HEADER HYDROLASE/ANTIBIOTIC 07-JUN-10 3NDG
TITLE CRYSTAL STRUCTURE OF BLAC-E166A COVALENTLY BOUND WITH METHICILLIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-LACTAMASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PENICILLINASE;
COMPND 5 EC: 3.5.2.6;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 GENE: BLAA, BLAC, MT2128, MTCY49.07C, RV2068C;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: ROSETTA2;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS PENICILLIN BINDING PROTEIN, BETA-LACTAM COVALENT ADDUCT, HYDROLASE-
KEYWDS 2 ANTIBIOTIC COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR L.W.TREMBLAY,J.S.BLANCHARD
REVDAT 4 06-SEP-23 3NDG 1 REMARK SEQADV LINK
REVDAT 3 08-NOV-17 3NDG 1 REMARK
REVDAT 2 28-MAR-12 3NDG 1 HEADER KEYWDS HETSYN
REVDAT 1 14-DEC-11 3NDG 0
JRNL AUTH L.W.TREMBLAY,J.S.BLANCHARD
JRNL TITL BLAC-E166A COVALENTLY BOUND WITH CEPHALOSPORINS AND
JRNL TITL 2 PENICILLINS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.94
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 3 NUMBER OF REFLECTIONS : 19808
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) : 0.155
REMARK 3 R VALUE (WORKING SET) : 0.153
REMARK 3 FREE R VALUE : 0.191
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1018
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1348
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.36
REMARK 3 BIN R VALUE (WORKING SET) : 0.1670
REMARK 3 BIN FREE R VALUE SET COUNT : 71
REMARK 3 BIN FREE R VALUE : 0.2210
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1984
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 36
REMARK 3 SOLVENT ATOMS : 215
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.32
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.13
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.01000
REMARK 3 B22 (A**2) : 0.01000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.129
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.078
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.595
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.937
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2058 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2813 ; 1.392 ; 1.984
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 264 ; 6.153 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 87 ;38.615 ;23.103
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 302 ;11.706 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 19 ;20.621 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 319 ; 0.096 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1581 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 972 ; 0.213 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1432 ; 0.301 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 181 ; 0.142 ; 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): 59 ; 0.207 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 24 ; 0.116 ; 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): 1358 ; 0.792 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2110 ; 1.294 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 797 ; 2.179 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 703 ; 3.364 ; 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 3NDG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JUN-10.
REMARK 100 THE DEPOSITION ID IS D_1000059690.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 2009; 2009
REMARK 200 TEMPERATURE (KELVIN) : 100; 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : NSLS; NSLS
REMARK 200 BEAMLINE : X12C; X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL; NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000; 1.000
REMARK 200 MONOCHROMATOR : SI(111) CHANNEL CUT; SI(111)
REMARK 200 CHANNEL CUT
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210; ADSC QUANTUM
REMARK 200 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19843
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 39.940
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : 0.10300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.4
REMARK 200 DATA REDUNDANCY IN SHELL : 6.40
REMARK 200 R MERGE FOR SHELL (I) : 0.31500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: DIRECT
REMARK 200 STARTING MODEL: PDB ENTRY 3DWZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, 2 M NH4H2PO4, PH 7.5,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 24.67750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 37.78450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.95400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 37.78450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.67750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 33.95400
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 THR A 66 -164.89 -122.45
REMARK 500 CYS A 83 -147.16 47.30
REMARK 500 ARG A 236 -118.02 -116.57
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 7EP A 1
DBREF 3NDG A 43 307 UNP P0C5C1 BLAC_MYCTU 43 307
SEQADV 3NDG ALA A 182 UNP P0C5C1 GLU 182 ENGINEERED MUTATION
SEQRES 1 A 265 ASP LEU ALA ASP ARG PHE ALA GLU LEU GLU ARG ARG TYR
SEQRES 2 A 265 ASP ALA ARG LEU GLY VAL TYR VAL PRO ALA THR GLY THR
SEQRES 3 A 265 THR ALA ALA ILE GLU TYR ARG ALA ASP GLU ARG PHE ALA
SEQRES 4 A 265 PHE CYS SER THR PHE LYS ALA PRO LEU VAL ALA ALA VAL
SEQRES 5 A 265 LEU HIS GLN ASN PRO LEU THR HIS LEU ASP LYS LEU ILE
SEQRES 6 A 265 THR TYR THR SER ASP ASP ILE ARG SER ILE SER PRO VAL
SEQRES 7 A 265 ALA GLN GLN HIS VAL GLN THR GLY MET THR ILE GLY GLN
SEQRES 8 A 265 LEU CYS ASP ALA ALA ILE ARG TYR SER ASP GLY THR ALA
SEQRES 9 A 265 ALA ASN LEU LEU LEU ALA ASP LEU GLY GLY PRO GLY GLY
SEQRES 10 A 265 GLY THR ALA ALA PHE THR GLY TYR LEU ARG SER LEU GLY
SEQRES 11 A 265 ASP THR VAL SER ARG LEU ASP ALA GLU ALA PRO GLU LEU
SEQRES 12 A 265 ASN ARG ASP PRO PRO GLY ASP GLU ARG ASP THR THR THR
SEQRES 13 A 265 PRO HIS ALA ILE ALA LEU VAL LEU GLN GLN LEU VAL LEU
SEQRES 14 A 265 GLY ASN ALA LEU PRO PRO ASP LYS ARG ALA LEU LEU THR
SEQRES 15 A 265 ASP TRP MET ALA ARG ASN THR THR GLY ALA LYS ARG ILE
SEQRES 16 A 265 ARG ALA GLY PHE PRO ALA ASP TRP LYS VAL ILE ASP LYS
SEQRES 17 A 265 THR GLY THR GLY ASP TYR GLY ARG ALA ASN ASP ILE ALA
SEQRES 18 A 265 VAL VAL TRP SER PRO THR GLY VAL PRO TYR VAL VAL ALA
SEQRES 19 A 265 VAL MET SER ASP ARG ALA GLY GLY GLY TYR ASP ALA GLU
SEQRES 20 A 265 PRO ARG GLU ALA LEU LEU ALA GLU ALA ALA THR CYS VAL
SEQRES 21 A 265 ALA GLY VAL LEU ALA
HET PO4 A 2 5
HET PO4 A 3 5
HET 7EP A 1 26
HETNAM PO4 PHOSPHATE ION
HETNAM 7EP (2R,4S)-2-[(1R)-1-{[(2,6-DIMETHOXYPHENYL)
HETNAM 2 7EP CARBONYL]AMINO}-2-OXOETHYL]-5,5-DIMETHYL-1,3-
HETNAM 3 7EP THIAZOLIDINE-4-CARBOXYLIC ACID
HETSYN 7EP METHICILLIN, BOUND FORM
FORMUL 2 PO4 2(O4 P 3-)
FORMUL 4 7EP C17 H22 N2 O6 S
FORMUL 5 HOH *215(H2 O)
HELIX 1 1 ASP A 43 TYR A 55 1 13
HELIX 2 2 CYS A 83 THR A 85 5 3
HELIX 3 3 PHE A 86 ASN A 98 1 13
HELIX 4 4 PRO A 99 ASP A 104 5 6
HELIX 5 5 THR A 110 ILE A 114 5 5
HELIX 6 6 VAL A 120 VAL A 125 5 6
HELIX 7 7 ILE A 131 TYR A 141 1 11
HELIX 8 8 ASP A 143 GLY A 155 1 13
HELIX 9 9 PRO A 157 GLY A 159 5 3
HELIX 10 10 GLY A 160 LEU A 171 1 12
HELIX 11 11 PRO A 183 ARG A 187 5 5
HELIX 12 12 THR A 198 LEU A 211 1 14
HELIX 13 13 PRO A 216 ARG A 229 1 14
HELIX 14 14 ARG A 236 PHE A 241 1 6
HELIX 15 15 ARG A 281 GLY A 285 5 5
HELIX 16 16 ARG A 291 ALA A 307 1 17
SHEET 1 A 5 ILE A 72 TYR A 74 0
SHEET 2 A 5 ARG A 58 VAL A 63 -1 N VAL A 61 O TYR A 74
SHEET 3 A 5 PRO A 272 ASP A 280 -1 O MET A 278 N GLY A 60
SHEET 4 A 5 ALA A 259 TRP A 266 -1 N VAL A 265 O TYR A 273
SHEET 5 A 5 LYS A 246 THR A 253 -1 N GLY A 252 O ASN A 260
SHEET 1 B 2 PHE A 80 ALA A 81 0
SHEET 2 B 2 THR A 196 THR A 197 -1 O THR A 197 N PHE A 80
SHEET 1 C 2 LEU A 106 ILE A 107 0
SHEET 2 C 2 MET A 129 THR A 130 -1 O MET A 129 N ILE A 107
LINK C 7EP A 1 OG SER A 84 1555 1555 1.33
CISPEP 1 ALA A 182 PRO A 183 0 2.98
SITE 1 AC1 4 HOH A 29 ARG A 75 GLU A 78 GLU A 184
SITE 1 AC2 7 7EP A 1 ARG A 79 ARG A 187 GLU A 193
SITE 2 AC2 7 ASP A 255 TYR A 286 HOH A 478
SITE 1 AC3 16 PO4 A 3 CYS A 83 SER A 84 ILE A 117
SITE 2 AC3 16 SER A 142 PRO A 183 ASN A 186 LYS A 250
SITE 3 AC3 16 THR A 251 GLY A 252 THR A 253 GLY A 254
SITE 4 AC3 16 ASP A 255 HOH A 337 HOH A 471 HOH A 474
CRYST1 49.355 67.908 75.569 90.00 90.00 90.00 P 21 21 21 4
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 0.020261 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014726 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013233 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
