HEADER OXIDOREDUCTASE 30-JUN-10 3AK2
TITLE SUPEROXIDE DISMUTASE FROM AEROPYRUM PERNIX K1, MN-BOUND FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUPEROXIDE DISMUTASE [MN/FE];
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 1.15.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AEROPYRUM PERNIX;
SOURCE 3 ORGANISM_TAXID: 272557;
SOURCE 4 STRAIN: K1;
SOURCE 5 GENE: APE0741;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET11
KEYWDS SUPEROXIDE DISMUTASE, CAMBIALISTIC, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.NAKAMURA,K.UEGAKI
REVDAT 3 01-NOV-23 3AK2 1 REMARK LINK
REVDAT 2 23-FEB-11 3AK2 1 JRNL
REVDAT 1 02-FEB-11 3AK2 0
JRNL AUTH T.NAKAMURA,K.TORIKAI,K.UEGAKI,J.MORITA,K.MACHIDA,A.SUZUKI,
JRNL AUTH 2 Y.KAWATA
JRNL TITL CRYSTAL STRUCTURE OF THE CAMBIALISTIC SUPEROXIDE DISMUTASE
JRNL TITL 2 FROM AEROPYRUM PERNIX K1 - INSIGHTS INTO THE ENZYME
JRNL TITL 3 MECHANISM AND STABILITY
JRNL REF FEBS J. V. 278 598 2011
JRNL REFN ISSN 1742-464X
JRNL PMID 21182595
JRNL DOI 10.1111/J.1742-4658.2010.07977.X
REMARK 2
REMARK 2 RESOLUTION. 1.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.86
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 152991
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 + TEST SET) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 8101
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.35
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.38
REMARK 3 REFLECTION IN BIN (WORKING SET) : 10838
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.90
REMARK 3 BIN R VALUE (WORKING SET) : 0.2390
REMARK 3 BIN FREE R VALUE SET COUNT : 594
REMARK 3 BIN FREE R VALUE : 0.2540
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6823
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 76
REMARK 3 SOLVENT ATOMS : 734
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.81
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.12
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.065
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.063
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.037
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.861
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.955
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7081 ; 0.006 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9575 ; 1.052 ; 1.943
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 835 ; 5.927 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 343 ;35.790 ;24.315
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1173 ;10.768 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;14.129 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 993 ; 0.078 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5417 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3811 ; 0.186 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4864 ; 0.306 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 680 ; 0.116 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 37 ; 0.164 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 48 ; 0.100 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 4311 ; 0.598 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6714 ; 0.672 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3252 ; 1.144 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2861 ; 1.778 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3AK2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-JUL-10.
REMARK 100 THE DEPOSITION ID IS D_1000029348.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-FEB-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL44XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-225
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 161154
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.350
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 (%) : 98.0
REMARK 200 DATA REDUNDANCY : 7.300
REMARK 200 R MERGE (I) : 0.04800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.90
REMARK 200 R MERGE FOR SHELL (I) : 0.36100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: PDB ENTRY 3AK1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM HEPES, 8% PEG 6000, 8% ETHYLENE
REMARK 280 GLYCOL, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 35.89100
REMARK 290 SMTRY3 2 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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15510 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -80.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 LEU A 212
REMARK 465 PRO A 213
REMARK 465 GLN A 214
REMARK 465 MET B 1
REMARK 465 VAL B 2
REMARK 465 SER B 3
REMARK 465 PHE B 4
REMARK 465 GLN B 214
REMARK 465 LEU C 211
REMARK 465 LEU C 212
REMARK 465 PRO C 213
REMARK 465 GLN C 214
REMARK 465 MET D 1
REMARK 465 LEU D 211
REMARK 465 LEU D 212
REMARK 465 PRO D 213
REMARK 465 GLN D 214
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 O LYS D 49 O HOH D 416 1.84
REMARK 500 O HOH C 255 O HOH C 592 2.07
REMARK 500 O HOH A 248 O HOH C 541 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 LYS A 34 -61.21 -101.56
REMARK 500 LYS A 149 -126.93 47.10
REMARK 500 ASN A 151 30.89 -148.23
REMARK 500 LEU A 153 -13.66 80.79
REMARK 500 TYR A 171 -17.84 -145.18
REMARK 500 LYS A 176 -133.34 53.81
REMARK 500 LYS B 34 -64.09 -104.88
REMARK 500 LYS B 149 -129.63 50.94
REMARK 500 ASN B 151 30.38 -147.42
REMARK 500 LEU B 153 -14.06 81.93
REMARK 500 TYR B 171 -17.69 -145.67
REMARK 500 LYS B 176 -135.51 54.75
REMARK 500 LYS C 34 -62.19 -98.60
REMARK 500 LYS C 149 -125.78 47.73
REMARK 500 ASN C 151 31.66 -145.72
REMARK 500 LEU C 153 -12.64 81.35
REMARK 500 TYR C 171 -17.33 -145.58
REMARK 500 LYS C 176 -132.83 54.49
REMARK 500 LYS D 34 -62.57 -100.56
REMARK 500 LYS D 149 -126.82 51.14
REMARK 500 ASN D 151 30.36 -147.77
REMARK 500 LEU D 153 -14.30 80.90
REMARK 500 TYR D 171 -17.38 -143.95
REMARK 500 LYS D 176 -134.11 55.52
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 215 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 31 NE2
REMARK 620 2 HIS A 79 NE2 90.7
REMARK 620 3 ASP A 165 OD2 82.8 106.6
REMARK 620 4 HIS A 169 NE2 89.6 135.1 117.9
REMARK 620 5 HOH A 223 O 171.3 92.4 88.5 93.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 215 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 31 NE2
REMARK 620 2 HIS B 79 NE2 90.7
REMARK 620 3 ASP B 165 OD2 82.1 105.2
REMARK 620 4 HIS B 169 NE2 89.8 136.0 118.4
REMARK 620 5 HOH B 221 O 169.0 94.6 87.2 93.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN C 215 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 31 NE2
REMARK 620 2 HIS C 79 NE2 90.4
REMARK 620 3 ASP C 165 OD2 82.4 104.6
REMARK 620 4 HIS C 169 NE2 91.7 137.0 118.2
REMARK 620 5 HOH C 220 O 168.7 94.0 86.4 92.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN D 215 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 31 NE2
REMARK 620 2 HIS D 79 NE2 89.8
REMARK 620 3 ASP D 165 OD2 83.1 103.4
REMARK 620 4 HIS D 169 NE2 90.6 136.5 119.8
REMARK 620 5 HOH D 221 O 171.2 92.1 88.1 93.9
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 215
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 216
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 217
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 218
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 219
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 220
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 215
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 216
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 217
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 218
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 219
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 215
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 216
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 217
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 218
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 219
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN D 215
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 216
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 217
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 218
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 219
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 220
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3AK1 RELATED DB: PDB
REMARK 900 SAME PROTEIN, APO-FORM
REMARK 900 RELATED ID: 3AK3 RELATED DB: PDB
REMARK 900 SAME PROTEIN, FE-BOUND FORM
DBREF 3AK2 A 1 214 UNP Q9Y8H8 SODF_AERPE 1 214
DBREF 3AK2 B 1 214 UNP Q9Y8H8 SODF_AERPE 1 214
DBREF 3AK2 C 1 214 UNP Q9Y8H8 SODF_AERPE 1 214
DBREF 3AK2 D 1 214 UNP Q9Y8H8 SODF_AERPE 1 214
SEQRES 1 A 214 MET VAL SER PHE LYS ARG TYR GLU LEU PRO PRO LEU PRO
SEQRES 2 A 214 TYR ASN TYR ASN ALA LEU GLU PRO TYR ILE ILE GLU GLU
SEQRES 3 A 214 ILE MET LYS LEU HIS HIS GLN LYS HIS HIS ASN THR TYR
SEQRES 4 A 214 VAL LYS GLY ALA ASN ALA ALA LEU GLU LYS ILE GLU LYS
SEQRES 5 A 214 HIS LEU LYS GLY GLU ILE GLN ILE ASP VAL ARG ALA VAL
SEQRES 6 A 214 MET ARG ASP PHE SER PHE ASN TYR ALA GLY HIS ILE MET
SEQRES 7 A 214 HIS THR ILE PHE TRP PRO ASN MET ALA PRO PRO GLY LYS
SEQRES 8 A 214 GLY GLY GLY THR PRO GLY GLY ARG VAL ALA ASP LEU ILE
SEQRES 9 A 214 GLU LYS GLN PHE GLY GLY PHE GLU LYS PHE LYS ALA LEU
SEQRES 10 A 214 PHE SER ALA ALA ALA LYS THR VAL GLU GLY VAL GLY TRP
SEQRES 11 A 214 GLY VAL LEU ALA PHE ASP PRO LEU THR GLU GLU LEU ARG
SEQRES 12 A 214 ILE LEU GLN VAL GLU LYS HIS ASN VAL LEU MET THR ALA
SEQRES 13 A 214 GLY LEU VAL PRO ILE LEU VAL ILE ASP VAL TRP GLU HIS
SEQRES 14 A 214 ALA TYR TYR LEU GLN TYR LYS ASN ASP ARG GLY SER TYR
SEQRES 15 A 214 VAL GLU ASN TRP TRP ASN VAL VAL ASN TRP ASP ASP VAL
SEQRES 16 A 214 GLU LYS ARG LEU GLU GLN ALA LEU ASN ASN ALA LYS PRO
SEQRES 17 A 214 LEU TYR LEU LEU PRO GLN
SEQRES 1 B 214 MET VAL SER PHE LYS ARG TYR GLU LEU PRO PRO LEU PRO
SEQRES 2 B 214 TYR ASN TYR ASN ALA LEU GLU PRO TYR ILE ILE GLU GLU
SEQRES 3 B 214 ILE MET LYS LEU HIS HIS GLN LYS HIS HIS ASN THR TYR
SEQRES 4 B 214 VAL LYS GLY ALA ASN ALA ALA LEU GLU LYS ILE GLU LYS
SEQRES 5 B 214 HIS LEU LYS GLY GLU ILE GLN ILE ASP VAL ARG ALA VAL
SEQRES 6 B 214 MET ARG ASP PHE SER PHE ASN TYR ALA GLY HIS ILE MET
SEQRES 7 B 214 HIS THR ILE PHE TRP PRO ASN MET ALA PRO PRO GLY LYS
SEQRES 8 B 214 GLY GLY GLY THR PRO GLY GLY ARG VAL ALA ASP LEU ILE
SEQRES 9 B 214 GLU LYS GLN PHE GLY GLY PHE GLU LYS PHE LYS ALA LEU
SEQRES 10 B 214 PHE SER ALA ALA ALA LYS THR VAL GLU GLY VAL GLY TRP
SEQRES 11 B 214 GLY VAL LEU ALA PHE ASP PRO LEU THR GLU GLU LEU ARG
SEQRES 12 B 214 ILE LEU GLN VAL GLU LYS HIS ASN VAL LEU MET THR ALA
SEQRES 13 B 214 GLY LEU VAL PRO ILE LEU VAL ILE ASP VAL TRP GLU HIS
SEQRES 14 B 214 ALA TYR TYR LEU GLN TYR LYS ASN ASP ARG GLY SER TYR
SEQRES 15 B 214 VAL GLU ASN TRP TRP ASN VAL VAL ASN TRP ASP ASP VAL
SEQRES 16 B 214 GLU LYS ARG LEU GLU GLN ALA LEU ASN ASN ALA LYS PRO
SEQRES 17 B 214 LEU TYR LEU LEU PRO GLN
SEQRES 1 C 214 MET VAL SER PHE LYS ARG TYR GLU LEU PRO PRO LEU PRO
SEQRES 2 C 214 TYR ASN TYR ASN ALA LEU GLU PRO TYR ILE ILE GLU GLU
SEQRES 3 C 214 ILE MET LYS LEU HIS HIS GLN LYS HIS HIS ASN THR TYR
SEQRES 4 C 214 VAL LYS GLY ALA ASN ALA ALA LEU GLU LYS ILE GLU LYS
SEQRES 5 C 214 HIS LEU LYS GLY GLU ILE GLN ILE ASP VAL ARG ALA VAL
SEQRES 6 C 214 MET ARG ASP PHE SER PHE ASN TYR ALA GLY HIS ILE MET
SEQRES 7 C 214 HIS THR ILE PHE TRP PRO ASN MET ALA PRO PRO GLY LYS
SEQRES 8 C 214 GLY GLY GLY THR PRO GLY GLY ARG VAL ALA ASP LEU ILE
SEQRES 9 C 214 GLU LYS GLN PHE GLY GLY PHE GLU LYS PHE LYS ALA LEU
SEQRES 10 C 214 PHE SER ALA ALA ALA LYS THR VAL GLU GLY VAL GLY TRP
SEQRES 11 C 214 GLY VAL LEU ALA PHE ASP PRO LEU THR GLU GLU LEU ARG
SEQRES 12 C 214 ILE LEU GLN VAL GLU LYS HIS ASN VAL LEU MET THR ALA
SEQRES 13 C 214 GLY LEU VAL PRO ILE LEU VAL ILE ASP VAL TRP GLU HIS
SEQRES 14 C 214 ALA TYR TYR LEU GLN TYR LYS ASN ASP ARG GLY SER TYR
SEQRES 15 C 214 VAL GLU ASN TRP TRP ASN VAL VAL ASN TRP ASP ASP VAL
SEQRES 16 C 214 GLU LYS ARG LEU GLU GLN ALA LEU ASN ASN ALA LYS PRO
SEQRES 17 C 214 LEU TYR LEU LEU PRO GLN
SEQRES 1 D 214 MET VAL SER PHE LYS ARG TYR GLU LEU PRO PRO LEU PRO
SEQRES 2 D 214 TYR ASN TYR ASN ALA LEU GLU PRO TYR ILE ILE GLU GLU
SEQRES 3 D 214 ILE MET LYS LEU HIS HIS GLN LYS HIS HIS ASN THR TYR
SEQRES 4 D 214 VAL LYS GLY ALA ASN ALA ALA LEU GLU LYS ILE GLU LYS
SEQRES 5 D 214 HIS LEU LYS GLY GLU ILE GLN ILE ASP VAL ARG ALA VAL
SEQRES 6 D 214 MET ARG ASP PHE SER PHE ASN TYR ALA GLY HIS ILE MET
SEQRES 7 D 214 HIS THR ILE PHE TRP PRO ASN MET ALA PRO PRO GLY LYS
SEQRES 8 D 214 GLY GLY GLY THR PRO GLY GLY ARG VAL ALA ASP LEU ILE
SEQRES 9 D 214 GLU LYS GLN PHE GLY GLY PHE GLU LYS PHE LYS ALA LEU
SEQRES 10 D 214 PHE SER ALA ALA ALA LYS THR VAL GLU GLY VAL GLY TRP
SEQRES 11 D 214 GLY VAL LEU ALA PHE ASP PRO LEU THR GLU GLU LEU ARG
SEQRES 12 D 214 ILE LEU GLN VAL GLU LYS HIS ASN VAL LEU MET THR ALA
SEQRES 13 D 214 GLY LEU VAL PRO ILE LEU VAL ILE ASP VAL TRP GLU HIS
SEQRES 14 D 214 ALA TYR TYR LEU GLN TYR LYS ASN ASP ARG GLY SER TYR
SEQRES 15 D 214 VAL GLU ASN TRP TRP ASN VAL VAL ASN TRP ASP ASP VAL
SEQRES 16 D 214 GLU LYS ARG LEU GLU GLN ALA LEU ASN ASN ALA LYS PRO
SEQRES 17 D 214 LEU TYR LEU LEU PRO GLN
HET MN A 215 1
HET EDO A 216 4
HET EDO A 217 4
HET EDO A 218 4
HET EDO A 219 4
HET EDO A 220 4
HET MN B 215 1
HET EDO B 216 4
HET EDO B 217 4
HET EDO B 218 4
HET EDO B 219 4
HET MN C 215 1
HET EDO C 216 4
HET EDO C 217 4
HET EDO C 218 4
HET EDO C 219 4
HET MN D 215 1
HET EDO D 216 4
HET EDO D 217 4
HET EDO D 218 4
HET EDO D 219 4
HET EDO D 220 4
HETNAM MN MANGANESE (II) ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 5 MN 4(MN 2+)
FORMUL 6 EDO 18(C2 H6 O2)
FORMUL 27 HOH *734(H2 O)
HELIX 1 1 ILE A 24 LYS A 34 1 11
HELIX 2 2 LYS A 34 LYS A 55 1 22
HELIX 3 3 ASP A 61 TRP A 83 1 23
HELIX 4 4 GLY A 97 GLY A 109 1 13
HELIX 5 5 GLY A 110 THR A 124 1 15
HELIX 6 6 TRP A 167 ALA A 170 5 4
HELIX 7 7 TYR A 171 LYS A 176 1 6
HELIX 8 8 ASP A 178 TRP A 187 1 10
HELIX 9 9 ASN A 188 VAL A 190 5 3
HELIX 10 10 ASN A 191 ALA A 206 1 16
HELIX 11 11 LYS A 207 TYR A 210 5 4
HELIX 12 12 ILE B 24 LYS B 34 1 11
HELIX 13 13 LYS B 34 LYS B 55 1 22
HELIX 14 14 ASP B 61 TRP B 83 1 23
HELIX 15 15 GLY B 97 GLY B 109 1 13
HELIX 16 16 GLY B 110 THR B 124 1 15
HELIX 17 17 TRP B 167 ALA B 170 5 4
HELIX 18 18 TYR B 171 LYS B 176 1 6
HELIX 19 19 ASP B 178 TRP B 187 1 10
HELIX 20 20 ASN B 188 VAL B 190 5 3
HELIX 21 21 ASN B 191 ALA B 206 1 16
HELIX 22 22 LYS B 207 TYR B 210 5 4
HELIX 23 23 ILE C 24 LYS C 34 1 11
HELIX 24 24 LYS C 34 LYS C 55 1 22
HELIX 25 25 ASP C 61 TRP C 83 1 23
HELIX 26 26 GLY C 97 GLY C 109 1 13
HELIX 27 27 GLY C 110 THR C 124 1 15
HELIX 28 28 TRP C 167 ALA C 170 5 4
HELIX 29 29 TYR C 171 LYS C 176 1 6
HELIX 30 30 ASP C 178 TRP C 187 1 10
HELIX 31 31 ASN C 188 VAL C 190 5 3
HELIX 32 32 ASN C 191 TYR C 210 1 20
HELIX 33 33 ILE D 24 LYS D 34 1 11
HELIX 34 34 LYS D 34 LYS D 55 1 22
HELIX 35 35 ASP D 61 TRP D 83 1 23
HELIX 36 36 GLY D 97 GLY D 109 1 13
HELIX 37 37 GLY D 110 THR D 124 1 15
HELIX 38 38 TRP D 167 ALA D 170 5 4
HELIX 39 39 TYR D 171 LYS D 176 1 6
HELIX 40 40 ASP D 178 TRP D 187 1 10
HELIX 41 41 ASN D 188 VAL D 190 5 3
HELIX 42 42 ASN D 191 ALA D 206 1 16
HELIX 43 43 LYS D 207 TYR D 210 5 4
SHEET 1 A 3 GLU A 141 GLU A 148 0
SHEET 2 A 3 GLY A 129 ASP A 136 -1 N ASP A 136 O GLU A 141
SHEET 3 A 3 VAL A 159 ASP A 165 -1 O ILE A 161 N LEU A 133
SHEET 1 B 3 LEU B 142 GLU B 148 0
SHEET 2 B 3 GLY B 129 PHE B 135 -1 N ALA B 134 O ARG B 143
SHEET 3 B 3 VAL B 159 ASP B 165 -1 O LEU B 162 N LEU B 133
SHEET 1 C 3 LEU C 142 GLU C 148 0
SHEET 2 C 3 GLY C 129 PHE C 135 -1 N ALA C 134 O ARG C 143
SHEET 3 C 3 VAL C 159 ASP C 165 -1 O LEU C 162 N LEU C 133
SHEET 1 D 3 LEU D 142 GLU D 148 0
SHEET 2 D 3 GLY D 129 PHE D 135 -1 N ALA D 134 O ARG D 143
SHEET 3 D 3 VAL D 159 ASP D 165 -1 O LEU D 162 N LEU D 133
LINK NE2 HIS A 31 MN MN A 215 1555 1555 2.19
LINK NE2 HIS A 79 MN MN A 215 1555 1555 2.21
LINK OD2 ASP A 165 MN MN A 215 1555 1555 2.03
LINK NE2 HIS A 169 MN MN A 215 1555 1555 2.21
LINK MN MN A 215 O HOH A 223 1555 1555 2.12
LINK NE2 HIS B 31 MN MN B 215 1555 1555 2.18
LINK NE2 HIS B 79 MN MN B 215 1555 1555 2.19
LINK OD2 ASP B 165 MN MN B 215 1555 1555 2.04
LINK NE2 HIS B 169 MN MN B 215 1555 1555 2.27
LINK MN MN B 215 O HOH B 221 1555 1555 2.05
LINK NE2 HIS C 31 MN MN C 215 1555 1555 2.16
LINK NE2 HIS C 79 MN MN C 215 1555 1555 2.20
LINK OD2 ASP C 165 MN MN C 215 1555 1555 2.03
LINK NE2 HIS C 169 MN MN C 215 1555 1555 2.28
LINK MN MN C 215 O HOH C 220 1555 1555 1.99
LINK NE2 HIS D 31 MN MN D 215 1555 1555 2.19
LINK NE2 HIS D 79 MN MN D 215 1555 1555 2.19
LINK OD2 ASP D 165 MN MN D 215 1555 1555 2.08
LINK NE2 HIS D 169 MN MN D 215 1555 1555 2.22
LINK MN MN D 215 O HOH D 221 1555 1555 2.09
CISPEP 1 GLU A 20 PRO A 21 0 3.80
CISPEP 2 GLU B 20 PRO B 21 0 4.00
CISPEP 3 GLU C 20 PRO C 21 0 3.45
CISPEP 4 GLU D 20 PRO D 21 0 4.24
SITE 1 AC1 5 HIS A 31 HIS A 79 ASP A 165 HIS A 169
SITE 2 AC1 5 HOH A 223
SITE 1 AC2 6 GLU A 148 LYS A 149 HOH A 280 HOH A 284
SITE 2 AC2 6 GLU C 148 LYS C 149
SITE 1 AC3 6 PRO A 11 LEU A 12 TYR A 14 TYR A 16
SITE 2 AC3 6 EDO A 220 HOH A 465
SITE 1 AC4 5 HOH A 331 HOH A 371 EDO B 218 EDO C 218
SITE 2 AC4 5 EDO D 220
SITE 1 AC5 5 LYS A 34 HIS A 35 THR A 38 HOH A 488
SITE 2 AC5 5 ASN C 177
SITE 1 AC6 5 LEU A 9 PRO A 10 PRO A 11 HIS A 32
SITE 2 AC6 5 EDO A 217
SITE 1 AC7 5 HIS B 31 HIS B 79 ASP B 165 HIS B 169
SITE 2 AC7 5 HOH B 221
SITE 1 AC8 4 PRO B 21 ASN B 185 HOH B 271 HOH B 533
SITE 1 AC9 5 PRO B 11 LEU B 12 TYR B 14 TYR B 16
SITE 2 AC9 5 HOH B 703
SITE 1 BC1 5 EDO A 218 GLU B 148 LYS B 149 EDO C 218
SITE 2 BC1 5 GLU D 148
SITE 1 BC2 6 HIS B 35 TYR B 39 TRP B 167 GLU D 168
SITE 2 BC2 6 ARG D 179 EDO D 218
SITE 1 BC3 5 HIS C 31 HIS C 79 ASP C 165 HIS C 169
SITE 2 BC3 5 HOH C 220
SITE 1 BC4 7 PRO C 11 LEU C 12 TYR C 16 HIS C 32
SITE 2 BC4 7 HOH C 436 HOH C 570 HOH C 634
SITE 1 BC5 5 GLN C 107 PHE C 108 LEU C 142 ARG C 143
SITE 2 BC5 5 HOH C 251
SITE 1 BC6 10 EDO A 218 HOH A 331 ARG B 67 EDO B 218
SITE 2 BC6 10 ARG C 67 HOH C 255 HOH C 262 HOH C 388
SITE 3 BC6 10 HOH C 672 GLU D 148
SITE 1 BC7 6 TRP A 167 HOH A 488 GLY C 127 GLU C 168
SITE 2 BC7 6 ARG C 179 HOH C 555
SITE 1 BC8 5 HIS D 31 HIS D 79 ASP D 165 HIS D 169
SITE 2 BC8 5 HOH D 221
SITE 1 BC9 5 PRO D 96 GLY D 97 GLY D 98 TRP D 192
SITE 2 BC9 5 GLU D 196
SITE 1 CC1 5 THR C 124 ASP D 61 VAL D 62 ARG D 63
SITE 2 CC1 5 HOH D 258
SITE 1 CC2 5 PHE B 71 EDO B 219 HOH B 316 VAL D 125
SITE 2 CC2 5 GLY D 127
SITE 1 CC3 4 PRO D 11 LEU D 12 TYR D 14 TYR D 16
SITE 1 CC4 9 ARG A 67 EDO A 218 HOH A 371 GLU C 148
SITE 2 CC4 9 ARG D 67 HOH D 237 HOH D 269 HOH D 271
SITE 3 CC4 9 HOH D 403
CRYST1 69.064 71.782 76.853 90.00 91.81 90.00 P 1 21 1 8
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 0.014479 0.000000 0.000457 0.00000
SCALE2 0.000000 0.013931 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013018 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
