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HEADER LYASE 30-JUL-10 2XMZ
TITLE STRUCTURE OF MENH FROM S. AUREUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYDROLASE, ALPHA/BETA HYDROLASE FOLD FAMILY;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: 2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE
COMPND 5 SYNTHASE;
COMPND 6 EC: 4.2.99.20;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE 3 ORGANISM_TAXID: 1280;
SOURCE 4 STRAIN: COL;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET15BTEV;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET15BTEV_SAMENH
KEYWDS MENAQUINONE BIOSYNTHESIS, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.DAWSON,P.K.FYFE,F.GILLET,W.N.HUNTER
REVDAT 1 25-MAY-11 2XMZ 0
JRNL AUTH A.DAWSON,P.K.FYFE,F.GILLET,W.N.HUNTER
JRNL TITL EXPLOITING THE HIGH-RESOLUTION CRYSTAL STRUCTURE OF
JRNL TITL 2 STAPHYLOCOCCUS AUREUS MENH TO GAIN INSIGHT INTO ENZYME
JRNL TITL 3 ACTIVITY.
JRNL REF BMC STRUCT.BIOL. V. 11 19 2011
JRNL REFN ISSN 1472-6807
JRNL PMID 21513522
JRNL DOI 10.1186/1472-6807-11-19
REMARK 2
REMARK 2 RESOLUTION. 1.94 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.94
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.73
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.00
REMARK 3 NUMBER OF REFLECTIONS : 16378
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) : 0.18642
REMARK 3 R VALUE (WORKING SET) : 0.18341
REMARK 3 FREE R VALUE : 0.24073
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 864
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) : 1.943
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.993
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1046
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.55
REMARK 3 BIN R VALUE (WORKING SET) : 0.286
REMARK 3 BIN FREE R VALUE SET COUNT : 61
REMARK 3 BIN FREE R VALUE : 0.344
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2211
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 185
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.652
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.18
REMARK 3 B22 (A**2) : -0.74
REMARK 3 B33 (A**2) : 0.50
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : -0.23
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.216
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.183
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.128
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.466
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.916
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2259 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3052 ; 1.253 ; 1.956
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 265 ; 5.299 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 119 ;37.485 ;25.294
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 428 ;15.325 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;17.577 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 334 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1703 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 1329 ; 0.606 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2169 ; 1.092 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 930 ; 1.717 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 883 ; 2.736 ; 4.500
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 : 3
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 2 A 45
REMARK 3 ORIGIN FOR THE GROUP (A): 12.2730 26.9560 16.4930
REMARK 3 T TENSOR
REMARK 3 T11: 0.1377 T22: 0.0223
REMARK 3 T33: 0.1091 T12: -0.0191
REMARK 3 T13: 0.0505 T23: -0.0221
REMARK 3 L TENSOR
REMARK 3 L11: 1.6083 L22: 4.6294
REMARK 3 L33: 4.3031 L12: 0.2532
REMARK 3 L13: -0.3162 L23: -1.5454
REMARK 3 S TENSOR
REMARK 3 S11: 0.0135 S12: -0.0672 S13: 0.3198
REMARK 3 S21: -0.1068 S22: 0.0346 S23: -0.3490
REMARK 3 S31: -0.3792 S32: 0.2560 S33: -0.0481
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 46 A 119
REMARK 3 ORIGIN FOR THE GROUP (A): 2.0630 17.1790 15.3720
REMARK 3 T TENSOR
REMARK 3 T11: 0.1015 T22: 0.0322
REMARK 3 T33: 0.0187 T12: 0.0210
REMARK 3 T13: 0.0085 T23: -0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 1.7514 L22: 1.8758
REMARK 3 L33: 3.2264 L12: -0.1957
REMARK 3 L13: 0.0457 L23: 0.3141
REMARK 3 S TENSOR
REMARK 3 S11: -0.0061 S12: 0.0707 S13: 0.0872
REMARK 3 S21: -0.1226 S22: -0.0427 S23: 0.1223
REMARK 3 S31: -0.2166 S32: -0.2617 S33: 0.0487
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 120 A 265
REMARK 3 ORIGIN FOR THE GROUP (A): 12.9510 8.9990 20.5640
REMARK 3 T TENSOR
REMARK 3 T11: 0.0991 T22: 0.0395
REMARK 3 T33: 0.0346 T12: 0.0281
REMARK 3 T13: 0.0039 T23: -0.0252
REMARK 3 L TENSOR
REMARK 3 L11: 2.0897 L22: 1.7364
REMARK 3 L33: 2.5342 L12: -0.5569
REMARK 3 L13: -0.3451 L23: 0.3771
REMARK 3 S TENSOR
REMARK 3 S11: -0.0212 S12: -0.1284 S13: -0.0275
REMARK 3 S21: 0.0791 S22: 0.1824 S23: -0.1796
REMARK 3 S31: 0.1717 S32: 0.2524 S33: -0.1612
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS.
REMARK 3 ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS.
REMARK 4
REMARK 4 2XMZ COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-JUL-10.
REMARK 100 THE PDBE ID CODE IS EBI-44146.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-SEP-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
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 MICROMAX 007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : SI
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17242
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.94
REMARK 200 RESOLUTION RANGE LOW (A) : 19.73
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 4.1
REMARK 200 R MERGE (I) : 0.05
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.50
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.94
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.3
REMARK 200 R MERGE FOR SHELL (I) : 0.37
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.20
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1R3D
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.5
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.9
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN BUFFER: 20 MM TRIS-HCL,
REMARK 280 50 MM NACL, PH 7.5. RESERVOIR: 0.1 M NA HEPES PH 7.5, 25 %
REMARK 280 W/V PEG 4000.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 38.27400
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 21.78150
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 38.27400
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 21.78150
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 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 GLY A -1
REMARK 465 HIS A 0
REMARK 465 ASP A 267
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 2 -17.84 63.25
REMARK 500 SER A 89 -117.59 54.17
REMARK 500 ASN A 232 66.89 -108.00
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUAL GH FROM TAG CLEAVAGE AT N-TERMINUS
DBREF 2XMZ A 1 267 UNP Q5HH39 Q5HH39_STAAC 1 267
SEQADV 2XMZ GLY A -1 UNP Q5HH39 EXPRESSION TAG
SEQADV 2XMZ HIS A 0 UNP Q5HH39 EXPRESSION TAG
SEQRES 1 A 269 GLY HIS MET THR HIS TYR LYS PHE TYR GLU ALA ASN VAL
SEQRES 2 A 269 GLU THR ASN GLN VAL LEU VAL PHE LEU HIS GLY PHE LEU
SEQRES 3 A 269 SER ASP SER ARG THR TYR HIS ASN HIS ILE GLU LYS PHE
SEQRES 4 A 269 THR ASP ASN TYR HIS VAL ILE THR ILE ASP LEU PRO GLY
SEQRES 5 A 269 HIS GLY GLU ASP GLN SER SER MET ASP GLU THR TRP ASN
SEQRES 6 A 269 PHE ASP TYR ILE THR THR LEU LEU ASP ARG ILE LEU ASP
SEQRES 7 A 269 LYS TYR LYS ASP LYS SER ILE THR LEU PHE GLY TYR SER
SEQRES 8 A 269 MET GLY GLY ARG VAL ALA LEU TYR TYR ALA ILE ASN GLY
SEQRES 9 A 269 HIS ILE PRO ILE SER ASN LEU ILE LEU GLU SER THR SER
SEQRES 10 A 269 PRO GLY ILE LYS GLU GLU ALA ASN GLN LEU GLU ARG ARG
SEQRES 11 A 269 LEU VAL ASP ASP ALA ARG ALA LYS VAL LEU ASP ILE ALA
SEQRES 12 A 269 GLY ILE GLU LEU PHE VAL ASN ASP TRP GLU LYS LEU PRO
SEQRES 13 A 269 LEU PHE GLN SER GLN LEU GLU LEU PRO VAL GLU ILE GLN
SEQRES 14 A 269 HIS GLN ILE ARG GLN GLN ARG LEU SER GLN SER PRO HIS
SEQRES 15 A 269 LYS MET ALA LYS ALA LEU ARG ASP TYR GLY THR GLY GLN
SEQRES 16 A 269 MET PRO ASN LEU TRP PRO ARG LEU LYS GLU ILE LYS VAL
SEQRES 17 A 269 PRO THR LEU ILE LEU ALA GLY GLU TYR ASP GLU LYS PHE
SEQRES 18 A 269 VAL GLN ILE ALA LYS LYS MET ALA ASN LEU ILE PRO ASN
SEQRES 19 A 269 SER LYS CYS LYS LEU ILE SER ALA THR GLY HIS THR ILE
SEQRES 20 A 269 HIS VAL GLU ASP SER ASP GLU PHE ASP THR MET ILE LEU
SEQRES 21 A 269 GLY PHE LEU LYS GLU GLU GLN ASN ASP
FORMUL 2 HOH *185(H2 O)
HELIX 1 1 ASP A 26 HIS A 31 5 6
HELIX 2 2 HIS A 33 ASP A 39 1 7
HELIX 3 3 ASN A 63 ASP A 76 1 14
HELIX 4 4 LYS A 77 LYS A 79 5 3
HELIX 5 5 SER A 89 GLY A 102 1 14
HELIX 6 6 GLU A 120 GLY A 142 1 23
HELIX 7 7 GLY A 142 GLU A 151 1 10
HELIX 8 8 LYS A 152 LEU A 162 5 11
HELIX 9 9 PRO A 163 SER A 176 1 14
HELIX 10 10 SER A 178 GLY A 190 1 13
HELIX 11 11 LEU A 197 ILE A 204 5 8
HELIX 12 12 ASP A 216 ILE A 230 1 15
HELIX 13 13 THR A 244 ASP A 249 1 6
HELIX 14 14 ASP A 249 GLN A 265 1 17
SHEET 1 AA 7 TYR A 4 TYR A 7 0
SHEET 2 AA 7 HIS A 42 ILE A 46 -1 O VAL A 43 N TYR A 7
SHEET 3 AA 7 GLN A 15 LEU A 20 1 O GLN A 15 N HIS A 42
SHEET 4 AA 7 SER A 82 TYR A 88 1 O SER A 82 N VAL A 16
SHEET 5 AA 7 ASN A 108 GLU A 112 1 O ASN A 108 N LEU A 85
SHEET 6 AA 7 THR A 208 GLY A 213 1 O LEU A 209 N LEU A 111
SHEET 7 AA 7 SER A 233 ILE A 238 1 O LYS A 234 N ILE A 210
CRYST1 76.548 43.563 71.650 90.00 98.26 90.00 C 1 2 1 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 0.013064 0.000000 0.001896 0.00000
SCALE2 0.000000 0.022955 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014103 0.00000
TER 2212 ASN A 266
MASTER 319 0 0 14 7 0 0 6 2396 1 0 21
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