PRO ASP LEU HIS VAL VAL GLN LEU ASP
SEQRES 12 E 305 ALA HIS LEU ASP PHE THR ASP THR ARG ASN ASP THR LYS
SEQRES 13 E 305 TRP SER ASN SER SER PRO PHE ARG ARG ALA CYS GLU ALA
SEQRES 14 E 305 LEU PRO ASN LEU VAL HIS ILE THR THR VAL GLY LEU ARG
SEQRES 15 E 305 GLY LEU ARG PHE ASP PRO GLU ALA VAL ALA ALA ALA ARG
SEQRES 16 E 305 ALA ARG GLY HIS THR ILE ILE PRO MET ASP ASP VAL THR
SEQRES 17 E 305 ALA ASP LEU ALA GLY VAL LEU ALA GLN LEU PRO ARG GLY
SEQRES 18 E 305 GLN ASN VAL TYR PHE SER VAL ASP VAL ASP GLY PHE ASP
SEQRES 19 E 305 PRO ALA VAL ILE PRO GLY THR SER SER PRO GLU PRO ASP
SEQRES 20 E 305 GLY LEU THR TYR ALA GLN GLY MET LYS ILE LEU ALA ALA
SEQRES 21 E 305 ALA ALA ALA ASN ASN THR VAL VAL GLY LEU ASP LEU VAL
SEQRES 22 E 305 GLU LEU ALA PRO ASN LEU ASP PRO THR GLY ARG SER GLU
SEQRES 23 E 305 LEU LEU MET ALA ARG LEU VAL MET GLU THR LEU CYS GLU
SEQRES 24 E 305 VAL PHE ASP HIS VAL LEU
SEQRES 1 F 305 MET SER GLY PRO ALA HIS LEU PRO TYR GLY GLY ILE PRO
SEQRES 2 F 305 THR PHE ALA ARG ALA PRO LEU VAL GLN PRO ASP GLY ASP
SEQRES 3 F 305 TRP GLN ALA ASP VAL ALA ALA LEU GLY VAL PRO PHE ASP
SEQRES 4 F 305 ILE ALA LEU GLY PHE ARG PRO GLY ALA ARG PHE ALA PRO
SEQRES 5 F 305 ARG ALA LEU ARG GLU ALA SER LEU ARG SER VAL PRO PRO
SEQRES 6 F 305 PHE THR GLY LEU ASP GLY LYS THR ARG LEU GLN GLY VAL
SEQRES 7 F 305 THR PHE ALA ASP ALA GLY ASP VAL ILE LEU PRO SER LEU
SEQRES 8 F 305 GLU PRO GLN LEU ALA HIS ASP ARG ILE THR GLU ALA ALA
SEQRES 9 F 305 ARG GLN VAL ARG GLY ARG CYS ARG VAL PRO VAL PHE LEU
SEQRES 10 F 305 GLY GLY ASP HIS SER VAL SER TYR PRO LEU LEU ARG ALA
SEQRES 11 F 305 PHE ALA ASP VAL PRO ASP LEU HIS VAL VAL GLN LEU ASP
SEQRES 12 F 305 ALA HIS LEU ASP PHE THR ASP THR ARG ASN ASP THR LYS
SEQRES 13 F 305 TRP SER ASN SER SER PRO PHE ARG ARG ALA CYS GLU ALA
SEQRES 14 F 305 LEU PRO ASN LEU VAL HIS ILE THR THR VAL GLY LEU ARG
SEQRES 15 F 305 GLY LEU ARG PHE ASP PRO GLU ALA VAL ALA ALA ALA ARG
SEQRES 16 F 305 ALA ARG GLY HIS THR ILE ILE PRO MET ASP ASP VAL THR
SEQRES 17 F 305 ALA ASP LEU ALA GLY VAL LEU ALA GLN LEU PRO ARG GLY
SEQRES 18 F 305 GLN ASN VAL TYR PHE SER VAL ASP VAL ASP GLY PHE ASP
SEQRES 19 F 305 PRO ALA VAL ILE PRO GLY THR SER SER PRO GLU PRO ASP
SEQRES 20 F 305 GLY LEU THR TYR ALA GLN GLY MET LYS ILE LEU ALA ALA
SEQRES 21 F 305 ALA ALA ALA ASN ASN THR VAL VAL GLY LEU ASP LEU VAL
SEQRES 22 F 305 GLU LEU ALA PRO ASN LEU ASP PRO THR GLY ARG SER GLU
SEQRES 23 F 305 LEU LEU MET ALA ARG LEU VAL MET GLU THR LEU CYS GLU
SEQRES 24 F 305 VAL PHE ASP HIS VAL LEU
HET MN A1601 1
HET MN A1602 1
HET 16D A1401 8
HET MN B1603 1
HET MN B1604 1
HET 16D B1402 8
HET MN C1605 1
HET MN C1606 1
HET 16D C1403 8
HET MN D1607 1
HET MN D1608 1
HET 16D D1404 8
HET MN E1609 1
HET MN E1610 1
HET 16D E1405 8
HET MN F1611 1
HET MN F1612 1
HET 16D F1406 8
HETNAM MN MANGANESE (II) ION
HETNAM 16D HEXANE-1,6-DIAMINE
HETSYN 16D 1,6-DIAMINOHEXANE
FORMUL 7 MN 12(MN 2+)
FORMUL 9 16D 6(C6 H16 N2)
FORMUL 25 HOH *843(H2 O)
HELIX 1 1 THR A 14 ALA A 18 5 5
HELIX 2 2 GLY A 47 ARG A 49 5 3
HELIX 3 3 PHE A 50 LEU A 60 1 11
HELIX 4 4 GLU A 92 GLY A 109 1 18
HELIX 5 5 ASP A 120 SER A 122 5 3
HELIX 6 6 VAL A 123 ARG A 129 1 7
HELIX 7 7 ALA A 130 ALA A 132 5 3
HELIX 8 8 SER A 161 LEU A 170 1 10
HELIX 9 9 ASP A 187 ARG A 197 1 11
HELIX 10 10 MET A 204 ASP A 210 1 7
HELIX 11 11 ASP A 210 ALA A 216 1 7
HELIX 12 12 ASP A 231 PHE A 233 5 3
HELIX 13 13 THR A 250 ASN A 265 1 16
HELIX 14 14 ALA A 276 ASP A 280 5 5
HELIX 15 15 GLY A 283 HIS A 303 1 21
HELIX 16 16 THR B 14 ALA B 18 5 5
HELIX 17 17 GLY B 47 ARG B 49 5 3
HELIX 18 18 PHE B 50 LEU B 60 1 11
HELIX 19 19 GLU B 92 GLY B 109 1 18
HELIX 20 20 ASP B 120 SER B 122 5 3
HELIX 21 21 VAL B 123 ARG B 129 1 7
HELIX 22 22 ALA B 130 ALA B 132 5 3
HELIX 23 23 SER B 161 LEU B 170 1 10
HELIX 24 24 ASP B 187 ARG B 197 1 11
HELIX 25 25 MET B 204 ASP B 210 1 7
HELIX 26 26 ASP B 210 ALA B 216 1 7
HELIX 27 27 ASP B 231 PHE B 233 5 3
HELIX 28 28 THR B 250 ASN B 265 1 16
HELIX 29 29 ALA B 276 ASP B 280 5 5
HELIX 30 30 GLY B 283 PHE B 301 1 19
HELIX 31 31 THR C 14 ALA C 18 5 5
HELIX 32 32 GLY C 47 ARG C 49 5 3
HELIX 33 33 PHE C 50 LEU C 60 1 11
HELIX 34 34 GLU C 92 ARG C 110 1 19
HELIX 35 35 ASP C 120 SER C 122 5 3
HELIX 36 36 VAL C 123 ALA C 130 1 8
HELIX 37 37 SER C 161 LEU C 170 1 10
HELIX 38 38 ASP C 187 ARG C 197 1 11
HELIX 39 39 MET C 204 ASP C 210 1 7
HELIX 40 40 ASP C 210 ALA C 216 1 7
HELIX 41 41 ASP C 231 PHE C 233 5 3
HELIX 42 42 THR C 250 ASN C 265 1 16
HELIX 43 43 ALA C 276 ASP C 280 5 5
HELIX 44 44 GLY C 283 ASP C 302 1 20
HELIX 45 45 THR D 14 ALA D 18 5 5
HELIX 46 46 GLY D 47 ARG D 49 5 3
HELIX 47 47 PHE D 50 SER D 59 1 10
HELIX 48 48 LEU D 60 SER D 62 5 3
HELIX 49 49 GLU D 92 GLY D 109 1 18
HELIX 50 50 ASP D 120 SER D 122 5 3
HELIX 51 51 VAL D 123 ARG D 129 1 7
HELIX 52 52 ALA D 130 ALA D 132 5 3
HELIX 53 53 SER D 161 GLU D 168 1 8
HELIX 54 54 ASP D 187 ARG D 197 1 11
HELIX 55 55 MET D 204 ALA D 216 1 13
HELIX 56 56 ASP D 231 PHE D 233 5 3
HELIX 57 57 THR D 250 ASN D 264 1 15
HELIX 58 58 ALA D 276 ASP D 280 5 5
HELIX 59 59 GLY D 283 ASP D 302 1 20
HELIX 60 60 THR E 14 ALA E 18 5 5
HELIX 61 61 GLY E 47 ARG E 49 5 3
HELIX 62 62 PHE E 50 LEU E 60 1 11
HELIX 63 63 GLU E 92 GLY E 109 1 18
HELIX 64 64 ASP E 120 SER E 122 5 3
HELIX 65 65 VAL E 123 ARG E 129 1 7
HELIX 66 66 ALA E 130 ALA E 132 5 3
HELIX 67 67 SER E 161 LEU E 170 1 10
HELIX 68 68 ASP E 187 ARG E 197 1 11
HELIX 69 69 MET E 204 ASP E 210 1 7
HELIX 70 70 ASP E 210 ALA E 216 1 7
HELIX 71 71 ASP E 231 PHE E 233 5 3
HELIX 72 72 THR E 250 ASN E 264 1 15
HELIX 73 73 ALA E 276 ASP E 280 5 5
HELIX 74 74 GLY E 283 PHE E 301 1 19
HELIX 75 75 THR F 14 ALA F 18 5 5
HELIX 76 76 GLY F 47 ARG F 49 5 3
HELIX 77 77 PHE F 50 LEU F 60 1 11
HELIX 78 78 GLU F 92 GLY F 109 1 18
HELIX 79 79 ASP F 120 SER F 122 5 3
HELIX 80 80 VAL F 123 ARG F 129 1 7
HELIX 81 81 ALA F 130 ALA F 132 5 3
HELIX 82 82 SER F 161 LEU F 170 1 10
HELIX 83 83 ASP F 187 ARG F 197 1 11
HELIX 84 84 MET F 204 ASP F 210 1 7
HELIX 85 85 ASP F 210 GLN F 217 1 8
HELIX 86 86 ASP F 231 PHE F 233 5 3
HELIX 87 87 THR F 250 ASN F 264 1 15
HELIX 88 88 ALA F 276 ASP F 280 5 5
HELIX 89 89 GLY F 283 ASP F 302 1 20
SHEET 1 A 8 PHE A 80 ASP A 85 0
SHEET 2 A 8 ALA A 29 VAL A 36 1 N ALA A 33 O ALA A 83
SHEET 3 A 8 CYS A 111 GLY A 118 1 O VAL A 115 N ALA A 32
SHEET 4 A 8 THR A 266 VAL A 273 1 O LEU A 270 N PHE A 116
SHEET 5 A 8 ASN A 223 ASP A 229 1 N VAL A 224 O THR A 266
SHEET 6 A 8 LEU A 137 LEU A 142 1 N HIS A 138 O ASN A 223
SHEET 7 A 8 LEU A 173 LEU A 181 1 O THR A 177 N GLN A 141
SHEET 8 A 8 THR A 200 PRO A 203 1 O ILE A 202 N THR A 178
SHEET 1 B 2 PHE A 66 THR A 67 0
SHEET 2 B 2 THR A 73 ARG A 74 -1 O ARG A 74 N PHE A 66
SHEET 1 C 8 PHE B 80 ASP B 85 0
SHEET 2 C 8 ALA B 29 VAL B 36 1 N ALA B 33 O ALA B 83
SHEET 3 C 8 CYS B 111 GLY B 118 1 O LEU B 117 N VAL B 36
SHEET 4 C 8 THR B 266 VAL B 273 1 O LEU B 270 N PHE B 116
SHEET 5 C 8 ASN B 223 ASP B 229 1 N PHE B 226 O GLY B 269
SHEET 6 C 8 LEU B 137 LEU B 142 1 N HIS B 138 O ASN B 223
SHEET 7 C 8 LEU B 173 LEU B 181 1 O THR B 177 N GLN B 141
SHEET 8 C 8 THR B 200 PRO B 203 1 O ILE B 202 N THR B 178
SHEET 1 D 2 PHE B 66 THR B 67 0
SHEET 2 D 2 THR B 73 ARG B 74 -1 O ARG B 74 N PHE B 66
SHEET 1 E 8 PHE C 80 ASP C 85 0
SHEET 2 E 8 ALA C 29 VAL C 36 1 N ALA C 33 O ALA C 83
SHEET 3 E 8 CYS C 111 GLY C 118 1 O LEU C 117 N VAL C 36
SHEET 4 E 8 THR C 266 VAL C 273 1 O LEU C 270 N PHE C 116
SHEET 5 E 8 ASN C 223 ASP C 229 1 N VAL C 224 O THR C 266
SHEET 6 E 8 LEU C 137 LEU C 142 1 N HIS C 138 O ASN C 223
SHEET 7 E 8 LEU C 173 LEU C 181 1 O THR C 177 N GLN C 141
SHEET 8 E 8 THR C 200 PRO C 203 1 O ILE C 202 N THR C 178
SHEET 1 F 2 PHE C 66 THR C 67 0
SHEET 2 F 2 THR C 73 ARG C 74 -1 O ARG C 74 N PHE C 66
SHEET 1 G 8 PHE D 80 ASP D 85 0
SHEET 2 G 8 ALA D 29 VAL D 36 1 N ALA D 33 O ALA D 83
SHEET 3 G 8 CYS D 111 GLY D 118 1 O LEU D 117 N VAL D 36
SHEET 4 G 8 THR D 266 VAL D 273 1 O LEU D 270 N PHE D 116
SHEET 5 G 8 ASN D 223 ASP D 229 1 N VAL D 228 O ASP D 271
SHEET 6 G 8 LEU D 137 LEU D 142 1 N HIS D 138 O ASN D 223
SHEET 7 G 8 LEU D 173 LEU D 181 1 O THR D 177 N GLN D 141
SHEET 8 G 8 THR D 200 PRO D 203 1 O ILE D 202 N THR D 178
SHEET 1 H 2 PHE D 66 THR D 67 0
SHEET 2 H 2 THR D 73 ARG D 74 -1 O ARG D 74 N PHE D 66
SHEET 1 I 8 PHE E 80 ASP E 85 0
SHEET 2 I 8 ALA E 29 VAL E 36 1 N ALA E 33 O ALA E 83
SHEET 3 I 8 CYS E 111 GLY E 118 1 O LEU E 117 N VAL E 36
SHEET 4 I 8 THR E 266 VAL E 273 1 O LEU E 270 N PHE E 116
SHEET 5 I 8 ASN E 223 ASP E 229 1 N PHE E 226 O GLY E 269
SHEET 6 I 8 LEU E 137 LEU E 142 1 N HIS E 138 O ASN E 223
SHEET 7 I 8 LEU E 173 LEU E 181 1 O THR E 177 N VAL E 139
SHEET 8 I 8 THR E 200 PRO E 203 1 O ILE E 202 N THR E 178
SHEET 1 J 2 PHE E 66 THR E 67 0
SHEET 2 J 2 THR E 73 ARG E 74 -1 O ARG E 74 N PHE E 66
SHEET 1 K 8 PHE F 80 ASP F 85 0
SHEET 2 K 8 ALA F 29 VAL F 36 1 N ALA F 33 O ALA F 83
SHEET 3 K 8 CYS F 111 GLY F 118 1 O LEU F 117 N VAL F 36
SHEET 4 K 8 THR F 266 VAL F 273 1 O LEU F 270 N PHE F 116
SHEET 5 K 8 ASN F 223 ASP F 229 1 N VAL F 224 O THR F 266
SHEET 6 K 8 LEU F 137 LEU F 142 1 N HIS F 138 O ASN F 223
SHEET 7 K 8 LEU F 173 LEU F 181 1 O VAL F 179 N GLN F 141
SHEET 8 K 8 THR F 200 PRO F 203 1 O ILE F 202 N THR F 178
SHEET 1 L 2 PHE F 66 THR F 67 0
SHEET 2 L 2 THR F 73 ARG F 74 -1 O ARG F 74 N PHE F 66
LINK ND1 HIS A 121 MN MN A1601 1555 1555 2.03
LINK OD2 ASP A 143 MN MN A1601 1555 1555 2.10
LINK OD1 ASP A 143 MN MN A1602 1555 1555 2.20
LINK ND1 HIS A 145 MN MN A1602 1555 1555 2.23
LINK OD2 ASP A 147 MN MN A1601 1555 1555 2.05
LINK OD2 ASP A 229 MN MN A1601 1555 1555 2.22
LINK OD2 ASP A 229 MN MN A1602 1555 1555 2.32
LINK OD1 ASP A 231 MN MN A1602 1555 1555 2.33
LINK OD2 ASP A 231 MN MN A1602 1555 1555 2.21
LINK ND1 HIS B 121 MN MN B1603 1555 1555 2.17
LINK OD2 ASP B 143 MN MN B1603 1555 1555 2.11
LINK OD1 ASP B 143 MN MN B1604 1555 1555 2.25
LINK ND1 HIS B 145 MN MN B1604 1555 1555 2.46
LINK OD2 ASP B 147 MN MN B1603 1555 1555 2.11
LINK OD2 ASP B 229 MN MN B1603 1555 1555 2.18
LINK OD2 ASP B 229 MN MN B1604 1555 1555 2.25
LINK OD1 ASP B 231 MN MN B1604 1555 1555 2.36
LINK OD2 ASP B 231 MN MN B1604 1555 1555 2.18
LINK ND1 HIS C 121 MN MN C1605 1555 1555 2.03
LINK OD2 ASP C 143 MN MN C1605 1555 1555 2.04
LINK OD1 ASP C 143 MN MN C1606 1555 1555 2.19
LINK ND1 HIS C 145 MN MN C1606 1555 1555 2.28
LINK OD2 ASP C 147 MN MN C1605 1555 1555 2.09
LINK OD2 ASP C 229 MN MN C1605 1555 1555 2.17
LINK OD2 ASP C 229 MN MN C1606 1555 1555 2.21
LINK OD1 ASP C 231 MN MN C1606 1555 1555 2.37
LINK OD2 ASP C 231 MN MN C1606 1555 1555 2.27
LINK ND1 HIS D 121 MN MN D1607 1555 1555 2.09
LINK OD2 ASP D 143 MN MN D1607 1555 1555 2.02
LINK OD1 ASP D 143 MN MN D1608 1555 1555 2.20
LINK ND1 HIS D 145 MN MN D1608 1555 1555 2.25
LINK OD2 ASP D 147 MN MN D1607 1555 1555 2.05
LINK OD2 ASP D 229 MN MN D1607 1555 1555 2.16
LINK OD2 ASP D 229 MN MN D1608 1555 1555 2.29
LINK OD1 ASP D 231 MN MN D1608 1555 1555 2.38
LINK OD2 ASP D 231 MN MN D1608 1555 1555 2.10
LINK ND1 HIS E 121 MN MN E1609 1555 1555 2.11
LINK OD2 ASP E 143 MN MN E1609 1555 1555 2.12
LINK OD1 ASP E 143 MN MN E1610 1555 1555 2.21
LINK ND1 HIS E 145 MN MN E1610 1555 1555 2.30
LINK OD2 ASP E 147 MN MN E1609 1555 1555 2.12
LINK OD2 ASP E 229 MN MN E1609 1555 1555 2.18
LINK OD2 ASP E 229 MN MN E1610 1555 1555 2.22
LINK OD1 ASP E 231 MN MN E1610 1555 1555 2.35
LINK OD2 ASP E 231 MN MN E1610 1555 1555 2.22
LINK ND1 HIS F 121 MN MN F1611 1555 1555 2.04
LINK OD2 ASP F 143 MN MN F1611 1555 1555 2.08
LINK OD1 ASP F 143 MN MN F1612 1555 1555 2.24
LINK ND1 HIS F 145 MN MN F1612 1555 1555 2.37
LINK OD2 ASP F 147 MN MN F1611 1555 1555 2.11
LINK OD2 ASP F 229 MN MN F1611 1555 1555 2.24
LINK OD2 ASP F 229 MN MN F1612 1555 1555 2.25
LINK OD1 ASP F 231 MN MN F1612 1555 1555 2.30
LINK OD2 ASP F 231 MN MN F1612 1555 1555 2.20
CISPEP 1 PRO A 64 PRO A 65 0 -0.28
CISPEP 2 GLY A 118 GLY A 119 0 1.10
CISPEP 3 PRO B 64 PRO B 65 0 -0.49
CISPEP 4 GLY B 118 GLY B 119 0 0.51
CISPEP 5 PRO C 64 PRO C 65 0 -0.29
CISPEP 6 GLY C 118 GLY C 119 0 0.36
CISPEP 7 PRO D 64 PRO D 65 0 -0.17
CISPEP 8 GLY D 118 GLY D 119 0 0.67
CISPEP 9 PRO E 64 PRO E 65 0 -0.34
CISPEP 10 GLY E 118 GLY E 119 0 0.61
CISPEP 11 PRO F 64 PRO F 65 0 -0.27
CISPEP 12 GLY F 118 GLY F 119 0 0.44
SITE 1 AC1 6 HIS A 121 ASP A 143 ASP A 147 ASP A 229
SITE 2 AC1 6 16D A1401 MN A1602
SITE 1 AC2 6 ASP A 143 HIS A 145 ASP A 229 ASP A 231
SITE 2 AC2 6 16D A1401 MN A1601
SITE 1 AC3 6 HIS B 121 ASP B 143 ASP B 147 ASP B 229
SITE 2 AC3 6 16D B1402 MN B1604
SITE 1 AC4 6 ASP B 143 HIS B 145 ASP B 229 ASP B 231
SITE 2 AC4 6 16D B1402 MN B1603
SITE 1 AC5 6 HIS C 121 ASP C 143 ASP C 147 ASP C 229
SITE 2 AC5 6 16D C1403 MN C1606
SITE 1 AC6 6 ASP C 143 HIS C 145 ASP C 229 ASP C 231
SITE 2 AC6 6 16D C1403 MN C1605
SITE 1 AC7 6 HIS D 121 ASP D 143 ASP D 147 ASP D 229
SITE 2 AC7 6 16D D1404 MN D1608
SITE 1 AC8 6 ASP D 143 HIS D 145 ASP D 229 ASP D 231
SITE 2 AC8 6 16D D1404 MN D1607
SITE 1 AC9 6 HIS E 121 ASP E 143 ASP E 147 ASP E 229
SITE 2 AC9 6 16D E1405 MN E1610
SITE 1 BC1 6 ASP E 143 HIS E 145 ASP E 229 ASP E 231
SITE 2 BC1 6 16D E1405 MN E1609
SITE 1 BC2 6 HIS F 121 ASP F 143 ASP F 147 ASP F 229
SITE 2 BC2 6 16D F1406 MN F1612
SITE 1 BC3 6 ASP F 143 HIS F 145 ASP F 229 ASP F 231
SITE 2 BC3 6 16D F1406 MN F1611
SITE 1 BC4 11 HIS A 145 ASP A 147 ASN A 159 SER A 160
SITE 2 BC4 11 ASP A 229 ASP A 231 MN A1601 MN A1602
SITE 3 BC4 11 HOH A1620 HOH A1672 HOH A1680
SITE 1 BC5 11 HIS B 145 ASP B 147 ASN B 159 SER B 160
SITE 2 BC5 11 ASP B 229 ASP B 231 MN B1603 MN B1604
SITE 3 BC5 11 HOH B1605 HOH B1636 HOH B1723
SITE 1 BC6 11 HIS C 145 ASP C 147 ASN C 159 SER C 160
SITE 2 BC6 11 ASP C 229 ASP C 231 MN C1605 MN C1606
SITE 3 BC6 11 HOH C1629 HOH C1686 HOH C1712
SITE 1 BC7 11 HIS D 145 ASP D 147 ASN D 159 SER D 160
SITE 2 BC7 11 ASP D 229 ASP D 231 MN D1607 MN D1608
SITE 3 BC7 11 HOH D1611 HOH D1654 HOH D1675
SITE 1 BC8 10 HIS E 145 ASP E 147 ASN E 159 SER E 160
SITE 2 BC8 10 ASP E 229 ASP E 231 MN E1609 MN E1610
SITE 3 BC8 10 HOH E1679 HOH E1689
SITE 1 BC9 10 HIS F 145 ASP F 147 ASN F 159 SER F 160
SITE 2 BC9 10 ASP F 229 ASP F 231 MN F1611 MN F1612
SITE 3 BC9 10 HOH F1654 HOH F1670
CRYST1 81.769 131.436 168.854 90.00 90.00 90.00 P 21 21 21 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 0.012230 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007608 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005922 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
