HEADER HYDROLASE/HYDROLASE INHIBITOR 15-JUN-10 3NIA
TITLE GES-2 CARBAPENEMASE TAZOBACTAM COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-LACTAMASE GES-2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 19-287;
COMPND 5 SYNONYM: EXPANDED-SPECTRUM BETA-LACTAMASE GES-2;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 287;
SOURCE 4 GENE: BLA GES-2;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS BETA-LACTAMASE, ANTIBIOTIC RESISTANCE, CARBAPENEMASE, LACTAMASE
KEYWDS 2 INHIBITOR, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.FRASE,C.A.SMITH,M.TOTH,S.B.VAKULENKO
REVDAT 4 06-SEP-23 3NIA 1 REMARK LINK
REVDAT 3 04-MAY-11 3NIA 1 REMARK
REVDAT 2 09-MAR-11 3NIA 1 HEADER
REVDAT 1 02-MAR-11 3NIA 0
JRNL AUTH H.FRASE,C.A.SMITH,M.TOTH,M.M.CHAMPION,S.MOBASHERY,
JRNL AUTH 2 S.B.VAKULENKO
JRNL TITL INHIBITION OF THE GES-2 BETA-LACTAMSE BY TAZOBACTAM:
JRNL TITL 2 DETECTION OF REACTION INTERMEDIATES BY UV AND MASS
JRNL TITL 3 SPECTROMETRY AND X-RAY CRYSTALLOGRAPHY
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6_289)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.24
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 30711
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.157
REMARK 3 R VALUE (WORKING SET) : 0.155
REMARK 3 FREE R VALUE : 0.193
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1536
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 27.2410 - 3.6670 1.00 2847 151 0.1414 0.1535
REMARK 3 2 3.6670 - 2.9117 1.00 2708 142 0.1460 0.1739
REMARK 3 3 2.9117 - 2.5439 1.00 2662 140 0.1577 0.2154
REMARK 3 4 2.5439 - 2.3115 1.00 2652 140 0.1487 0.1945
REMARK 3 5 2.3115 - 2.1459 1.00 2613 137 0.1394 0.1658
REMARK 3 6 2.1459 - 2.0194 1.00 2655 140 0.1379 0.1888
REMARK 3 7 2.0194 - 1.9183 1.00 2610 137 0.1516 0.1909
REMARK 3 8 1.9183 - 1.8348 1.00 2623 138 0.1606 0.2099
REMARK 3 9 1.8348 - 1.7642 1.00 2602 137 0.1711 0.2603
REMARK 3 10 1.7642 - 1.7033 1.00 2608 138 0.1864 0.2101
REMARK 3 11 1.7033 - 1.6500 1.00 2595 136 0.1938 0.2511
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.33
REMARK 3 B_SOL : 35.99
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.150
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.59390
REMARK 3 B22 (A**2) : 1.59390
REMARK 3 B33 (A**2) : -3.18770
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.006 2192
REMARK 3 ANGLE : 1.143 2983
REMARK 3 CHIRALITY : 0.073 344
REMARK 3 PLANARITY : 0.005 388
REMARK 3 DIHEDRAL : 17.981 830
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3NIA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUN-10.
REMARK 100 THE DEPOSITION ID IS D_1000059863.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-OCT-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9785
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30744
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 27.241
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.09500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.52200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.550
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB CODE 2QPN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M POTASSIUM THIOCYANATE, 20% (W/V)
REMARK 280 PEG 3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
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 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 35.48500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 41.72000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 41.72000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 53.22750
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 41.72000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 41.72000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 17.74250
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 41.72000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 41.72000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 53.22750
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 41.72000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 41.72000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 17.74250
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
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 35.48500
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 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 A 355 LIES ON A SPECIAL POSITION.
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 ASP A 286
REMARK 465 LYS A 287
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 HOH A 301 O HOH A 541 2.17
REMARK 500
REMARK 500 REMARK: NULL
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 O HOH A 375 O HOH A 376 8555 2.16
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 CYS A 63 -134.68 37.86
REMARK 500 CYS A 63 -134.05 36.42
REMARK 500 TRP A 99 74.81 59.32
REMARK 500 LYS A 160 -169.13 -111.62
REMARK 500 THR A 215 -128.95 -105.98
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 TBE A 288
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TF7 A 289
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3NI9 RELATED DB: PDB
REMARK 900 GES-2 APO FORM
DBREF 3NIA A 19 287 UNP Q93F76 Q93F76_PSEAE 19 287
SEQRES 1 A 269 SER GLU LYS LEU THR PHE LYS THR ASP LEU GLU LYS LEU
SEQRES 2 A 269 GLU ARG GLU LYS ALA ALA GLN ILE GLY VAL ALA ILE VAL
SEQRES 3 A 269 ASP PRO GLN GLY GLU ILE VAL ALA GLY HIS ARG MET ALA
SEQRES 4 A 269 GLN ARG PHE ALA MET CYS SER THR PHE LYS PHE PRO LEU
SEQRES 5 A 269 ALA ALA LEU VAL PHE GLU ARG ILE ASP SER GLY THR GLU
SEQRES 6 A 269 ARG GLY ASP ARG LYS LEU SER TYR GLY PRO ASP MET ILE
SEQRES 7 A 269 VAL GLU TRP SER PRO ALA THR GLU ARG PHE LEU ALA SER
SEQRES 8 A 269 GLY HIS MET THR VAL LEU GLU ALA ALA GLN ALA ALA VAL
SEQRES 9 A 269 GLN LEU SER ASP ASN GLY ALA THR ASN LEU LEU LEU ARG
SEQRES 10 A 269 GLU ILE GLY GLY PRO ALA ALA MET THR GLN TYR PHE ARG
SEQRES 11 A 269 LYS ILE GLY ASP SER VAL SER ARG LEU ASP ARG LYS GLU
SEQRES 12 A 269 PRO GLU MET ASN ASP ASN THR PRO GLY ASP LEU ARG ASP
SEQRES 13 A 269 THR THR THR PRO ILE ALA MET ALA ARG THR VAL ALA LYS
SEQRES 14 A 269 VAL LEU TYR GLY GLY ALA LEU THR SER THR SER THR HIS
SEQRES 15 A 269 THR ILE GLU ARG TRP LEU ILE GLY ASN GLN THR GLY ASP
SEQRES 16 A 269 ALA THR LEU ARG ALA GLY PHE PRO LYS ASP TRP VAL VAL
SEQRES 17 A 269 GLY GLU LYS THR GLY THR CYS ALA ASN GLY GLY ARG ASN
SEQRES 18 A 269 ASP ILE GLY PHE PHE LYS ALA GLN GLU ARG ASP TYR ALA
SEQRES 19 A 269 VAL ALA VAL TYR THR THR ALA PRO LYS LEU SER ALA VAL
SEQRES 20 A 269 GLU ARG ASP GLU LEU VAL ALA SER VAL GLY GLN VAL ILE
SEQRES 21 A 269 THR GLN LEU ILE LEU SER THR ASP LYS
HET TBE A 288 23
HET TF7 A 289 16
HETNAM TBE TAZOBACTAM INTERMEDIATE
HETNAM TF7 (3S)-3-(DIHYDROXY-LAMBDA~4~-SULFANYL)-4-(1H-1,2,3-
HETNAM 2 TF7 TRIAZOL-1-YL)-D-VALINE
FORMUL 2 TBE C10 H14 N4 O5 S
FORMUL 3 TF7 C7 H14 N4 O4 S
FORMUL 4 HOH *354(H2 O)
HELIX 1 1 SER A 19 ALA A 36 1 18
HELIX 2 2 CYS A 63 THR A 65 5 3
HELIX 3 3 PHE A 66 SER A 80 1 15
HELIX 4 4 GLY A 92 ILE A 96 5 5
HELIX 5 5 SER A 100 LEU A 107 1 8
HELIX 6 6 VAL A 114 LEU A 124 1 11
HELIX 7 7 ASP A 126 GLY A 138 1 13
HELIX 8 8 GLY A 138 ILE A 150 1 13
HELIX 9 9 PRO A 162 ASP A 166 5 5
HELIX 10 10 THR A 177 GLY A 191 1 15
HELIX 11 11 THR A 195 GLY A 208 1 14
HELIX 12 12 THR A 215 PHE A 220 5 6
HELIX 13 13 SER A 263 THR A 285 1 23
SHEET 1 A 5 ILE A 50 HIS A 54 0
SHEET 2 A 5 GLN A 38 VAL A 44 -1 N ILE A 43 O VAL A 51
SHEET 3 A 5 ARG A 249 THR A 258 -1 O TYR A 256 N GLY A 40
SHEET 4 A 5 GLY A 237 ALA A 246 -1 N GLY A 242 O VAL A 253
SHEET 5 A 5 VAL A 225 CYS A 233 -1 N LYS A 229 O ILE A 241
SHEET 1 B 2 PHE A 60 ALA A 61 0
SHEET 2 B 2 THR A 175 THR A 176 -1 O THR A 176 N PHE A 60
SHEET 1 C 2 LYS A 88 SER A 90 0
SHEET 2 C 2 HIS A 111 THR A 113 -1 O MET A 112 N LEU A 89
SSBOND 1 CYS A 63 CYS A 233 1555 1555 2.04
LINK OG SER A 64 C7 TBE A 288 1555 1555 1.44
CISPEP 1 GLU A 161 PRO A 162 0 4.54
SITE 1 AC1 15 CYS A 63 SER A 64 ASN A 127 PRO A 162
SITE 2 AC1 15 ASN A 165 GLY A 231 THR A 232 TF7 A 289
SITE 3 AC1 15 HOH A 385 HOH A 386 HOH A 404 HOH A 444
SITE 4 AC1 15 HOH A 519 HOH A 555 HOH A 573
SITE 1 AC2 15 SER A 64 TRP A 99 SER A 125 THR A 211
SITE 2 AC2 15 LYS A 229 THR A 230 GLY A 231 THR A 232
SITE 3 AC2 15 ARG A 238 TBE A 288 HOH A 383 HOH A 385
SITE 4 AC2 15 HOH A 386 HOH A 400 HOH A 558
CRYST1 83.440 83.440 70.970 90.00 90.00 90.00 P 43 21 2 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 0.011985 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011985 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014090 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
