HEADER HYDROLASE 16-AUG-07 2QZ6
TITLE FIRST CRYSTAL STRUCTURE OF A PSYCHROPHILE CLASS C BETA-LACTAMASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-LACTAMASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CEPHALOSPORINASE;
COMPND 5 EC: 3.5.2.6
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS FLUORESCENS;
SOURCE 3 ORGANISM_TAXID: 294;
SOURCE 4 STRAIN: TAE 4
KEYWDS CLASS C BETA-LACTAMASE, PSYCHROPHILE, COLD ADAPTATION, ANTIBIOTIC
KEYWDS 2 RESISTANCE, HYDROLASE, PERIPLASM
EXPDTA X-RAY DIFFRACTION
AUTHOR C.MICHAUX,J.MASSANT,F.KERFF,P.CHARLIER,J.WOUTERS
REVDAT 4 25-OCT-23 2QZ6 1 REMARK
REVDAT 3 24-FEB-09 2QZ6 1 VERSN
REVDAT 2 08-APR-08 2QZ6 1 JRNL
REVDAT 1 18-MAR-08 2QZ6 0
JRNL AUTH C.MICHAUX,J.MASSANT,F.KERFF,J.D.DOCQUIER,I.VANDENBERGHE,
JRNL AUTH 2 B.SAMYN,A.PIERRARD,G.FELLER,P.CHARLIER,J.VAN BEEUMEN,
JRNL AUTH 3 J.WOUTERS
JRNL TITL CRYSTAL STRUCTURE OF A COLD-ADAPTED CLASS C BETA-LACTAMASE
JRNL REF FEBS J. V. 275 1687 2008
JRNL REFN ISSN 1742-464X
JRNL PMID 18312599
JRNL DOI 10.1111/J.1742-4658.2008.06324.X
REMARK 2
REMARK 2 RESOLUTION. 2.26 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) : 2.26
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.12
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.1
REMARK 3 NUMBER OF REFLECTIONS : 13722
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) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.243
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 722
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) : 2.26
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.32
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1048
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.1910
REMARK 3 BIN FREE R VALUE SET COUNT : 60
REMARK 3 BIN FREE R VALUE : 0.2580
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2661
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 134
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.57
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) : 0.01000
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): 0.432
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.253
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.146
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.706
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.909
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.873
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2713 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3693 ; 1.405 ; 1.969
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 345 ; 6.309 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 106 ;37.853 ;25.189
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 432 ;20.697 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 5 ;24.201 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 413 ; 0.097 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2055 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1382 ; 0.228 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1843 ; 0.305 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 135 ; 0.174 ; 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): 35 ; 0.215 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 4 ; 0.202 ; 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): 1772 ; 0.755 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2783 ; 1.255 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1073 ; 1.987 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 910 ; 2.942 ; 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 2QZ6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-AUG-07.
REMARK 100 THE DEPOSITION ID IS D_1000044228.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-APR-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM30A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9797
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 : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15724
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 4.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.03800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.9400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.06100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 16.62
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: AB INITIO
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 2BLT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 6K, 0.1M TRIS, PH8.0, VAPOR
REMARK 280 DIFFUSION, TEMPERATURE 298K, VAPOR DIFFUSION
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 34.85000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 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 ALA A 5
REMARK 465 THR A 6
REMARK 465 GLU A 123
REMARK 465 GLU A 124
REMARK 465 SER A 125
REMARK 465 ASP A 126
REMARK 465 ASN A 127
REMARK 465 ASP A 361
REMARK 465 GLN A 362
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS A 130 CG CD CE NZ
REMARK 480 MET A 131 CE
REMARK 480 SER A 213 CA CB OG
REMARK 480 ASP A 281 CG OD1 OD2
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 LEU A 83 CA - CB - CG ANGL. DEV. = 14.3 DEGREES
REMARK 500 TYR A 199 CB - CG - CD2 ANGL. DEV. = 4.5 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 ASP A 99 -103.82 -178.57
REMARK 500 LYS A 100 -79.57 -10.29
REMARK 500 PHE A 101 3.01 -68.91
REMARK 500 SER A 165 98.01 -69.59
REMARK 500 LEU A 166 3.76 136.26
REMARK 500 THR A 177 -68.37 -120.13
REMARK 500 PRO A 214 157.26 -46.06
REMARK 500 TYR A 222 19.04 -150.09
REMARK 500 LEU A 309 171.35 -57.31
REMARK 500 ASN A 341 46.77 -94.71
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2QZ6 A 5 362 UNP P85302 AMPC_PSEFL 1 358
SEQRES 1 A 358 ALA THR ASP ILE ARG GLN VAL VAL ASP SER THR VAL GLU
SEQRES 2 A 358 PRO LEU MET GLN GLN GLN ASP ILE ALA GLY LEU SER VAL
SEQRES 3 A 358 ALA VAL ILE GLN ASN GLY LYS ALA GLN TYR PHE ASN TYR
SEQRES 4 A 358 GLY VAL ALA ASN LYS ASP SER LYS GLN PRO ILE THR GLU
SEQRES 5 A 358 ASN THR LEU PHE GLU ILE GLY SER VAL SER LYS THR PHE
SEQRES 6 A 358 THR ALA THR LEU ALA GLY TYR ALA LEU ALA ASN GLY LYS
SEQRES 7 A 358 LEU LYS LEU SER ASP PRO ALA SER GLN TYR LEU PRO ALA
SEQRES 8 A 358 LEU ARG GLY ASP LYS PHE ASP HIS ILE SER LEU LEU ASN
SEQRES 9 A 358 LEU GLY THR TYR THR ALA GLY GLY LEU PRO LEU GLN PHE
SEQRES 10 A 358 PRO GLU GLU SER ASP ASN THR GLY LYS MET ILE SER TYR
SEQRES 11 A 358 TYR GLN HIS TRP LYS PRO ALA PHE ALA PRO GLY THR GLN
SEQRES 12 A 358 ARG LEU TYR SER ASN PRO SER ILE GLY LEU PHE GLY HIS
SEQRES 13 A 358 LEU ALA ALA GLN SER LEU GLY GLN PRO PHE GLU LYS LEU
SEQRES 14 A 358 MET GLU GLN THR VAL LEU PRO LYS LEU GLY LEU LYS HIS
SEQRES 15 A 358 THR PHE ILE SER VAL PRO GLU THR GLN MET SER LEU TYR
SEQRES 16 A 358 ALA GLN GLY TYR ASP LYS ALA GLY LYS PRO VAL ARG VAL
SEQRES 17 A 358 SER PRO GLY ALA LEU ASP ALA GLU ALA TYR GLY ILE LYS
SEQRES 18 A 358 THR SER THR SER ASP LEU ILE HIS TYR VAL GLU VAL ASN
SEQRES 19 A 358 MET HIS PRO ALA LYS LEU GLU LYS PRO LEU GLN GLN ALA
SEQRES 20 A 358 ILE ALA ALA THR HIS THR GLY TYR TYR THR VAL ASP GLY
SEQRES 21 A 358 MET THR GLN GLY LEU GLY TRP GLU MET TYR PRO TYR PRO
SEQRES 22 A 358 ILE LYS VAL ASP ALA LEU VAL GLU GLY ASN SER THR GLN
SEQRES 23 A 358 MET ALA MET GLU PRO HIS LYS VAL ASN TRP LEU THR PRO
SEQRES 24 A 358 PRO GLN ALA ALA PRO LEU ASP THR LEU VAL ASN LYS THR
SEQRES 25 A 358 GLY SER THR GLY GLY PHE GLY ALA TYR VAL ALA TYR VAL
SEQRES 26 A 358 PRO SER LYS GLY LEU GLY VAL VAL ILE LEU ALA ASN LYS
SEQRES 27 A 358 ASN TYR PRO ASN ALA GLU ARG VAL LYS ALA ALA HIS ALA
SEQRES 28 A 358 ILE LEU SER ALA MET ASP GLN
FORMUL 2 HOH *134(H2 O)
HELIX 1 1 ASP A 7 GLN A 23 1 17
HELIX 2 2 VAL A 65 ASN A 80 1 16
HELIX 3 3 PRO A 88 ARG A 97 5 10
HELIX 4 4 ASP A 99 HIS A 103 5 5
HELIX 5 5 SER A 105 THR A 111 1 7
HELIX 6 6 THR A 128 TRP A 138 1 11
HELIX 7 7 SER A 151 SER A 165 1 15
HELIX 8 8 PRO A 169 THR A 177 1 9
HELIX 9 9 LEU A 179 GLY A 183 5 5
HELIX 10 10 PRO A 192 TYR A 199 5 8
HELIX 11 11 LEU A 217 TYR A 222 1 6
HELIX 12 12 SER A 227 HIS A 240 1 14
HELIX 13 13 PRO A 241 LEU A 244 5 4
HELIX 14 14 GLU A 245 HIS A 256 1 12
HELIX 15 15 LYS A 279 ASN A 287 1 9
HELIX 16 16 THR A 289 GLU A 294 1 6
HELIX 17 17 PRO A 345 MET A 360 1 16
SHEET 1 A 9 LYS A 37 GLY A 44 0
SHEET 2 A 9 GLY A 27 GLN A 34 -1 N VAL A 30 O PHE A 41
SHEET 3 A 9 LEU A 334 ALA A 340 -1 O VAL A 337 N ALA A 31
SHEET 4 A 9 GLY A 323 VAL A 329 -1 N VAL A 329 O LEU A 334
SHEET 5 A 9 THR A 311 SER A 318 -1 N GLY A 317 O ALA A 324
SHEET 6 A 9 GLU A 272 PRO A 275 -1 N TYR A 274 O LEU A 312
SHEET 7 A 9 MET A 265 GLN A 267 -1 N THR A 266 O MET A 273
SHEET 8 A 9 GLY A 258 VAL A 262 -1 N TYR A 259 O GLN A 267
SHEET 9 A 9 ASN A 299 GLN A 305 -1 O LEU A 301 N TYR A 259
SHEET 1 B 3 PHE A 60 GLU A 61 0
SHEET 2 B 3 LYS A 225 THR A 226 -1 O THR A 226 N PHE A 60
SHEET 3 B 3 THR A 187 PHE A 188 -1 N PHE A 188 O LYS A 225
SHEET 1 C 2 GLN A 147 ARG A 148 0
SHEET 2 C 2 HIS A 296 LYS A 297 -1 O HIS A 296 N ARG A 148
CISPEP 1 TYR A 276 PRO A 277 0 -0.60
CRYST1 43.600 69.700 53.900 90.00 90.90 90.00 P 1 21 1 2
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 0.022936 0.000000 0.000360 0.00000
SCALE2 0.000000 0.014347 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018555 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
