HEADER HYDROLASE (PROTEASE) 04-JAN-01 1HI9
TITLE ZN-DEPENDENT D-AMINOPEPTIDASE DPPA FROM BACILLUS SUBTILIS, A SELF-
TITLE 2 COMPARTMENTALIZING PROTEASE.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDE TRANSPORT PROTEIN DPPA;
COMPND 3 CHAIN: A, B, C, D, E;
COMPND 4 SYNONYM: DCIAA;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 STRAIN: 168;
SOURCE 5 CELLULAR_LOCATION: CYTOPLASM;
SOURCE 6 GENE: DCIAA;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: B834(DE3);
SOURCE 10 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_VECTOR: PET22B;
SOURCE 13 OTHER_DETAILS: RECOMBINANT EXPRESSION IN E. COLI
KEYWDS HYDROLASE (PROTEASE), PROTEASE, D-AMINOPEPTIDASE, DECAMER, SELF-
KEYWDS 2 COMPARTMENTALIZING
EXPDTA X-RAY DIFFRACTION
AUTHOR H.REMAUT,C.BOMPARD-GILLES,C.GOFFIN,J.M.FRERE,J.VAN BEEUMEN
REVDAT 3 24-JUL-19 1HI9 1 REMARK
REVDAT 2 24-FEB-09 1HI9 1 VERSN
REVDAT 1 09-AUG-01 1HI9 0
JRNL AUTH H.REMAUT,C.BOMPARD-GILLES,C.GOFFIN,J.M.FRERE,J.VAN BEEUMEN
JRNL TITL STRUCTURE OF THE BACILLUS SUBTILIS D-AMINOPEPTIDASE DPPA
JRNL TITL 2 REVEALS A NOVEL SELF-COMPARTMENTALIZING PROTEASE
JRNL REF NAT.STRUCT.BIOL. V. 8 674 2001
JRNL REFN ISSN 1072-8368
JRNL PMID 11473256
JRNL DOI 10.1038/90380
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.8
REMARK 3 NUMBER OF REFLECTIONS : 49995
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) : 0.232
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2544
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10570
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 247
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 48.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 11.27500
REMARK 3 B22 (A**2) : -11.09400
REMARK 3 B33 (A**2) : -0.18200
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) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.240
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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) : 1.110 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.770 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.800 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.650 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : RESTRAINTS
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: INITIAL REFINEMENT WITH REFMAC DURING
REMARK 3 MODEL BUILDING
REMARK 4
REMARK 4 1HI9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-JAN-01.
REMARK 100 THE DEPOSITION ID IS D_1290005753.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-OCT-99
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : BW7B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8445,1.2832,1.2834
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
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 : 51831
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.403
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 200 DATA REDUNDANCY : 3.480
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.7000
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 (%) : 98.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.24700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: MLPHARE, DM, DM
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: ANOMALOUS SCATERRERS: 2 ZN2+/274AA.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG6000, 100MM TRIS, PH 8.5, 5MM
REMARK 280 NACL, 5MM MGCL2, PH 8.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 54.96500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 54.96500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 72.55500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 82.93000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 72.55500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 82.93000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 54.96500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 72.55500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 82.93000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 54.96500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 72.55500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 82.93000
REMARK 290 SMTRY3 8 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 300 REMARK: THE ENZYME IS A HOMODECAMER WITH 52 POINT
REMARK 300 -GROUP SYMMETRY
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: DECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DECAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E
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 -1.000000 0.000000 0.000000 145.11000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 54.96500
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OE1 GLN D 203 OE1 GLN D 203 3656 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 96 NE - CZ - NH1 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG A 96 NE - CZ - NH2 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG A 192 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG A 192 NE - CZ - NH2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 ARG B 96 NE - CZ - NH1 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG B 96 NE - CZ - NH2 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG B 156 CD - NE - CZ ANGL. DEV. = 8.8 DEGREES
REMARK 500 ARG B 156 NE - CZ - NH1 ANGL. DEV. = -8.4 DEGREES
REMARK 500 ARG B 156 NE - CZ - NH2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 ARG B 192 CD - NE - CZ ANGL. DEV. = 8.9 DEGREES
REMARK 500 ARG B 192 NE - CZ - NH1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 ARG B 192 NE - CZ - NH2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ARG C 96 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG C 96 NE - CZ - NH2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 ARG C 192 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG C 192 NE - CZ - NH2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 ARG D 96 CD - NE - CZ ANGL. DEV. = 8.6 DEGREES
REMARK 500 ARG D 96 NE - CZ - NH1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ARG D 96 NE - CZ - NH2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 ARG D 192 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG D 192 NE - CZ - NH2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 ARG E 96 NE - CZ - NH1 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG E 96 NE - CZ - NH2 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ARG E 192 CD - NE - CZ ANGL. DEV. = 8.9 DEGREES
REMARK 500 ARG E 192 NE - CZ - NH1 ANGL. DEV. = -6.7 DEGREES
REMARK 500 ARG E 192 NE - CZ - NH2 ANGL. DEV. = 6.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 61 -114.22 45.49
REMARK 500 ASP A 81 -169.50 -115.12
REMARK 500 SER A 86 -113.19 37.30
REMARK 500 MET A 117 -63.71 66.87
REMARK 500 ASP A 128 -0.25 69.13
REMARK 500 ASN A 233 1.70 -66.41
REMARK 500 SER B 61 -115.66 47.20
REMARK 500 ASP B 81 -167.69 -113.11
REMARK 500 SER B 86 -111.91 33.94
REMARK 500 MET B 117 -62.58 66.76
REMARK 500 ASP B 128 -1.58 68.67
REMARK 500 ASN B 233 2.50 -68.10
REMARK 500 SER C 61 -113.73 45.55
REMARK 500 ASP C 81 -169.17 -114.31
REMARK 500 SER C 86 -114.52 35.58
REMARK 500 MET C 117 -62.44 66.83
REMARK 500 ASP C 128 -0.26 68.06
REMARK 500 ASN C 233 2.41 -68.54
REMARK 500 SER D 61 -116.61 46.69
REMARK 500 ASP D 81 -169.66 -112.50
REMARK 500 SER D 86 -112.74 35.49
REMARK 500 HIS D 115 172.88 175.98
REMARK 500 MET D 117 -62.96 67.86
REMARK 500 ASP D 128 -1.40 71.19
REMARK 500 ASN D 233 1.35 -66.32
REMARK 500 SER E 61 -113.39 46.66
REMARK 500 SER E 86 -110.00 33.66
REMARK 500 HIS E 115 171.64 175.93
REMARK 500 MET E 117 -60.21 66.40
REMARK 500 ASP E 128 -0.72 70.10
REMARK 500 ASN E 233 1.22 -66.69
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 ZN A 300 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 133 OE1
REMARK 620 2 ASP A 8 OD2 97.0
REMARK 620 3 HIS A 104 NE2 112.4 103.9
REMARK 620 4 GLU A 133 OE2 53.1 150.0 88.3
REMARK 620 5 HOH A2059 O 100.9 117.3 122.6 75.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 8 OD1
REMARK 620 2 HOH A2059 O 103.8
REMARK 620 3 HIS A 60 ND1 93.2 138.3
REMARK 620 4 GLU A 10 OE1 92.8 118.7 97.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 300 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 8 OD2
REMARK 620 2 HIS B 104 NE2 102.3
REMARK 620 3 GLU B 133 OE1 101.6 113.9
REMARK 620 4 GLU B 133 OE2 154.9 87.2 53.6
REMARK 620 5 HOH B2025 O 117.4 119.3 101.4 75.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 10 OE1
REMARK 620 2 HOH B2025 O 116.6
REMARK 620 3 ASP B 8 OD1 94.6 104.9
REMARK 620 4 HIS B 60 ND1 99.8 138.4 90.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 300 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 8 OD2
REMARK 620 2 HOH C2037 O 118.7
REMARK 620 3 HIS C 104 NE2 103.9 116.4
REMARK 620 4 GLU C 133 OE1 101.0 102.6 113.5
REMARK 620 5 GLU C 133 OE2 154.6 74.2 87.0 53.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 60 ND1
REMARK 620 2 ASP C 8 OD1 92.9
REMARK 620 3 HOH C2037 O 142.4 107.2
REMARK 620 4 GLU C 10 OE1 99.9 91.6 110.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 300 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 8 OD2
REMARK 620 2 GLU D 133 OE1 100.5
REMARK 620 3 GLU D 133 OE2 155.3 55.2
REMARK 620 4 HOH D2053 O 116.3 106.7 79.0
REMARK 620 5 HIS D 104 NE2 99.9 114.7 88.3 117.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 8 OD1
REMARK 620 2 GLU D 10 OE1 93.1
REMARK 620 3 GLU D 10 OE2 141.2 50.3
REMARK 620 4 HOH D2053 O 105.0 118.4 104.3
REMARK 620 5 HIS D 60 ND1 91.4 97.4 82.8 139.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN E 300 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 133 OE2
REMARK 620 2 HOH E2073 O 82.5
REMARK 620 3 ASP E 8 OD2 154.0 113.3
REMARK 620 4 HIS E 104 NE2 86.8 120.3 101.1
REMARK 620 5 GLU E 133 OE1 55.8 106.5 98.7 114.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN E 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 10 OE1
REMARK 620 2 HIS E 60 ND1 101.7
REMARK 620 3 HOH E2073 O 114.1 139.1
REMARK 620 4 ASP E 8 OD1 95.6 92.7 102.3
REMARK 620 N 1 2 3
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 301
DBREF 1HI9 A 1 274 UNP P26902 DPPA_BACSU 1 274
DBREF 1HI9 B 1 274 UNP P26902 DPPA_BACSU 1 274
DBREF 1HI9 C 1 274 UNP P26902 DPPA_BACSU 1 274
DBREF 1HI9 D 1 274 UNP P26902 DPPA_BACSU 1 274
DBREF 1HI9 E 1 274 UNP P26902 DPPA_BACSU 1 274
SEQRES 1 A 274 MET LYS LEU TYR MET SER VAL ASP MET GLU GLY ILE SER
SEQRES 2 A 274 GLY LEU PRO ASP ASP THR PHE VAL ASP SER GLY LYS ARG
SEQRES 3 A 274 ASN TYR GLU ARG GLY ARG LEU ILE MET THR GLU GLU ALA
SEQRES 4 A 274 ASN TYR CYS ILE ALA GLU ALA PHE ASN SER GLY CYS THR
SEQRES 5 A 274 GLU VAL LEU VAL ASN ASP SER HIS SER LYS MET ASN ASN
SEQRES 6 A 274 LEU MET VAL GLU LYS LEU HIS PRO GLU ALA ASP LEU ILE
SEQRES 7 A 274 SER GLY ASP VAL LYS PRO PHE SER MET VAL GLU GLY LEU
SEQRES 8 A 274 ASP ASP THR PHE ARG GLY ALA LEU PHE LEU GLY TYR HIS
SEQRES 9 A 274 ALA ARG ALA SER THR PRO GLY VAL MET SER HIS SER MET
SEQRES 10 A 274 ILE PHE GLY VAL ARG HIS PHE TYR ILE ASN ASP ARG PRO
SEQRES 11 A 274 VAL GLY GLU LEU GLY LEU ASN ALA TYR VAL ALA GLY TYR
SEQRES 12 A 274 TYR ASP VAL PRO VAL LEU MET VAL ALA GLY ASP ASP ARG
SEQRES 13 A 274 ALA ALA LYS GLU ALA GLU GLU LEU ILE PRO ASN VAL THR
SEQRES 14 A 274 THR ALA ALA VAL LYS GLN THR ILE SER ARG SER ALA VAL
SEQRES 15 A 274 LYS CYS LEU SER PRO ALA LYS ARG GLY ARG LEU LEU THR
SEQRES 16 A 274 GLU LYS THR ALA PHE ALA LEU GLN ASN LYS ASP LYS VAL
SEQRES 17 A 274 LYS PRO LEU THR PRO PRO ASP ARG PRO VAL LEU SER ILE
SEQRES 18 A 274 GLU PHE ALA ASN TYR GLY GLN ALA GLU TRP ALA ASN LEU
SEQRES 19 A 274 MET PRO GLY THR GLU ILE LYS THR GLY THR THR THR VAL
SEQRES 20 A 274 GLN PHE GLN ALA LYS ASP MET LEU GLU ALA TYR GLN ALA
SEQRES 21 A 274 MET LEU VAL MET THR GLU LEU ALA MET ARG THR SER PHE
SEQRES 22 A 274 CYS
SEQRES 1 B 274 MET LYS LEU TYR MET SER VAL ASP MET GLU GLY ILE SER
SEQRES 2 B 274 GLY LEU PRO ASP ASP THR PHE VAL ASP SER GLY LYS ARG
SEQRES 3 B 274 ASN TYR GLU ARG GLY ARG LEU ILE MET THR GLU GLU ALA
SEQRES 4 B 274 ASN TYR CYS ILE ALA GLU ALA PHE ASN SER GLY CYS THR
SEQRES 5 B 274 GLU VAL LEU VAL ASN ASP SER HIS SER LYS MET ASN ASN
SEQRES 6 B 274 LEU MET VAL GLU LYS LEU HIS PRO GLU ALA ASP LEU ILE
SEQRES 7 B 274 SER GLY ASP VAL LYS PRO PHE SER MET VAL GLU GLY LEU
SEQRES 8 B 274 ASP ASP THR PHE ARG GLY ALA LEU PHE LEU GLY TYR HIS
SEQRES 9 B 274 ALA ARG ALA SER THR PRO GLY VAL MET SER HIS SER MET
SEQRES 10 B 274 ILE PHE GLY VAL ARG HIS PHE TYR ILE ASN ASP ARG PRO
SEQRES 11 B 274 VAL GLY GLU LEU GLY LEU ASN ALA TYR VAL ALA GLY TYR
SEQRES 12 B 274 TYR ASP VAL PRO VAL LEU MET VAL ALA GLY ASP ASP ARG
SEQRES 13 B 274 ALA ALA LYS GLU ALA GLU GLU LEU ILE PRO ASN VAL THR
SEQRES 14 B 274 THR ALA ALA VAL LYS GLN THR ILE SER ARG SER ALA VAL
SEQRES 15 B 274 LYS CYS LEU SER PRO ALA LYS ARG GLY ARG LEU LEU THR
SEQRES 16 B 274 GLU LYS THR ALA PHE ALA LEU GLN ASN LYS ASP LYS VAL
SEQRES 17 B 274 LYS PRO LEU THR PRO PRO ASP ARG PRO VAL LEU SER ILE
SEQRES 18 B 274 GLU PHE ALA ASN TYR GLY GLN ALA GLU TRP ALA ASN LEU
SEQRES 19 B 274 MET PRO GLY THR GLU ILE LYS THR GLY THR THR THR VAL
SEQRES 20 B 274 GLN PHE GLN ALA LYS ASP MET LEU GLU ALA TYR GLN ALA
SEQRES 21 B 274 MET LEU VAL MET THR GLU LEU ALA MET ARG THR SER PHE
SEQRES 22 B 274 CYS
SEQRES 1 C 274 MET LYS LEU TYR MET SER VAL ASP MET GLU GLY ILE SER
SEQRES 2 C 274 GLY LEU PRO ASP ASP THR PHE VAL ASP SER GLY LYS ARG
SEQRES 3 C 274 ASN TYR GLU ARG GLY ARG LEU ILE MET THR GLU GLU ALA
SEQRES 4 C 274 ASN TYR CYS ILE ALA GLU ALA PHE ASN SER GLY CYS THR
SEQRES 5 C 274 GLU VAL LEU VAL ASN ASP SER HIS SER LYS MET ASN ASN
SEQRES 6 C 274 LEU MET VAL GLU LYS LEU HIS PRO GLU ALA ASP LEU ILE
SEQRES 7 C 274 SER GLY ASP VAL LYS PRO PHE SER MET VAL GLU GLY LEU
SEQRES 8 C 274 ASP ASP THR PHE ARG GLY ALA LEU PHE LEU GLY TYR HIS
SEQRES 9 C 274 ALA ARG ALA SER THR PRO GLY VAL MET SER HIS SER MET
SEQRES 10 C 274 ILE PHE GLY VAL ARG HIS PHE TYR ILE ASN ASP ARG PRO
SEQRES 11 C 274 VAL GLY GLU LEU GLY LEU ASN ALA TYR VAL ALA GLY TYR
SEQRES 12 C 274 TYR ASP VAL PRO VAL LEU MET VAL ALA GLY ASP ASP ARG
SEQRES 13 C 274 ALA ALA LYS GLU ALA GLU GLU LEU ILE PRO ASN VAL THR
SEQRES 14 C 274 THR ALA ALA VAL LYS GLN THR ILE SER ARG SER ALA VAL
SEQRES 15 C 274 LYS CYS LEU SER PRO ALA LYS ARG GLY ARG LEU LEU THR
SEQRES 16 C 274 GLU LYS THR ALA PHE ALA LEU GLN ASN LYS ASP LYS VAL
SEQRES 17 C 274 LYS PRO LEU THR PRO PRO ASP ARG PRO VAL LEU SER ILE
SEQRES 18 C 274 GLU PHE ALA ASN TYR GLY GLN ALA GLU TRP ALA ASN LEU
SEQRES 19 C 274 MET PRO GLY THR GLU ILE LYS THR GLY THR THR THR VAL
SEQRES 20 C 274 GLN PHE GLN ALA LYS ASP MET LEU GLU ALA TYR GLN ALA
SEQRES 21 C 274 MET LEU VAL MET THR GLU LEU ALA MET ARG THR SER PHE
SEQRES 22 C 274 CYS
SEQRES 1 D 274 MET LYS LEU TYR MET SER VAL ASP MET GLU GLY ILE SER
SEQRES 2 D 274 GLY LEU PRO ASP ASP THR PHE VAL ASP SER GLY LYS ARG
SEQRES 3 D 274 ASN TYR GLU ARG GLY ARG LEU ILE MET THR GLU GLU ALA
SEQRES 4 D 274 ASN TYR CYS ILE ALA GLU ALA PHE ASN SER GLY CYS THR
SEQRES 5 D 274 GLU VAL LEU VAL ASN ASP SER HIS SER LYS MET ASN ASN
SEQRES 6 D 274 LEU MET VAL GLU LYS LEU HIS PRO GLU ALA ASP LEU ILE
SEQRES 7 D 274 SER GLY ASP VAL LYS PRO PHE SER MET VAL GLU GLY LEU
SEQRES 8 D 274 ASP ASP THR PHE ARG GLY ALA LEU PHE LEU GLY TYR HIS
SEQRES 9 D 274 ALA ARG ALA SER THR PRO GLY VAL MET SER HIS SER MET
SEQRES 10 D 274 ILE PHE GLY VAL ARG HIS PHE TYR ILE ASN ASP ARG PRO
SEQRES 11 D 274 VAL GLY GLU LEU GLY LEU ASN ALA TYR VAL ALA GLY TYR
SEQRES 12 D 274 TYR ASP VAL PRO VAL LEU MET VAL ALA GLY ASP ASP ARG
SEQRES 13 D 274 ALA ALA LYS GLU ALA GLU GLU LEU ILE PRO ASN VAL THR
SEQRES 14 D 274 THR ALA ALA VAL LYS GLN THR ILE SER ARG SER ALA VAL
SEQRES 15 D 274 LYS CYS LEU SER PRO ALA LYS ARG GLY ARG LEU LEU THR
SEQRES 16 D 274 GLU LYS THR ALA PHE ALA LEU GLN ASN LYS ASP LYS VAL
SEQRES 17 D 274 LYS PRO LEU THR PRO PRO ASP ARG PRO VAL LEU SER ILE
SEQRES 18 D 274 GLU PHE ALA ASN TYR GLY GLN ALA GLU TRP ALA ASN LEU
SEQRES 19 D 274 MET PRO GLY THR GLU ILE LYS THR GLY THR THR THR VAL
SEQRES 20 D 274 GLN PHE GLN ALA LYS ASP MET LEU GLU ALA TYR GLN ALA
SEQRES 21 D 274 MET LEU VAL MET THR GLU LEU ALA MET ARG THR SER PHE
SEQRES 22 D 274 CYS
SEQRES 1 E 274 MET LYS LEU TYR MET SER VAL ASP MET GLU GLY ILE SER
SEQRES 2 E 274 GLY LEU PRO ASP ASP THR PHE VAL ASP SER GLY LYS ARG
SEQRES 3 E 274 ASN TYR GLU ARG GLY ARG LEU ILE MET THR GLU GLU ALA
SEQRES 4 E 274 ASN TYR CYS ILE ALA GLU ALA PHE ASN SER GLY CYS THR
SEQRES 5 E 274 GLU VAL LEU VAL ASN ASP SER HIS SER LYS MET ASN ASN
SEQRES 6 E 274 LEU MET VAL GLU LYS LEU HIS PRO GLU ALA ASP LEU ILE
SEQRES 7 E 274 SER GLY ASP VAL LYS PRO PHE SER MET VAL GLU GLY LEU
SEQRES 8 E 274 ASP ASP THR PHE ARG GLY ALA LEU PHE LEU GLY TYR HIS
SEQRES 9 E 274 ALA ARG ALA SER THR PRO GLY VAL MET SER HIS SER MET
SEQRES 10 E 274 ILE PHE GLY VAL ARG HIS PHE TYR ILE ASN ASP ARG PRO
SEQRES 11 E 274 VAL GLY GLU LEU GLY LEU ASN ALA TYR VAL ALA GLY TYR
SEQRES 12 E 274 TYR ASP VAL PRO VAL LEU MET VAL ALA GLY ASP ASP ARG
SEQRES 13 E 274 ALA ALA LYS GLU ALA GLU GLU LEU ILE PRO ASN VAL THR
SEQRES 14 E 274 THR ALA ALA VAL LYS GLN THR ILE SER ARG SER ALA VAL
SEQRES 15 E 274 LYS CYS LEU SER PRO ALA LYS ARG GLY ARG LEU LEU THR
SEQRES 16 E 274 GLU LYS THR ALA PHE ALA LEU GLN ASN LYS ASP LYS VAL
SEQRES 17 E 274 LYS PRO LEU THR PRO PRO ASP ARG PRO VAL LEU SER ILE
SEQRES 18 E 274 GLU PHE ALA ASN TYR GLY GLN ALA GLU TRP ALA ASN LEU
SEQRES 19 E 274 MET PRO GLY THR GLU ILE LYS THR GLY THR THR THR VAL
SEQRES 20 E 274 GLN PHE GLN ALA LYS ASP MET LEU GLU ALA TYR GLN ALA
SEQRES 21 E 274 MET LEU VAL MET THR GLU LEU ALA MET ARG THR SER PHE
SEQRES 22 E 274 CYS
HET ZN A 300 1
HET ZN A 301 1
HET ZN B 300 1
HET ZN B 301 1
HET ZN C 300 1
HET ZN C 301 1
HET ZN D 300 1
HET ZN D 301 1
HET ZN E 300 1
HET ZN E 301 1
HETNAM ZN ZINC ION
FORMUL 6 ZN 10(ZN 2+)
FORMUL 16 HOH *247(H2 O)
HELIX 1 1 ASP A 17 VAL A 21 5 5
HELIX 2 2 ASN A 27 SER A 49 1 23
HELIX 3 3 GLY A 132 TYR A 144 1 13
HELIX 4 4 ASP A 155 GLU A 163 1 9
HELIX 5 5 SER A 186 ASN A 204 1 19
HELIX 6 6 LYS A 205 VAL A 208 5 4
HELIX 7 7 ASN A 225 ASN A 233 1 9
HELIX 8 8 ASP A 253 MET A 269 1 17
HELIX 9 9 ASP B 17 VAL B 21 5 5
HELIX 10 10 ASN B 27 SER B 49 1 23
HELIX 11 11 GLY B 132 TYR B 144 1 13
HELIX 12 12 ASP B 155 GLU B 163 1 9
HELIX 13 13 SER B 186 ASN B 204 1 19
HELIX 14 14 LYS B 205 VAL B 208 5 4
HELIX 15 15 ASN B 225 ASN B 233 1 9
HELIX 16 16 ASP B 253 MET B 269 1 17
HELIX 17 17 ASP C 17 VAL C 21 5 5
HELIX 18 18 ASN C 27 SER C 49 1 23
HELIX 19 19 GLY C 132 TYR C 144 1 13
HELIX 20 20 ASP C 155 GLU C 163 1 9
HELIX 21 21 SER C 186 ASN C 204 1 19
HELIX 22 22 LYS C 205 VAL C 208 5 4
HELIX 23 23 ASN C 225 ASN C 233 1 9
HELIX 24 24 ASP C 253 MET C 269 1 17
HELIX 25 25 ASP D 17 VAL D 21 5 5
HELIX 26 26 ASN D 27 SER D 49 1 23
HELIX 27 27 GLY D 132 TYR D 144 1 13
HELIX 28 28 ASP D 155 GLU D 163 1 9
HELIX 29 29 SER D 186 ASN D 204 1 19
HELIX 30 30 LYS D 205 VAL D 208 5 4
HELIX 31 31 ASN D 225 ASN D 233 1 9
HELIX 32 32 ASP D 253 MET D 269 1 17
HELIX 33 33 ASP E 17 VAL E 21 5 5
HELIX 34 34 ASN E 27 SER E 49 1 23
HELIX 35 35 GLY E 132 TYR E 144 1 13
HELIX 36 36 ASP E 155 GLU E 163 1 9
HELIX 37 37 SER E 186 ASN E 204 1 19
HELIX 38 38 LYS E 205 VAL E 208 5 4
HELIX 39 39 ASN E 225 ASN E 233 1 9
HELIX 40 40 ASP E 253 MET E 269 1 17
SHEET 1 A 2 ALA A 181 CYS A 184 0
SHEET 2 A 2 LYS A 174 SER A 178 -1 N SER A 178 O ALA A 181
SHEET 1 B 6 THR A 169 ALA A 172 0
SHEET 2 B 6 PRO A 147 GLY A 153 1 N VAL A 151 O THR A 169
SHEET 3 B 6 GLY A 97 LEU A 101 1 N ALA A 98 O PRO A 147
SHEET 4 B 6 LYS A 2 ASP A 8 1 N TYR A 4 O GLY A 97
SHEET 5 B 6 GLU A 53 ASP A 58 1 N GLU A 53 O LEU A 3
SHEET 6 B 6 ALA A 75 SER A 79 1 N ASP A 76 O VAL A 56
SHEET 1 C 5 ARG A 129 VAL A 131 0
SHEET 2 C 5 VAL A 121 ILE A 126 -1 N ILE A 126 O ARG A 129
SHEET 3 C 5 PRO A 217 PHE A 223 -1 N GLU A 222 O ARG A 122
SHEET 4 C 5 THR A 246 ALA A 251 -1 N ALA A 251 O PRO A 217
SHEET 5 C 5 THR A 238 LYS A 241 -1 N GLU A 239 O GLN A 248
SHEET 1 D 2 ALA B 181 CYS B 184 0
SHEET 2 D 2 LYS B 174 SER B 178 -1 N SER B 178 O ALA B 181
SHEET 1 E 6 THR B 169 ALA B 172 0
SHEET 2 E 6 PRO B 147 GLY B 153 1 N VAL B 151 O THR B 169
SHEET 3 E 6 GLY B 97 LEU B 101 1 N PHE B 100 O MET B 150
SHEET 4 E 6 LYS B 2 ASP B 8 1 N TYR B 4 O GLY B 97
SHEET 5 E 6 GLU B 53 ASP B 58 1 N GLU B 53 O LEU B 3
SHEET 6 E 6 ALA B 75 SER B 79 1 N ASP B 76 O VAL B 56
SHEET 1 F 5 ARG B 129 VAL B 131 0
SHEET 2 F 5 VAL B 121 ILE B 126 -1 N ILE B 126 O ARG B 129
SHEET 3 F 5 PRO B 217 PHE B 223 -1 N GLU B 222 O ARG B 122
SHEET 4 F 5 THR B 246 ALA B 251 -1 N ALA B 251 O PRO B 217
SHEET 5 F 5 THR B 238 LYS B 241 -1 N GLU B 239 O GLN B 248
SHEET 1 G 2 ALA C 181 CYS C 184 0
SHEET 2 G 2 LYS C 174 SER C 178 -1 N SER C 178 O ALA C 181
SHEET 1 H 6 THR C 169 ALA C 172 0
SHEET 2 H 6 PRO C 147 GLY C 153 1 N VAL C 151 O THR C 169
SHEET 3 H 6 GLY C 97 LEU C 101 1 N PHE C 100 O MET C 150
SHEET 4 H 6 LYS C 2 ASP C 8 1 N TYR C 4 O GLY C 97
SHEET 5 H 6 GLU C 53 ASP C 58 1 N GLU C 53 O LEU C 3
SHEET 6 H 6 ALA C 75 SER C 79 1 N ASP C 76 O VAL C 56
SHEET 1 I 5 ARG C 129 VAL C 131 0
SHEET 2 I 5 VAL C 121 ILE C 126 -1 N ILE C 126 O ARG C 129
SHEET 3 I 5 PRO C 217 PHE C 223 -1 N GLU C 222 O ARG C 122
SHEET 4 I 5 THR C 246 ALA C 251 -1 N ALA C 251 O PRO C 217
SHEET 5 I 5 THR C 238 LYS C 241 -1 N GLU C 239 O GLN C 248
SHEET 1 J 2 ALA D 181 CYS D 184 0
SHEET 2 J 2 LYS D 174 SER D 178 -1 N SER D 178 O ALA D 181
SHEET 1 K 6 THR D 169 ALA D 172 0
SHEET 2 K 6 PRO D 147 GLY D 153 1 N VAL D 151 O THR D 169
SHEET 3 K 6 GLY D 97 LEU D 101 1 N PHE D 100 O MET D 150
SHEET 4 K 6 LYS D 2 ASP D 8 1 N TYR D 4 O GLY D 97
SHEET 5 K 6 GLU D 53 ASP D 58 1 N GLU D 53 O LEU D 3
SHEET 6 K 6 ALA D 75 SER D 79 1 N ASP D 76 O VAL D 56
SHEET 1 L 5 ARG D 129 VAL D 131 0
SHEET 2 L 5 VAL D 121 ILE D 126 -1 N ILE D 126 O ARG D 129
SHEET 3 L 5 PRO D 217 PHE D 223 -1 N GLU D 222 O ARG D 122
SHEET 4 L 5 THR D 246 ALA D 251 -1 N ALA D 251 O PRO D 217
SHEET 5 L 5 THR D 238 LYS D 241 -1 N GLU D 239 O GLN D 248
SHEET 1 M 2 ALA E 181 CYS E 184 0
SHEET 2 M 2 LYS E 174 SER E 178 -1 N SER E 178 O ALA E 181
SHEET 1 N 6 THR E 169 ALA E 172 0
SHEET 2 N 6 PRO E 147 GLY E 153 1 N VAL E 151 O THR E 169
SHEET 3 N 6 GLY E 97 LEU E 101 1 N PHE E 100 O MET E 150
SHEET 4 N 6 LYS E 2 ASP E 8 1 N TYR E 4 O GLY E 97
SHEET 5 N 6 GLU E 53 ASP E 58 1 N GLU E 53 O LEU E 3
SHEET 6 N 6 ALA E 75 SER E 79 1 N ASP E 76 O VAL E 56
SHEET 1 O 5 ARG E 129 VAL E 131 0
SHEET 2 O 5 VAL E 121 ILE E 126 -1 N ILE E 126 O ARG E 129
SHEET 3 O 5 PRO E 217 PHE E 223 -1 N GLU E 222 O ARG E 122
SHEET 4 O 5 THR E 246 ALA E 251 -1 N ALA E 251 O PRO E 217
SHEET 5 O 5 THR E 238 LYS E 241 -1 N GLU E 239 O GLN E 248
LINK ZN ZN A 300 OE1 GLU A 133 1555 1555 1.98
LINK ZN ZN A 300 OD2 ASP A 8 1555 1555 2.02
LINK ZN ZN A 300 NE2 HIS A 104 1555 1555 1.91
LINK ZN ZN A 300 OE2 GLU A 133 1555 1555 2.71
LINK ZN ZN A 300 O HOH A2059 1555 1555 2.10
LINK ZN ZN A 301 OD1 ASP A 8 1555 1555 2.29
LINK ZN ZN A 301 O HOH A2059 1555 1555 2.55
LINK ZN ZN A 301 ND1 HIS A 60 1555 1555 2.52
LINK ZN ZN A 301 OE1 GLU A 10 1555 1555 2.29
LINK ZN ZN B 300 OD2 ASP B 8 1555 1555 1.98
LINK ZN ZN B 300 NE2 HIS B 104 1555 1555 1.97
LINK ZN ZN B 300 OE1 GLU B 133 1555 1555 1.95
LINK ZN ZN B 300 OE2 GLU B 133 1555 1555 2.68
LINK ZN ZN B 300 O HOH B2025 1555 1555 2.13
LINK ZN ZN B 301 OE1 GLU B 10 1555 1555 2.31
LINK ZN ZN B 301 O HOH B2025 1555 1555 2.60
LINK ZN ZN B 301 OD1 ASP B 8 1555 1555 2.31
LINK ZN ZN B 301 ND1 HIS B 60 1555 1555 2.52
LINK ZN ZN C 300 OD2 ASP C 8 1555 1555 1.95
LINK ZN ZN C 300 O HOH C2037 1555 1555 2.11
LINK ZN ZN C 300 NE2 HIS C 104 1555 1555 1.96
LINK ZN ZN C 300 OE1 GLU C 133 1555 1555 1.97
LINK ZN ZN C 300 OE2 GLU C 133 1555 1555 2.67
LINK ZN ZN C 301 ND1 HIS C 60 1555 1555 2.47
LINK ZN ZN C 301 OD1 ASP C 8 1555 1555 2.29
LINK ZN ZN C 301 O HOH C2037 1555 1555 2.59
LINK ZN ZN C 301 OE1 GLU C 10 1555 1555 2.39
LINK ZN ZN D 300 OD2 ASP D 8 1555 1555 2.05
LINK ZN ZN D 300 OE1 GLU D 133 1555 1555 1.87
LINK ZN ZN D 300 OE2 GLU D 133 1555 1555 2.62
LINK ZN ZN D 300 O HOH D2053 1555 1555 2.08
LINK ZN ZN D 300 NE2 HIS D 104 1555 1555 1.99
LINK ZN ZN D 301 OD1 ASP D 8 1555 1555 2.33
LINK ZN ZN D 301 OE1 GLU D 10 1555 1555 2.28
LINK ZN ZN D 301 OE2 GLU D 10 1555 1555 2.77
LINK ZN ZN D 301 O HOH D2053 1555 1555 2.49
LINK ZN ZN D 301 ND1 HIS D 60 1555 1555 2.55
LINK ZN ZN E 300 OE2 GLU E 133 1555 1555 2.60
LINK ZN ZN E 300 O HOH E2073 1555 1555 2.01
LINK ZN ZN E 300 OD2 ASP E 8 1555 1555 2.07
LINK ZN ZN E 300 NE2 HIS E 104 1555 1555 1.99
LINK ZN ZN E 300 OE1 GLU E 133 1555 1555 1.88
LINK ZN ZN E 301 OE1 GLU E 10 1555 1555 2.26
LINK ZN ZN E 301 ND1 HIS E 60 1555 1555 2.48
LINK ZN ZN E 301 O HOH E2073 1555 1555 2.51
LINK ZN ZN E 301 OD1 ASP E 8 1555 1555 2.32
SITE 1 AC1 6 ASP A 8 HIS A 104 HIS A 115 GLU A 133
SITE 2 AC1 6 ZN A 301 HOH A2059
SITE 1 AC2 5 ASP A 8 GLU A 10 HIS A 60 ZN A 300
SITE 2 AC2 5 HOH A2059
SITE 1 AC3 6 ASP B 8 HIS B 104 HIS B 115 GLU B 133
SITE 2 AC3 6 ZN B 301 HOH B2025
SITE 1 AC4 5 ASP B 8 GLU B 10 HIS B 60 ZN B 300
SITE 2 AC4 5 HOH B2025
SITE 1 AC5 6 ASP C 8 HIS C 104 HIS C 115 GLU C 133
SITE 2 AC5 6 ZN C 301 HOH C2037
SITE 1 AC6 5 ASP C 8 GLU C 10 HIS C 60 ZN C 300
SITE 2 AC6 5 HOH C2037
SITE 1 AC7 6 ASP D 8 HIS D 104 HIS D 115 GLU D 133
SITE 2 AC7 6 ZN D 301 HOH D2053
SITE 1 AC8 5 ASP D 8 GLU D 10 HIS D 60 ZN D 300
SITE 2 AC8 5 HOH D2053
SITE 1 AC9 6 ASP E 8 HIS E 104 HIS E 115 GLU E 133
SITE 2 AC9 6 ZN E 301 HOH E2073
SITE 1 BC1 5 ASP E 8 GLU E 10 HIS E 60 ZN E 300
SITE 2 BC1 5 HOH E2073
CRYST1 145.110 165.860 109.930 90.00 90.00 90.00 C 2 2 21 40
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 0.006891 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006029 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009097 0.00000
MTRIX1 1 0.611040 -0.709260 -0.351550 66.89993 1
MTRIX2 1 0.714400 0.302790 0.630830 -40.49408 1
MTRIX3 1 -0.340970 -0.636610 0.691710 59.21963 1
MTRIX1 2 -0.006240 -0.440290 -0.897840 115.91030 1
MTRIX2 2 0.435580 -0.809400 0.393890 31.78131 1
MTRIX3 2 -0.900130 -0.388620 0.196840 103.19849 1
MTRIX1 3 -0.020740 0.447520 -0.894030 80.21922 1
MTRIX2 3 -0.441050 -0.806600 -0.393530 116.98578 1
MTRIX3 3 -0.897240 0.386150 0.214110 70.84882 1
MTRIX1 4 0.616090 0.714650 -0.331230 7.87976 1
MTRIX2 4 -0.707370 0.317000 -0.631770 96.86948 1
MTRIX3 4 -0.346500 0.623530 0.700820 7.79661 1
(ATOM LINES ARE NOT SHOWN.)
END
