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HEADER HYDROLASE 18-DEC-08 3FLB
TITLE RIFR - TYPE II THIOESTERASE FROM RIFAMYCIN NRPS/PKS
TITLE 2 BIOSYNTHETIC PATHWAY - FORM 2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIFR;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.2.-;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AMYCOLATOPSIS MEDITERRANEI;
SOURCE 3 ORGANISM_COMMON: NOCARDIA MEDITERRANEI;
SOURCE 4 ORGANISM_TAXID: 33910;
SOURCE 5 GENE: RIFR;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21,PMS25
KEYWDS ALPHA-BETA HYDROLASE THIOESTERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.L.SMITH,D.L.AKEY
REVDAT 1 06-JAN-09 3FLB 0
JRNL AUTH H.B.CLAXTON,D.L.AKEY,M.K.SILVER,S.J.ADMIRAAL,
JRNL AUTH 2 J.L.SMITH
JRNL TITL STRUCTURE AND FUNCTIONAL ANALYSIS OF RIFR, THE
JRNL TITL 2 TYPE II THIOESTERASE FROM THE RIFAMYCIN
JRNL TITL 3 BIOSYNTHETIC PATHWAY.
JRNL REF J.BIOL.CHEM. 2008
JRNL REFN ESSN 1083-351X
JRNL PMID 19103602
JRNL DOI 10.1074/JBC.M808604200
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.81
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 3 NUMBER OF REFLECTIONS : 17702
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) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 957
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW : 1.84
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1179
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.29
REMARK 3 BIN R VALUE (WORKING SET) : 0.2490
REMARK 3 BIN FREE R VALUE SET COUNT : 63
REMARK 3 BIN FREE R VALUE : 0.3260
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 2110
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.29
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.54000
REMARK 3 B22 (A**2) : -1.41000
REMARK 3 B33 (A**2) : 1.95000
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): 0.164
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.152
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.103
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.680
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.931
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1991 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2708 ; 1.183 ; 1.984
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 253 ; 4.939 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 91 ;26.502 ;21.209
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 303 ;13.550 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 27 ;18.589 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 290 ; 0.078 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1571 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1026 ; 0.206 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1347 ; 0.306 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 178 ; 0.153 ; 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): 87 ; 0.146 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 28 ; 0.173 ; 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): 1277 ; 2.358 ; 5.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2012 ; 3.413 ; 8.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 776 ; 2.177 ; 5.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 696 ; 2.808 ; 5.000
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 : 1.40
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
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 3FLB COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-DEC-08.
REMARK 100 THE RCSB ID CODE IS RCSB050730.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JAN-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97934
REMARK 200 MONOCHROMATOR : APS BEAMLINE 23-ID-D
REMARK 200 OPTICS : APS BEAMLINE 23-ID-D
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 300 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18683
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 200 DATA REDUNDANCY : 2.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06900
REMARK 200 FOR THE DATA SET : 12.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.37600
REMARK 200 FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES PH 7.0, 12% PEG 8000,
REMARK 280 50 MM CACL2, 2 MM DTT , VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
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 19.46900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 41.23350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.24850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 41.23350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 19.46900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 31.24850
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 MET A 1
REMARK 465 HIS A 2
REMARK 465 ARG A 3
REMARK 465 PRO A 4
REMARK 465 ALA A 250
REMARK 465 LEU A 251
REMARK 465 THR A 252
REMARK 465 GLY A 253
REMARK 465 SER A 254
REMARK 465 THR A 255
REMARK 465 GLY A 256
REMARK 465 GLY A 257
REMARK 465 ASN A 258
REMARK 465 SER A 259
REMARK 465 LEU A 260
REMARK 465 GLU A 261
REMARK 465 HIS A 262
REMARK 465 HIS A 263
REMARK 465 HIS A 264
REMARK 465 HIS A 265
REMARK 465 HIS A 266
REMARK 465 HIS A 267
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 8 CD CE NZ
REMARK 480 ARG A 15 NE CZ NH1 NH2
REMARK 480 ASP A 233 CG OD1 OD2
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 GLN A 58 -117.61 39.84
REMARK 500 ALA A 94 -117.73 54.42
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 CL A 268
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A5798
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3FLA RELATED DB: PDB
DBREF 3FLB A 1 259 UNP Q7BUF9 Q7BUF9_AMYMD 1 259
SEQADV 3FLB ALA A 94 UNP Q7BUF9 SER 94 ENGINEERED
SEQADV 3FLB LEU A 260 UNP Q7BUF9 EXPRESSION TAG
SEQADV 3FLB GLU A 261 UNP Q7BUF9 EXPRESSION TAG
SEQADV 3FLB HIS A 262 UNP Q7BUF9 EXPRESSION TAG
SEQADV 3FLB HIS A 263 UNP Q7BUF9 EXPRESSION TAG
SEQADV 3FLB HIS A 264 UNP Q7BUF9 EXPRESSION TAG
SEQADV 3FLB HIS A 265 UNP Q7BUF9 EXPRESSION TAG
SEQADV 3FLB HIS A 266 UNP Q7BUF9 EXPRESSION TAG
SEQADV 3FLB HIS A 267 UNP Q7BUF9 EXPRESSION TAG
SEQRES 1 A 267 MET HIS ARG PRO GLU ALA GLU LYS TRP LEU ARG ARG PHE
SEQRES 2 A 267 GLU ARG ALA PRO ASP ALA ARG ALA ARG LEU VAL CYS LEU
SEQRES 3 A 267 PRO HIS ALA GLY GLY SER ALA SER PHE PHE PHE PRO LEU
SEQRES 4 A 267 ALA LYS ALA LEU ALA PRO ALA VAL GLU VAL LEU ALA VAL
SEQRES 5 A 267 GLN TYR PRO GLY ARG GLN ASP ARG ARG HIS GLU PRO PRO
SEQRES 6 A 267 VAL ASP SER ILE GLY GLY LEU THR ASN ARG LEU LEU GLU
SEQRES 7 A 267 VAL LEU ARG PRO PHE GLY ASP ARG PRO LEU ALA LEU PHE
SEQRES 8 A 267 GLY HIS ALA MET GLY ALA ILE ILE GLY TYR GLU LEU ALA
SEQRES 9 A 267 LEU ARG MET PRO GLU ALA GLY LEU PRO ALA PRO VAL HIS
SEQRES 10 A 267 LEU PHE ALA SER GLY ARG ARG ALA PRO SER ARG TYR ARG
SEQRES 11 A 267 ASP ASP ASP VAL ARG GLY ALA SER ASP GLU ARG LEU VAL
SEQRES 12 A 267 ALA GLU LEU ARG LYS LEU GLY GLY SER ASP ALA ALA MET
SEQRES 13 A 267 LEU ALA ASP PRO GLU LEU LEU ALA MET VAL LEU PRO ALA
SEQRES 14 A 267 ILE ARG SER ASP TYR ARG ALA VAL GLU THR TYR ARG HIS
SEQRES 15 A 267 GLU PRO GLY ARG ARG VAL ASP CYS PRO VAL THR VAL PHE
SEQRES 16 A 267 THR GLY ASP HIS ASP PRO ARG VAL SER VAL GLY GLU ALA
SEQRES 17 A 267 ARG ALA TRP GLU GLU HIS THR THR GLY PRO ALA ASP LEU
SEQRES 18 A 267 ARG VAL LEU PRO GLY GLY HIS PHE PHE LEU VAL ASP GLN
SEQRES 19 A 267 ALA ALA PRO MET ILE ALA THR MET THR GLU LYS LEU ALA
SEQRES 20 A 267 GLY PRO ALA LEU THR GLY SER THR GLY GLY ASN SER LEU
SEQRES 21 A 267 GLU HIS HIS HIS HIS HIS HIS
HET CL A 268 1
HET PG4 A5798 13
HETNAM CL CHLORIDE ION
HETNAM PG4 TETRAETHYLENE GLYCOL
FORMUL 2 CL CL 1-
FORMUL 3 PG4 C8 H18 O5
FORMUL 4 HOH *167(H2 O)
HELIX 1 1 GLU A 5 TRP A 9 1 5
HELIX 2 2 SER A 32 PHE A 35 5 4
HELIX 3 3 PHE A 36 ALA A 44 1 9
HELIX 4 4 ARG A 57 ARG A 61 5 5
HELIX 5 5 SER A 68 ARG A 81 1 14
HELIX 6 6 PRO A 82 ARG A 86 5 5
HELIX 7 7 ALA A 94 GLY A 111 1 18
HELIX 8 8 SER A 138 GLY A 150 1 13
HELIX 9 9 GLY A 150 MET A 156 1 7
HELIX 10 10 ASP A 159 TYR A 180 1 22
HELIX 11 11 SER A 204 ALA A 210 1 7
HELIX 12 12 TRP A 211 THR A 215 5 5
HELIX 13 13 GLN A 234 LEU A 246 1 13
SHEET 1 A 7 LEU A 10 ARG A 11 0
SHEET 2 A 7 VAL A 47 VAL A 52 -1 O ALA A 51 N ARG A 11
SHEET 3 A 7 ALA A 21 LEU A 26 1 N CYS A 25 O VAL A 52
SHEET 4 A 7 LEU A 88 HIS A 93 1 O PHE A 91 N VAL A 24
SHEET 5 A 7 HIS A 117 SER A 121 1 O PHE A 119 N LEU A 90
SHEET 6 A 7 VAL A 192 GLY A 197 1 O PHE A 195 N ALA A 120
SHEET 7 A 7 ALA A 219 LEU A 224 1 O LEU A 224 N THR A 196
CISPEP 1 ALA A 44 PRO A 45 0 4.75
SITE 1 AC1 4 ALA A 29 ALA A 94 MET A 95 HOH A 427
SITE 1 AC2 4 PHE A 35 PRO A 38 ALA A 235 HOH A 420
CRYST1 38.938 62.497 82.467 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 0.025682 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016001 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012126 0.00000
TER 1930 PRO A 249
MASTER 298 0 2 13 7 0 2 6 2110 1 13 21
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