| content |
HEADER HYDROLASE 05-FEB-11 3QMW
TITLE REDJ WITH PEG MOLECULE BOUND IN THE ACTIVE SITE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THIOESTERASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: UNP RESIDUES 6-261;
COMPND 5 SYNONYM: REDJ;
COMPND 6 EC: 3.1.2.-;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES COELICOLOR;
SOURCE 3 ORGANISM_TAXID: 1902;
SOURCE 4 GENE: SCO5894, SC3F7.14;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALPHA/BETA HYDROLASE FOLD, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.R.WHICHER,J.L.SMITH
REVDAT 1 04-MAY-11 3QMW 0
JRNL AUTH J.R.WHICHER,G.FLOROVA,P.K.SYDOR,R.SINGH,M.ALHAMADSHEH,
JRNL AUTH 2 G.L.CHALLIS,K.A.REYNOLDS,J.L.SMITH
JRNL TITL STRUCTURE AND FUNCTION OF REDJ, A THIOESTERASE FROM THE
JRNL TITL 2 PRODIGININE BIOSYNTHETIC PATHWAY IN STREPTOMYCES COELICOLOR
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.50 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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 33414
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) : 0.218
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.284
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1621
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.56
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1827
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 73.69
REMARK 3 BIN R VALUE (WORKING SET) : 0.3100
REMARK 3 BIN FREE R VALUE SET COUNT : 86
REMARK 3 BIN FREE R VALUE : 0.3570
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7692
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 13
REMARK 3 SOLVENT ATOMS : 151
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.48
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.92000
REMARK 3 B22 (A**2) : 2.91000
REMARK 3 B33 (A**2) : -2.06000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.11000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 3.878
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.370
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.932
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): 7946 ; 0.012 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 5637 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10835 ; 1.201 ; 1.971
REMARK 3 BOND ANGLES OTHERS (DEGREES): 13443 ; 4.006 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 974 ; 5.598 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 381 ;26.344 ;20.551
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1136 ;15.353 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 117 ;16.292 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1143 ; 0.073 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8974 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1823 ; 0.005 ; 0.020
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): 4929 ; 0.572 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1939 ; 0.000 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7888 ; 1.092 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3017 ; 1.325 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2947 ; 2.299 ; 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 : 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:
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 3 U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 3QMW COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-FEB-11.
REMARK 100 THE RCSB ID CODE IS RCSB063845.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-OCT-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
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) : 1.0332
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
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 : 33414
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.5
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10100
REMARK 200 FOR THE DATA SET : 11.0200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.35900
REMARK 200 FOR SHELL : 2.700
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 3QMV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG3350, 0.22 M SODIUM CHLORIDE, 2
REMARK 280 MM DTT, 0.1 M HEPES, PH 7, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
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 77.77250
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 22.50650
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 77.77250
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 22.50650
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3570 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C
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 SER A 3
REMARK 465 ASN A 4
REMARK 465 ALA A 5
REMARK 465 LEU A 6
REMARK 465 LEU A 7
REMARK 465 SER A 8
REMARK 465 GLN A 9
REMARK 465 ARG A 10
REMARK 465 PRO A 21
REMARK 465 ALA A 22
REMARK 465 ASP A 166
REMARK 465 ASP A 167
REMARK 465 ALA A 168
REMARK 465 SER B 3
REMARK 465 ASN B 4
REMARK 465 ALA B 5
REMARK 465 LEU B 6
REMARK 465 LEU B 7
REMARK 465 SER B 8
REMARK 465 GLN B 9
REMARK 465 ARG B 10
REMARK 465 ALA B 19
REMARK 465 ALA B 20
REMARK 465 PRO B 21
REMARK 465 ALA B 22
REMARK 465 ALA B 23
REMARK 465 SER C 3
REMARK 465 ASN C 4
REMARK 465 ALA C 5
REMARK 465 ALA C 22
REMARK 465 LEU C 165
REMARK 465 ASP C 166
REMARK 465 ASP C 167
REMARK 465 ALA C 168
REMARK 465 ASP C 169
REMARK 465 THR C 170
REMARK 465 LEU C 171
REMARK 465 GLY C 172
REMARK 465 ALA C 173
REMARK 465 ALA C 174
REMARK 465 TYR C 175
REMARK 465 PHE C 176
REMARK 465 ASP C 177
REMARK 465 ARG C 178
REMARK 465 SER D 3
REMARK 465 ASN D 4
REMARK 465 ALA D 5
REMARK 465 LEU D 6
REMARK 465 LEU D 7
REMARK 465 SER D 8
REMARK 465 GLN D 9
REMARK 465 ARG D 10
REMARK 465 ASP D 167
REMARK 465 ALA D 168
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 SER A 107 -118.86 56.16
REMARK 500 SER B 107 -122.44 59.79
REMARK 500 SER C 107 -124.63 49.11
REMARK 500 SER D 107 -132.43 60.47
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 PG4 B 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3QMV RELATED DB: PDB
REMARK 900 STRUCTURE OF REDJ WITHOUT PEG BOUND IN THE ACTIVE SITE.
DBREF 3QMW A 6 261 UNP O54157 O54157_STRCO 6 261
DBREF 3QMW B 6 261 UNP O54157 O54157_STRCO 6 261
DBREF 3QMW C 6 261 UNP O54157 O54157_STRCO 6 261
DBREF 3QMW D 6 261 UNP O54157 O54157_STRCO 6 261
SEQADV 3QMW SER A 3 UNP O54157 EXPRESSION TAG
SEQADV 3QMW ASN A 4 UNP O54157 EXPRESSION TAG
SEQADV 3QMW ALA A 5 UNP O54157 EXPRESSION TAG
SEQADV 3QMW SER B 3 UNP O54157 EXPRESSION TAG
SEQADV 3QMW ASN B 4 UNP O54157 EXPRESSION TAG
SEQADV 3QMW ALA B 5 UNP O54157 EXPRESSION TAG
SEQADV 3QMW SER C 3 UNP O54157 EXPRESSION TAG
SEQADV 3QMW ASN C 4 UNP O54157 EXPRESSION TAG
SEQADV 3QMW ALA C 5 UNP O54157 EXPRESSION TAG
SEQADV 3QMW SER D 3 UNP O54157 EXPRESSION TAG
SEQADV 3QMW ASN D 4 UNP O54157 EXPRESSION TAG
SEQADV 3QMW ALA D 5 UNP O54157 EXPRESSION TAG
SEQRES 1 A 259 SER ASN ALA LEU LEU SER GLN ARG SER ALA TRP PHE PRO
SEQRES 2 A 259 ARG PRO VAL ALA ALA PRO ALA ALA GLU PRO PRO ASP PRO
SEQRES 3 A 259 ALA ALA ALA PRO LEU ARG LEU VAL CYS PHE PRO TYR ALA
SEQRES 4 A 259 GLY GLY THR VAL SER ALA PHE ARG GLY TRP GLN GLU ARG
SEQRES 5 A 259 LEU GLY ASP GLU VAL ALA VAL VAL PRO VAL GLN LEU PRO
SEQRES 6 A 259 GLY ARG GLY LEU ARG LEU ARG GLU ARG PRO TYR ASP THR
SEQRES 7 A 259 MET GLU PRO LEU ALA GLU ALA VAL ALA ASP ALA LEU GLU
SEQRES 8 A 259 GLU HIS ARG LEU THR HIS ASP TYR ALA LEU PHE GLY HIS
SEQRES 9 A 259 SER MET GLY ALA LEU LEU ALA TYR GLU VAL ALA CYS VAL
SEQRES 10 A 259 LEU ARG ARG ARG GLY ALA PRO ARG PRO ARG HIS LEU PHE
SEQRES 11 A 259 VAL SER GLY SER ARG ALA PRO HIS LEU TYR GLY ASP ARG
SEQRES 12 A 259 ALA ASP HIS THR LEU SER ASP THR ALA LEU ARG GLU VAL
SEQRES 13 A 259 ILE ARG ASP LEU GLY GLY LEU ASP ASP ALA ASP THR LEU
SEQRES 14 A 259 GLY ALA ALA TYR PHE ASP ARG ARG LEU PRO VAL LEU ARG
SEQRES 15 A 259 ALA ASP LEU ARG ALA CYS GLU ARG TYR ASP TRP HIS PRO
SEQRES 16 A 259 ARG PRO PRO LEU ASP CYS PRO THR THR ALA PHE SER ALA
SEQRES 17 A 259 ALA ALA ASP PRO ILE ALA THR PRO GLU MET VAL GLU ALA
SEQRES 18 A 259 TRP ARG PRO TYR THR THR GLY SER PHE LEU ARG ARG HIS
SEQRES 19 A 259 LEU PRO GLY ASN HIS PHE PHE LEU ASN GLY GLY PRO SER
SEQRES 20 A 259 ARG ASP ARG LEU LEU ALA HIS LEU GLY THR GLU LEU
SEQRES 1 B 259 SER ASN ALA LEU LEU SER GLN ARG SER ALA TRP PHE PRO
SEQRES 2 B 259 ARG PRO VAL ALA ALA PRO ALA ALA GLU PRO PRO ASP PRO
SEQRES 3 B 259 ALA ALA ALA PRO LEU ARG LEU VAL CYS PHE PRO TYR ALA
SEQRES 4 B 259 GLY GLY THR VAL SER ALA PHE ARG GLY TRP GLN GLU ARG
SEQRES 5 B 259 LEU GLY ASP GLU VAL ALA VAL VAL PRO VAL GLN LEU PRO
SEQRES 6 B 259 GLY ARG GLY LEU ARG LEU ARG GLU ARG PRO TYR ASP THR
SEQRES 7 B 259 MET GLU PRO LEU ALA GLU ALA VAL ALA ASP ALA LEU GLU
SEQRES 8 B 259 GLU HIS ARG LEU THR HIS ASP TYR ALA LEU PHE GLY HIS
SEQRES 9 B 259 SER MET GLY ALA LEU LEU ALA TYR GLU VAL ALA CYS VAL
SEQRES 10 B 259 LEU ARG ARG ARG GLY ALA PRO ARG PRO ARG HIS LEU PHE
SEQRES 11 B 259 VAL SER GLY SER ARG ALA PRO HIS LEU TYR GLY ASP ARG
SEQRES 12 B 259 ALA ASP HIS THR LEU SER ASP THR ALA LEU ARG GLU VAL
SEQRES 13 B 259 ILE ARG ASP LEU GLY GLY LEU ASP ASP ALA ASP THR LEU
SEQRES 14 B 259 GLY ALA ALA TYR PHE ASP ARG ARG LEU PRO VAL LEU ARG
SEQRES 15 B 259 ALA ASP LEU ARG ALA CYS GLU ARG TYR ASP TRP HIS PRO
SEQRES 16 B 259 ARG PRO PRO LEU ASP CYS PRO THR THR ALA PHE SER ALA
SEQRES 17 B 259 ALA ALA ASP PRO ILE ALA THR PRO GLU MET VAL GLU ALA
SEQRES 18 B 259 TRP ARG PRO TYR THR THR GLY SER PHE LEU ARG ARG HIS
SEQRES 19 B 259 LEU PRO GLY ASN HIS PHE PHE LEU ASN GLY GLY PRO SER
SEQRES 20 B 259 ARG ASP ARG LEU LEU ALA HIS LEU GLY THR GLU LEU
SEQRES 1 C 259 SER ASN ALA LEU LEU SER GLN ARG SER ALA TRP PHE PRO
SEQRES 2 C 259 ARG PRO VAL ALA ALA PRO ALA ALA GLU PRO PRO ASP PRO
SEQRES 3 C 259 ALA ALA ALA PRO LEU ARG LEU VAL CYS PHE PRO TYR ALA
SEQRES 4 C 259 GLY GLY THR VAL SER ALA PHE ARG GLY TRP GLN GLU ARG
SEQRES 5 C 259 LEU GLY ASP GLU VAL ALA VAL VAL PRO VAL GLN LEU PRO
SEQRES 6 C 259 GLY ARG GLY LEU ARG LEU ARG GLU ARG PRO TYR ASP THR
SEQRES 7 C 259 MET GLU PRO LEU ALA GLU ALA VAL ALA ASP ALA LEU GLU
SEQRES 8 C 259 GLU HIS ARG LEU THR HIS ASP TYR ALA LEU PHE GLY HIS
SEQRES 9 C 259 SER MET GLY ALA LEU LEU ALA TYR GLU VAL ALA CYS VAL
SEQRES 10 C 259 LEU ARG ARG ARG GLY ALA PRO ARG PRO ARG HIS LEU PHE
SEQRES 11 C 259 VAL SER GLY SER ARG ALA PRO HIS LEU TYR GLY ASP ARG
SEQRES 12 C 259 ALA ASP HIS THR LEU SER ASP THR ALA LEU ARG GLU VAL
SEQRES 13 C 259 ILE ARG ASP LEU GLY GLY LEU ASP ASP ALA ASP THR LEU
SEQRES 14 C 259 GLY ALA ALA TYR PHE ASP ARG ARG LEU PRO VAL LEU ARG
SEQRES 15 C 259 ALA ASP LEU ARG ALA CYS GLU ARG TYR ASP TRP HIS PRO
SEQRES 16 C 259 ARG PRO PRO LEU ASP CYS PRO THR THR ALA PHE SER ALA
SEQRES 17 C 259 ALA ALA ASP PRO ILE ALA THR PRO GLU MET VAL GLU ALA
SEQRES 18 C 259 TRP ARG PRO TYR THR THR GLY SER PHE LEU ARG ARG HIS
SEQRES 19 C 259 LEU PRO GLY ASN HIS PHE PHE LEU ASN GLY GLY PRO SER
SEQRES 20 C 259 ARG ASP ARG LEU LEU ALA HIS LEU GLY THR GLU LEU
SEQRES 1 D 259 SER ASN ALA LEU LEU SER GLN ARG SER ALA TRP PHE PRO
SEQRES 2 D 259 ARG PRO VAL ALA ALA PRO ALA ALA GLU PRO PRO ASP PRO
SEQRES 3 D 259 ALA ALA ALA PRO LEU ARG LEU VAL CYS PHE PRO TYR ALA
SEQRES 4 D 259 GLY GLY THR VAL SER ALA PHE ARG GLY TRP GLN GLU ARG
SEQRES 5 D 259 LEU GLY ASP GLU VAL ALA VAL VAL PRO VAL GLN LEU PRO
SEQRES 6 D 259 GLY ARG GLY LEU ARG LEU ARG GLU ARG PRO TYR ASP THR
SEQRES 7 D 259 MET GLU PRO LEU ALA GLU ALA VAL ALA ASP ALA LEU GLU
SEQRES 8 D 259 GLU HIS ARG LEU THR HIS ASP TYR ALA LEU PHE GLY HIS
SEQRES 9 D 259 SER MET GLY ALA LEU LEU ALA TYR GLU VAL ALA CYS VAL
SEQRES 10 D 259 LEU ARG ARG ARG GLY ALA PRO ARG PRO ARG HIS LEU PHE
SEQRES 11 D 259 VAL SER GLY SER ARG ALA PRO HIS LEU TYR GLY ASP ARG
SEQRES 12 D 259 ALA ASP HIS THR LEU SER ASP THR ALA LEU ARG GLU VAL
SEQRES 13 D 259 ILE ARG ASP LEU GLY GLY LEU ASP ASP ALA ASP THR LEU
SEQRES 14 D 259 GLY ALA ALA TYR PHE ASP ARG ARG LEU PRO VAL LEU ARG
SEQRES 15 D 259 ALA ASP LEU ARG ALA CYS GLU ARG TYR ASP TRP HIS PRO
SEQRES 16 D 259 ARG PRO PRO LEU ASP CYS PRO THR THR ALA PHE SER ALA
SEQRES 17 D 259 ALA ALA ASP PRO ILE ALA THR PRO GLU MET VAL GLU ALA
SEQRES 18 D 259 TRP ARG PRO TYR THR THR GLY SER PHE LEU ARG ARG HIS
SEQRES 19 D 259 LEU PRO GLY ASN HIS PHE PHE LEU ASN GLY GLY PRO SER
SEQRES 20 D 259 ARG ASP ARG LEU LEU ALA HIS LEU GLY THR GLU LEU
HET PG4 B 1 13
HETNAM PG4 TETRAETHYLENE GLYCOL
FORMUL 5 PG4 C8 H18 O5
FORMUL 6 HOH *151(H2 O)
HELIX 1 1 THR A 44 ARG A 49 5 6
HELIX 2 2 GLY A 50 GLY A 56 1 7
HELIX 3 3 ARG A 69 LEU A 73 5 5
HELIX 4 4 THR A 80 HIS A 95 1 16
HELIX 5 5 SER A 107 ARG A 123 1 17
HELIX 6 6 ALA A 138 TYR A 142 5 5
HELIX 7 7 ALA A 146 LEU A 150 5 5
HELIX 8 8 SER A 151 LEU A 162 1 12
HELIX 9 9 TYR A 175 ARG A 192 1 18
HELIX 10 10 THR A 217 ALA A 223 1 7
HELIX 11 11 TRP A 224 THR A 228 5 5
HELIX 12 12 GLY A 246 LEU A 261 1 16
HELIX 13 13 THR B 44 ARG B 49 5 6
HELIX 14 14 GLY B 50 GLY B 56 1 7
HELIX 15 15 ARG B 69 LEU B 73 5 5
HELIX 16 16 THR B 80 HIS B 95 1 16
HELIX 17 17 SER B 107 GLY B 124 1 18
HELIX 18 18 ALA B 138 TYR B 142 5 5
HELIX 19 19 SER B 151 GLY B 163 1 13
HELIX 20 20 ASP B 167 GLY B 172 1 6
HELIX 21 21 GLY B 172 TYR B 193 1 22
HELIX 22 22 THR B 217 ALA B 223 1 7
HELIX 23 23 TRP B 224 THR B 228 5 5
HELIX 24 24 PHE B 242 GLY B 246 5 5
HELIX 25 25 GLY B 247 THR B 259 1 13
HELIX 26 26 GLU B 260 LEU B 261 5 2
HELIX 27 27 LEU C 6 SER C 11 5 6
HELIX 28 28 THR C 44 PHE C 48 5 5
HELIX 29 29 GLY C 50 LEU C 55 1 6
HELIX 30 30 ARG C 69 LEU C 73 5 5
HELIX 31 31 THR C 80 HIS C 95 1 16
HELIX 32 32 SER C 107 GLY C 124 1 18
HELIX 33 33 ALA C 138 TYR C 142 5 5
HELIX 34 34 ALA C 146 LEU C 150 5 5
HELIX 35 35 SER C 151 ASP C 161 1 11
HELIX 36 36 ARG C 179 ARG C 192 1 14
HELIX 37 37 THR C 217 ALA C 223 1 7
HELIX 38 38 TRP C 224 THR C 228 5 5
HELIX 39 39 PHE C 242 GLY C 246 5 5
HELIX 40 40 GLY C 247 GLU C 260 1 14
HELIX 41 41 THR D 44 ARG D 49 5 6
HELIX 42 42 GLY D 50 GLY D 56 1 7
HELIX 43 43 ARG D 69 LEU D 73 5 5
HELIX 44 44 THR D 80 GLU D 94 1 15
HELIX 45 45 SER D 107 ARG D 123 1 17
HELIX 46 46 ALA D 138 TYR D 142 5 5
HELIX 47 47 SER D 151 LEU D 162 1 12
HELIX 48 48 THR D 170 ARG D 179 1 10
HELIX 49 49 ARG D 179 ARG D 192 1 14
HELIX 50 50 THR D 217 ALA D 223 1 7
HELIX 51 51 TRP D 224 THR D 228 5 5
HELIX 52 52 PHE D 242 GLY D 246 5 5
HELIX 53 53 GLY D 247 LEU D 261 1 15
SHEET 1 A 6 VAL A 59 PRO A 63 0
SHEET 2 A 6 LEU A 33 PHE A 38 1 N LEU A 33 O ALA A 60
SHEET 3 A 6 TYR A 101 HIS A 106 1 O ALA A 102 N VAL A 36
SHEET 4 A 6 LEU A 131 SER A 134 1 O PHE A 132 N LEU A 103
SHEET 5 A 6 THR A 205 ALA A 210 1 O THR A 206 N VAL A 133
SHEET 6 A 6 PHE A 232 LEU A 237 1 O LEU A 233 N ALA A 207
SHEET 1 B 6 VAL B 59 PRO B 63 0
SHEET 2 B 6 LEU B 33 PHE B 38 1 N LEU B 35 O VAL B 62
SHEET 3 B 6 TYR B 101 HIS B 106 1 O ALA B 102 N ARG B 34
SHEET 4 B 6 HIS B 130 SER B 134 1 O PHE B 132 N LEU B 103
SHEET 5 B 6 THR B 205 ALA B 210 1 O PHE B 208 N VAL B 133
SHEET 6 B 6 PHE B 232 LEU B 237 1 O ARG B 235 N ALA B 207
SHEET 1 C 6 VAL C 59 PRO C 63 0
SHEET 2 C 6 LEU C 33 PHE C 38 1 N LEU C 35 O ALA C 60
SHEET 3 C 6 TYR C 101 HIS C 106 1 O PHE C 104 N PHE C 38
SHEET 4 C 6 LEU C 131 SER C 134 1 O PHE C 132 N LEU C 103
SHEET 5 C 6 THR C 205 ALA C 212 1 O THR C 206 N LEU C 131
SHEET 6 C 6 PHE C 232 ASN C 240 1 O LEU C 237 N ALA C 211
SHEET 1 D 6 VAL D 59 PRO D 63 0
SHEET 2 D 6 LEU D 33 PHE D 38 1 N LEU D 35 O ALA D 60
SHEET 3 D 6 TYR D 101 HIS D 106 1 O PHE D 104 N PHE D 38
SHEET 4 D 6 LEU D 131 SER D 134 1 O PHE D 132 N LEU D 103
SHEET 5 D 6 THR D 205 ALA D 210 1 O THR D 206 N LEU D 131
SHEET 6 D 6 PHE D 232 LEU D 237 1 O LEU D 237 N SER D 209
SITE 1 AC1 3 LEU B 150 VAL B 158 LEU B 187
CRYST1 155.545 45.013 156.403 90.00 109.49 90.00 C 1 2 1 16
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 0.006429 0.000000 0.002275 0.00000
SCALE2 0.000000 0.022216 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006782 0.00000
TER 1927 LEU A 261
TER 3860 LEU B 261
TER 5749 LEU C 261
TER 7707 LEU D 261
MASTER 338 0 1 53 24 0 1 6 7856 4 13 80
END |