HEADER HYDROLASE 07-JAN-05 2BH3
TITLE ZN SUBSTITUTED E. COLI AMINOPEPTIDASE P IN COMPLEX WITH PRODUCT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: XAA-PRO AMINOPEPTIDASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: AMINOPEPTIDASE P, X-PRO AMINOPEPTIDASE, APP-II,
COMPND 5 AMINOPEPTIDASE P II, AMINOACYLPROLINE AMINOPEPTIDASE;
COMPND 6 EC: 3.4.11.9;
COMPND 7 ENGINEERED: YES;
COMPND 8 OTHER_DETAILS: DIPEPTIDE PRODUCT OF AMINOPEPTIDASE P (FORMED BY
COMPND 9 CLEVAGE OF XAA-PRO-LEU TRIPEPTIDE SUBSTRATE)
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 STRAIN: AN1459;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: AN1459;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PPL670
KEYWDS HYDROLASE, PROLINE-SPECIFIC PEPTIDASE, PRODUCT COMPLEX,
KEYWDS 2 METALLOENZYME, PITA-BREAD FOLD, DINUCLEAR HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.C.GRAHAM,C.S.BOND,H.C.FREEMAN,J.M.GUSS
REVDAT 7 13-DEC-23 2BH3 1 REMARK LINK
REVDAT 6 15-MAY-19 2BH3 1 REMARK
REVDAT 5 20-JUN-18 2BH3 1 JRNL REMARK LINK
REVDAT 4 13-JUL-11 2BH3 1 VERSN
REVDAT 3 24-FEB-09 2BH3 1 VERSN
REVDAT 2 26-OCT-05 2BH3 1 JRNL
REVDAT 1 29-SEP-05 2BH3 0
JRNL AUTH S.C.GRAHAM,C.S.BOND,H.C.FREEMAN,J.M.GUSS
JRNL TITL STRUCTURAL AND FUNCTIONAL IMPLICATIONS OF METAL ION
JRNL TITL 2 SELECTION IN AMINOPEPTIDASE P, A METALLOPROTEASE WITH A
JRNL TITL 3 DINUCLEAR METAL CENTER.
JRNL REF BIOCHEMISTRY V. 44 13820 2005
JRNL REFN ISSN 0006-2960
JRNL PMID 16229471
JRNL DOI 10.1021/BI0512849
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 60.19
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 41151
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) : 0.175
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.201
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2099
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2996
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2580
REMARK 3 BIN FREE R VALUE SET COUNT : 138
REMARK 3 BIN FREE R VALUE : 0.2970
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3487
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 34
REMARK 3 SOLVENT ATOMS : 146
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 55.02
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.17
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.58000
REMARK 3 B22 (A**2) : 1.58000
REMARK 3 B33 (A**2) : -3.16000
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): 0.159
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.147
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.104
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.434
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.954
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3614 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 3293 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4902 ; 1.117 ; 1.961
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7608 ; 0.755 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 440 ; 6.055 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 185 ;36.372 ;23.351
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 612 ;12.067 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 36 ;16.164 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 533 ; 0.063 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4059 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 761 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 667 ; 0.193 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 3280 ; 0.170 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1712 ; 0.169 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 2106 ; 0.081 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 150 ; 0.117 ; 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): 6 ; 0.245 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 67 ; 0.269 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 21 ; 0.133 ; 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): 2389 ; 1.131 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3541 ; 1.542 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1538 ; 2.522 ; 4.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1358 ; 3.879 ; 6.000
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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 172
REMARK 3 ORIGIN FOR THE GROUP (A): 19.9118 71.1196 69.2662
REMARK 3 T TENSOR
REMARK 3 T11: -0.0359 T22: -0.0101
REMARK 3 T33: -0.0768 T12: -0.0731
REMARK 3 T13: 0.0127 T23: -0.0637
REMARK 3 L TENSOR
REMARK 3 L11: 0.8971 L22: 1.8156
REMARK 3 L33: 0.7146 L12: -0.5130
REMARK 3 L13: -0.2340 L23: -0.0113
REMARK 3 S TENSOR
REMARK 3 S11: -0.0241 S12: -0.2233 S13: 0.0343
REMARK 3 S21: 0.2351 S22: 0.0675 S23: 0.0130
REMARK 3 S31: -0.0234 S32: 0.0652 S33: -0.0434
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 173 A 440
REMARK 3 ORIGIN FOR THE GROUP (A): 35.7273 53.1088 40.9022
REMARK 3 T TENSOR
REMARK 3 T11: -0.0738 T22: -0.0094
REMARK 3 T33: -0.0793 T12: -0.0398
REMARK 3 T13: 0.0259 T23: -0.0211
REMARK 3 L TENSOR
REMARK 3 L11: 0.5584 L22: 1.2590
REMARK 3 L33: 1.0649 L12: -0.0809
REMARK 3 L13: -0.0937 L23: 0.3830
REMARK 3 S TENSOR
REMARK 3 S11: 0.0353 S12: 0.0114 S13: 0.1029
REMARK 3 S21: -0.1567 S22: 0.0570 S23: -0.1711
REMARK 3 S31: -0.0235 S32: 0.1564 S33: -0.0922
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. SUFFICIENT DENSITY WAS NOT PRESENT FOR COMPLETE
REMARK 3 MODELLING OF RESIDUES A439 OR A440
REMARK 4
REMARK 4 2BH3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-JAN-05.
REMARK 100 THE DEPOSITION ID IS D_1290022310.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-DEC-04
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.00
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 RU200H
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : OSMIC MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43466
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 60.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 6.100
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.5
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 0.52000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1N51 STRIPPED OF MULTIPLE CONFORMERS,
REMARK 200 SOLVENT ATOMS AND HETERO COMPOUNDS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 76.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMINOPEPTIDASE P WAS DIALYSED AGAINST
REMARK 280 EGTA PRIOR TO CRYSTALLISATION. CRYSTALS WERE GROWN IN 26% MPD,
REMARK 280 100 MM NACITRATE (PH 7.0) AND 200 MM MGACETATE AT 4C. CRYSTALS
REMARK 280 WERE SOAKED FOR 2 HOURS IN RESERVOIR SOLUTION SUPPLEMENTED WITH
REMARK 280 1 MM ZNCL2 AND 10 MM PROLEU DIPEPTIDE PRIOR TO DATA COLLECTION.,
REMARK 280 PH 7.00, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 3555 -Y,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X,Z+3/4
REMARK 290 5555 -X+1/2,Y,-Z+3/4
REMARK 290 6555 X,-Y+1/2,-Z+1/4
REMARK 290 7555 Y+1/2,X+1/2,-Z+1/2
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 X+1/2,Y+1/2,Z+1/2
REMARK 290 10555 -X,-Y,Z
REMARK 290 11555 -Y+1/2,X,Z+3/4
REMARK 290 12555 Y,-X+1/2,Z+1/4
REMARK 290 13555 -X,Y+1/2,-Z+1/4
REMARK 290 14555 X+1/2,-Y,-Z+3/4
REMARK 290 15555 Y,X,-Z
REMARK 290 16555 -Y+1/2,-X+1/2,-Z+1/2
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 69.00600
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 69.00600
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 115.36700
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 69.00600
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 57.68350
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 69.00600
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 173.05050
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 69.00600
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 173.05050
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 69.00600
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 57.68350
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 69.00600
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 69.00600
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 115.36700
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 SMTRY1 9 1.000000 0.000000 0.000000 69.00600
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 69.00600
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 115.36700
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 69.00600
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 173.05050
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 69.00600
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 57.68350
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 69.00600
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 57.68350
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 69.00600
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 173.05050
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 69.00600
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 69.00600
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 115.36700
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: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 0.000000 -1.000000 0.000000 69.00600
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 69.00600
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 115.36700
REMARK 350 BIOMT1 3 0.000000 1.000000 0.000000 -69.00600
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 69.00600
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 115.36700
REMARK 350 BIOMT1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 138.01200
REMARK 350 BIOMT3 4 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 A2027 LIES ON A SPECIAL POSITION.
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 439 CG CD CE NZ
REMARK 470 GLN A 440 C O CB CG CD OE1 NE2
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 C PRO A 501 N LEU A 502 1.33
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 ALA A 37 -123.04 52.41
REMARK 500 THR A 53 -35.72 -133.49
REMARK 500 HIS A 243 51.39 -113.93
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 PRO A 501
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 ZN A1008 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 243 NE2
REMARK 620 2 HIS A 361 NE2 135.3
REMARK 620 3 PRO A 501 N 90.4 115.6
REMARK 620 4 PRO A 501 O 76.2 80.9 68.0
REMARK 620 5 HOH A2146 O 116.9 95.4 98.8 162.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1001 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 260 OD1
REMARK 620 2 ASP A 260 OD2 54.5
REMARK 620 3 ASP A 271 OD1 93.6 147.7
REMARK 620 4 GLU A 406 OE1 107.6 99.6 95.0
REMARK 620 5 HOH A2145 O 133.5 85.5 120.0 100.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1002 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 271 OD2
REMARK 620 2 HIS A 354 NE2 90.7
REMARK 620 3 GLU A 383 OE2 161.3 87.1
REMARK 620 4 GLU A 406 OE2 82.6 135.4 85.9
REMARK 620 5 HOH A2145 O 99.0 122.0 97.9 102.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1003 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A2087 O
REMARK 620 2 HOH A2089 O 91.4
REMARK 620 3 HOH A2091 O 91.3 89.1
REMARK 620 4 HOH A2131 O 176.6 89.2 92.0
REMARK 620 5 HOH A2132 O 89.5 178.8 90.0 90.0
REMARK 620 6 HOH A2133 O 87.1 91.5 178.4 89.5 89.5
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLC A1005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A1007
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A1008
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PRO A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LEU A 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1A16 RELATED DB: PDB
REMARK 900 AMINOPEPTIDASE P FROM E. COLI WITH THE INHIBITOR PRO-LEU
REMARK 900 RELATED ID: 1JAW RELATED DB: PDB
REMARK 900 AMINOPEPTIDASE P FROM E. COLI LOW PH FORM
REMARK 900 RELATED ID: 1M35 RELATED DB: PDB
REMARK 900 AMINOPEPTIDASE P FROM ESCHERICHIA COLI
REMARK 900 RELATED ID: 1N51 RELATED DB: PDB
REMARK 900 AMINOPEPTIDASE P IN COMPLEX WITH THE INHIBITOR APSTATIN
REMARK 900 RELATED ID: 1W2M RELATED DB: PDB
REMARK 900 CA-SUBSTITUTED FORM OF E. COLI AMINOPEPTIDASE P
REMARK 900 RELATED ID: 1W7V RELATED DB: PDB
REMARK 900 ZNMG SUBSTRITUTED AMINOPEPTIDASE P FROM E. COLI
REMARK 900 RELATED ID: 1WBQ RELATED DB: PDB
REMARK 900 ZNMG SUBSTITUTED AMINOPEPTIDASE P FROM E. COLI
REMARK 900 RELATED ID: 1WL6 RELATED DB: PDB
REMARK 900 MG-SUBSTITUTED FORM OF E. COLI AMINOPEPTIDASE P
REMARK 900 RELATED ID: 1WL9 RELATED DB: PDB
REMARK 900 STRUCTURE OF AMINOPEPTIDASE P FROM E. COLI
REMARK 900 RELATED ID: 1WLR RELATED DB: PDB
REMARK 900 APO AMINOPEPTIDASE P FROM E. COLI
REMARK 900 RELATED ID: 2BHA RELATED DB: PDB
REMARK 900 E. COLI AMINOPEPTIDASE P IN COMPLEX WITH SUBSTRATE
REMARK 900 RELATED ID: 2BHB RELATED DB: PDB
REMARK 900 ZN SUBSTITUTED E. COLI AMINOPEPTIDASE P
REMARK 900 RELATED ID: 2BHC RELATED DB: PDB
REMARK 900 NA SUBSTITUTED E. COLI AMINOPEPTIDASE P
REMARK 900 RELATED ID: 2BHD RELATED DB: PDB
REMARK 900 MG SUBSTITUTED E. COLI AMINOPEPTIDASE P IN COMPLEX WITH A PRODUCT-
REMARK 900 LIKE INHIBITOR
REMARK 900 RELATED ID: 2BN7 RELATED DB: PDB
REMARK 900 MN SUBSTITUTED E. COLI AMINOPEPTIDASE P IN COMPLEX WITH PRODUCT AND
REMARK 900 ZN
REMARK 900 RELATED ID: 2BWS RELATED DB: PDB
REMARK 900 HIS243ALA E. COLI AMINOPEPTIDASE P
REMARK 900 RELATED ID: 2BWT RELATED DB: PDB
REMARK 900 ASP260ALA E. COLI AMINOPEPTIDASE P
REMARK 900 RELATED ID: 2BWU RELATED DB: PDB
REMARK 900 ASP271ALA E. COLI AMINOPEPTIDASE P
REMARK 900 RELATED ID: 2BWV RELATED DB: PDB
REMARK 900 HIS361ALA E. COLI AMINOPEPTIDASE P
REMARK 900 RELATED ID: 2BWW RELATED DB: PDB
REMARK 900 HIS350ALA E. COLI AMINOPEPTIDASE P
REMARK 900 RELATED ID: 2BWX RELATED DB: PDB
REMARK 900 HIS354ALA E. COLI AMINOPEPTIDASE P
REMARK 900 RELATED ID: 2BWY RELATED DB: PDB
REMARK 900 GLU383ALA E. COLI AMINOPEPTIDASE P
DBREF 2BH3 A 1 440 UNP P15034 AMPP_ECOLI 1 440
SEQRES 1 A 440 SER GLU ILE SER ARG GLN GLU PHE GLN ARG ARG ARG GLN
SEQRES 2 A 440 ALA LEU VAL GLU GLN MET GLN PRO GLY SER ALA ALA LEU
SEQRES 3 A 440 ILE PHE ALA ALA PRO GLU VAL THR ARG SER ALA ASP SER
SEQRES 4 A 440 GLU TYR PRO TYR ARG GLN ASN SER ASP PHE TRP TYR PHE
SEQRES 5 A 440 THR GLY PHE ASN GLU PRO GLU ALA VAL LEU VAL LEU ILE
SEQRES 6 A 440 LYS SER ASP ASP THR HIS ASN HIS SER VAL LEU PHE ASN
SEQRES 7 A 440 ARG VAL ARG ASP LEU THR ALA GLU ILE TRP PHE GLY ARG
SEQRES 8 A 440 ARG LEU GLY GLN ASP ALA ALA PRO GLU LYS LEU GLY VAL
SEQRES 9 A 440 ASP ARG ALA LEU ALA PHE SER GLU ILE ASN GLN GLN LEU
SEQRES 10 A 440 TYR GLN LEU LEU ASN GLY LEU ASP VAL VAL TYR HIS ALA
SEQRES 11 A 440 GLN GLY GLU TYR ALA TYR ALA ASP VAL ILE VAL ASN SER
SEQRES 12 A 440 ALA LEU GLU LYS LEU ARG LYS GLY SER ARG GLN ASN LEU
SEQRES 13 A 440 THR ALA PRO ALA THR MET ILE ASP TRP ARG PRO VAL VAL
SEQRES 14 A 440 HIS GLU MET ARG LEU PHE LYS SER PRO GLU GLU ILE ALA
SEQRES 15 A 440 VAL LEU ARG ARG ALA GLY GLU ILE THR ALA MET ALA HIS
SEQRES 16 A 440 THR ARG ALA MET GLU LYS CYS ARG PRO GLY MET PHE GLU
SEQRES 17 A 440 TYR HIS LEU GLU GLY GLU ILE HIS HIS GLU PHE ASN ARG
SEQRES 18 A 440 HIS GLY ALA ARG TYR PRO SER TYR ASN THR ILE VAL GLY
SEQRES 19 A 440 SER GLY GLU ASN GLY CYS ILE LEU HIS TYR THR GLU ASN
SEQRES 20 A 440 GLU CYS GLU MET ARG ASP GLY ASP LEU VAL LEU ILE ASP
SEQRES 21 A 440 ALA GLY CYS GLU TYR LYS GLY TYR ALA GLY ASP ILE THR
SEQRES 22 A 440 ARG THR PHE PRO VAL ASN GLY LYS PHE THR GLN ALA GLN
SEQRES 23 A 440 ARG GLU ILE TYR ASP ILE VAL LEU GLU SER LEU GLU THR
SEQRES 24 A 440 SER LEU ARG LEU TYR ARG PRO GLY THR SER ILE LEU GLU
SEQRES 25 A 440 VAL THR GLY GLU VAL VAL ARG ILE MET VAL SER GLY LEU
SEQRES 26 A 440 VAL LYS LEU GLY ILE LEU LYS GLY ASP VAL ASP GLU LEU
SEQRES 27 A 440 ILE ALA GLN ASN ALA HIS ARG PRO PHE PHE MET HIS GLY
SEQRES 28 A 440 LEU SER HIS TRP LEU GLY LEU ASP VAL HIS ASP VAL GLY
SEQRES 29 A 440 VAL TYR GLY GLN ASP ARG SER ARG ILE LEU GLU PRO GLY
SEQRES 30 A 440 MET VAL LEU THR VAL GLU PRO GLY LEU TYR ILE ALA PRO
SEQRES 31 A 440 ASP ALA GLU VAL PRO GLU GLN TYR ARG GLY ILE GLY ILE
SEQRES 32 A 440 ARG ILE GLU ASP ASP ILE VAL ILE THR GLU THR GLY ASN
SEQRES 33 A 440 GLU ASN LEU THR ALA SER VAL VAL LYS LYS PRO GLU GLU
SEQRES 34 A 440 ILE GLU ALA LEU MET VAL ALA ALA ARG LYS GLN
HET PRO A 501 7
HET LEU A 502 9
HET ZN A1001 1
HET ZN A1002 1
HET MG A1003 1
HET FLC A1005 13
HET ZN A1007 1
HET ZN A1008 1
HETNAM PRO PROLINE
HETNAM LEU LEUCINE
HETNAM ZN ZINC ION
HETNAM MG MAGNESIUM ION
HETNAM FLC CITRATE ANION
FORMUL 2 PRO C5 H9 N O2
FORMUL 3 LEU C6 H13 N O2
FORMUL 4 ZN 4(ZN 2+)
FORMUL 6 MG MG 2+
FORMUL 7 FLC C6 H5 O7 3-
FORMUL 10 HOH *146(H2 O)
HELIX 1 1 SER A 4 MET A 19 1 16
HELIX 2 2 ASN A 46 GLY A 54 1 9
HELIX 3 3 ASP A 82 GLY A 90 1 9
HELIX 4 4 ALA A 97 GLY A 103 1 7
HELIX 5 5 GLU A 112 ASN A 122 1 11
HELIX 6 6 TYR A 134 GLY A 151 1 18
HELIX 7 7 SER A 152 ASN A 155 5 4
HELIX 8 8 TRP A 165 PHE A 175 1 11
HELIX 9 9 SER A 177 CYS A 202 1 26
HELIX 10 10 PHE A 207 HIS A 222 1 16
HELIX 11 11 GLU A 237 ILE A 241 5 5
HELIX 12 12 THR A 283 TYR A 304 1 22
HELIX 13 13 SER A 309 LEU A 328 1 20
HELIX 14 14 ASP A 334 GLN A 341 1 8
HELIX 15 15 GLY A 367 SER A 371 5 5
HELIX 16 16 PRO A 395 ARG A 399 5 5
HELIX 17 17 LYS A 426 LYS A 439 1 14
SHEET 1 AA 6 ARG A 106 ALA A 109 0
SHEET 2 AA 6 ASN A 72 ASN A 78 1 O SER A 74 N ARG A 106
SHEET 3 AA 6 VAL A 61 LYS A 66 -1 O VAL A 61 N PHE A 77
SHEET 4 AA 6 SER A 23 PHE A 28 -1 O SER A 23 N LYS A 66
SHEET 5 AA 6 VAL A 126 HIS A 129 1 O VAL A 126 N ALA A 24
SHEET 6 AA 6 THR A 161 ILE A 163 1 O THR A 161 N VAL A 127
SHEET 1 AB 2 THR A 34 SER A 36 0
SHEET 2 AB 2 SER A 39 GLU A 40 -1 O SER A 39 N ARG A 35
SHEET 1 AC 3 TYR A 226 PRO A 227 0
SHEET 2 AC 3 CYS A 263 TYR A 265 -1 O GLU A 264 N TYR A 226
SHEET 3 AC 3 TYR A 268 ALA A 269 -1 O TYR A 268 N TYR A 265
SHEET 1 AD 3 ILE A 232 SER A 235 0
SHEET 2 AD 3 LEU A 256 ALA A 261 -1 O LEU A 258 N GLY A 234
SHEET 3 AD 3 ILE A 272 PRO A 277 -1 O ILE A 272 N ALA A 261
SHEET 1 AE 3 VAL A 379 VAL A 382 0
SHEET 2 AE 3 ASP A 407 ILE A 411 -1 O ASP A 407 N VAL A 382
SHEET 3 AE 3 ASN A 416 ASN A 418 -1 O GLU A 417 N VAL A 410
SHEET 1 AF 2 GLY A 385 ILE A 388 0
SHEET 2 AF 2 ILE A 401 ARG A 404 -1 O ILE A 401 N ILE A 388
LINK NE2 HIS A 71 ZN ZN A1007 1555 1555 2.01
LINK NE2 HIS A 243 ZN ZN A1008 1555 1555 2.59
LINK OD1 ASP A 260 ZN ZN A1001 1555 1555 2.07
LINK OD2 ASP A 260 ZN ZN A1001 1555 1555 2.58
LINK OD1 ASP A 271 ZN ZN A1001 1555 1555 2.10
LINK OD2 ASP A 271 ZN ZN A1002 1555 1555 2.22
LINK NE2 HIS A 354 ZN ZN A1002 1555 1555 2.13
LINK NE2 HIS A 361 ZN ZN A1008 1555 1555 2.47
LINK OE2 GLU A 383 ZN ZN A1002 1555 1555 2.25
LINK OE1 GLU A 406 ZN ZN A1001 1555 1555 2.14
LINK OE2 GLU A 406 ZN ZN A1002 1555 1555 2.18
LINK N PRO A 501 ZN ZN A1008 1555 1555 2.48
LINK O PRO A 501 ZN ZN A1008 1555 1555 2.61
LINK ZN ZN A1001 O HOH A2145 1555 1555 1.97
LINK ZN ZN A1002 O HOH A2145 1555 1555 2.12
LINK MG MG A1003 O HOH A2087 1555 6555 2.16
LINK MG MG A1003 O HOH A2089 1555 6555 2.17
LINK MG MG A1003 O HOH A2091 1555 6555 2.18
LINK MG MG A1003 O HOH A2131 1555 1555 2.18
LINK MG MG A1003 O HOH A2132 1555 1555 2.18
LINK MG MG A1003 O HOH A2133 1555 1555 2.19
LINK ZN ZN A1008 O HOH A2146 1555 1555 2.57
SITE 1 AC1 7 TYR A 229 ASP A 260 ASP A 271 THR A 273
SITE 2 AC1 7 GLU A 406 ZN A1002 HOH A2145
SITE 1 AC2 7 ASP A 271 HIS A 354 THR A 381 GLU A 383
SITE 2 AC2 7 GLU A 406 ZN A1001 HOH A2145
SITE 1 AC3 4 ARG A 186 MET A 193 ARG A 221 HIS A 222
SITE 1 AC4 1 HIS A 71
SITE 1 AC5 4 HIS A 243 HIS A 361 PRO A 501 HOH A2146
SITE 1 AC6 7 ARG A 399 HOH A2087 HOH A2089 HOH A2091
SITE 2 AC6 7 HOH A2131 HOH A2132 HOH A2133
SITE 1 AC7 9 HIS A 243 ASP A 260 HIS A 350 HIS A 361
SITE 2 AC7 9 GLU A 383 ARG A 404 LEU A 502 ZN A1008
SITE 3 AC7 9 HOH A2145
SITE 1 AC8 7 TRP A 88 ARG A 153 GLY A 351 TYR A 366
SITE 2 AC8 7 ARG A 370 PRO A 501 HOH A2117
CRYST1 138.012 138.012 230.734 90.00 90.00 90.00 I 41 2 2 16
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 0.007246 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007246 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004334 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
