| content |
HEADER HYDROLASE 05-FEB-11 3QMV
TITLE REDJ-THIOESTERASE FROM THE PRODIGININE BIOSYNTHETIC PATHWAY IN
TITLE 2 STREPTOMYCES COELICOLOR
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 3QMV 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. 2.12 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) : 2.12
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 : 57954
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) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2945
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) : 2.12
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.17
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3814
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.47
REMARK 3 BIN R VALUE (WORKING SET) : 0.2420
REMARK 3 BIN FREE R VALUE SET COUNT : 192
REMARK 3 BIN FREE R VALUE : 0.2960
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8088
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 452
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.21
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.10000
REMARK 3 B22 (A**2) : -1.97000
REMARK 3 B33 (A**2) : 3.07000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.75000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.280
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.213
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 : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.926
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8425 ; 0.012 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 5959 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11507 ; 1.241 ; 1.969
REMARK 3 BOND ANGLES OTHERS (DEGREES): 14216 ; 4.027 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1045 ; 5.387 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 413 ;25.361 ;20.775
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1216 ;13.468 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 125 ;14.997 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1209 ; 0.075 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9627 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1946 ; 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): 5235 ; 0.678 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2058 ; 0.000 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8390 ; 1.271 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3190 ; 1.670 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3117 ; 2.762 ; 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 3QMV 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 RCSB063844.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-AUG-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.6
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) : 0.9794
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 : 57954
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.120
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08900
REMARK 200 FOR THE DATA SET : 22.1200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.12
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 7.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.42000
REMARK 200 FOR SHELL : 5.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG2000, 0.7 M SODIUM CHLORIDE, 2
REMARK 280 MM DTT, 0.1 M HEPES, PH 7.6, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
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 39.69950
REMARK 290 SMTRY3 2 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: 4200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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: 4300 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23190 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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 MSE A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 SER A -11
REMARK 465 SER A -10
REMARK 465 GLY A -9
REMARK 465 VAL A -8
REMARK 465 ASP A -7
REMARK 465 LEU A -6
REMARK 465 GLY A -5
REMARK 465 THR A -4
REMARK 465 GLU A -3
REMARK 465 ASN A -2
REMARK 465 LEU A -1
REMARK 465 TYR A 0
REMARK 465 PHE A 1
REMARK 465 GLN A 2
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 ASP A 167
REMARK 465 ALA A 168
REMARK 465 ASP A 169
REMARK 465 THR A 170
REMARK 465 LEU A 171
REMARK 465 GLY A 172
REMARK 465 ALA A 173
REMARK 465 ALA A 174
REMARK 465 TYR A 175
REMARK 465 MSE B -18
REMARK 465 HIS B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 SER B -11
REMARK 465 SER B -10
REMARK 465 GLY B -9
REMARK 465 VAL B -8
REMARK 465 ASP B -7
REMARK 465 LEU B -6
REMARK 465 GLY B -5
REMARK 465 THR B -4
REMARK 465 GLU B -3
REMARK 465 ASN B -2
REMARK 465 LEU B -1
REMARK 465 TYR B 0
REMARK 465 PHE B 1
REMARK 465 GLN B 2
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 MSE C -18
REMARK 465 HIS C -17
REMARK 465 HIS C -16
REMARK 465 HIS C -15
REMARK 465 HIS C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 SER C -11
REMARK 465 SER C -10
REMARK 465 GLY C -9
REMARK 465 VAL C -8
REMARK 465 ALA C 23
REMARK 465 MSE D -18
REMARK 465 HIS D -17
REMARK 465 HIS D -16
REMARK 465 HIS D -15
REMARK 465 HIS D -14
REMARK 465 HIS D -13
REMARK 465 HIS D -12
REMARK 465 SER D -11
REMARK 465 SER D -10
REMARK 465 GLY D -9
REMARK 465 VAL D -8
REMARK 465 PRO D 21
REMARK 465 ALA D 22
REMARK 465 ALA D 23
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 -124.71 58.61
REMARK 500 SER B 107 -119.36 57.72
REMARK 500 SER C 107 -121.19 59.11
REMARK 500 SER D 107 -120.72 60.66
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH C 274 DISTANCE = 5.10 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3QMW RELATED DB: PDB
REMARK 900 STRUCTURE OF REDJ WITH PEG BOUND IN THE ACTIVE SITE.
DBREF 3QMV A 6 261 UNP O54157 O54157_STRCO 6 261
DBREF 3QMV B 6 261 UNP O54157 O54157_STRCO 6 261
DBREF 3QMV C 6 261 UNP O54157 O54157_STRCO 6 261
DBREF 3QMV D 6 261 UNP O54157 O54157_STRCO 6 261
SEQADV 3QMV MSE A -18 UNP O54157 EXPRESSION TAG
SEQADV 3QMV HIS A -17 UNP O54157 EXPRESSION TAG
SEQADV 3QMV HIS A -16 UNP O54157 EXPRESSION TAG
SEQADV 3QMV HIS A -15 UNP O54157 EXPRESSION TAG
SEQADV 3QMV HIS A -14 UNP O54157 EXPRESSION TAG
SEQADV 3QMV HIS A -13 UNP O54157 EXPRESSION TAG
SEQADV 3QMV HIS A -12 UNP O54157 EXPRESSION TAG
SEQADV 3QMV SER A -11 UNP O54157 EXPRESSION TAG
SEQADV 3QMV SER A -10 UNP O54157 EXPRESSION TAG
SEQADV 3QMV GLY A -9 UNP O54157 EXPRESSION TAG
SEQADV 3QMV VAL A -8 UNP O54157 EXPRESSION TAG
SEQADV 3QMV ASP A -7 UNP O54157 EXPRESSION TAG
SEQADV 3QMV LEU A -6 UNP O54157 EXPRESSION TAG
SEQADV 3QMV GLY A -5 UNP O54157 EXPRESSION TAG
SEQADV 3QMV THR A -4 UNP O54157 EXPRESSION TAG
SEQADV 3QMV GLU A -3 UNP O54157 EXPRESSION TAG
SEQADV 3QMV ASN A -2 UNP O54157 EXPRESSION TAG
SEQADV 3QMV LEU A -1 UNP O54157 EXPRESSION TAG
SEQADV 3QMV TYR A 0 UNP O54157 EXPRESSION TAG
SEQADV 3QMV PHE A 1 UNP O54157 EXPRESSION TAG
SEQADV 3QMV GLN A 2 UNP O54157 EXPRESSION TAG
SEQADV 3QMV SER A 3 UNP O54157 EXPRESSION TAG
SEQADV 3QMV ASN A 4 UNP O54157 EXPRESSION TAG
SEQADV 3QMV ALA A 5 UNP O54157 EXPRESSION TAG
SEQADV 3QMV MSE B -18 UNP O54157 EXPRESSION TAG
SEQADV 3QMV HIS B -17 UNP O54157 EXPRESSION TAG
SEQADV 3QMV HIS B -16 UNP O54157 EXPRESSION TAG
SEQADV 3QMV HIS B -15 UNP O54157 EXPRESSION TAG
SEQADV 3QMV HIS B -14 UNP O54157 EXPRESSION TAG
SEQADV 3QMV HIS B -13 UNP O54157 EXPRESSION TAG
SEQADV 3QMV HIS B -12 UNP O54157 EXPRESSION TAG
SEQADV 3QMV SER B -11 UNP O54157 EXPRESSION TAG
SEQADV 3QMV SER B -10 UNP O54157 EXPRESSION TAG
SEQADV 3QMV GLY B -9 UNP O54157 EXPRESSION TAG
SEQADV 3QMV VAL B -8 UNP O54157 EXPRESSION TAG
SEQADV 3QMV ASP B -7 UNP O54157 EXPRESSION TAG
SEQADV 3QMV LEU B -6 UNP O54157 EXPRESSION TAG
SEQADV 3QMV GLY B -5 UNP O54157 EXPRESSION TAG
SEQADV 3QMV THR B -4 UNP O54157 EXPRESSION TAG
SEQADV 3QMV GLU B -3 UNP O54157 EXPRESSION TAG
SEQADV 3QMV ASN B -2 UNP O54157 EXPRESSION TAG
SEQADV 3QMV LEU B -1 UNP O54157 EXPRESSION TAG
SEQADV 3QMV TYR B 0 UNP O54157 EXPRESSION TAG
SEQADV 3QMV PHE B 1 UNP O54157 EXPRESSION TAG
SEQADV 3QMV GLN B 2 UNP O54157 EXPRESSION TAG
SEQADV 3QMV SER B 3 UNP O54157 EXPRESSION TAG
SEQADV 3QMV ASN B 4 UNP O54157 EXPRESSION TAG
SEQADV 3QMV ALA B 5 UNP O54157 EXPRESSION TAG
SEQADV 3QMV MSE C -18 UNP O54157 EXPRESSION TAG
SEQADV 3QMV HIS C -17 UNP O54157 EXPRESSION TAG
SEQADV 3QMV HIS C -16 UNP O54157 EXPRESSION TAG
SEQADV 3QMV HIS C -15 UNP O54157 EXPRESSION TAG
SEQADV 3QMV HIS C -14 UNP O54157 EXPRESSION TAG
SEQADV 3QMV HIS C -13 UNP O54157 EXPRESSION TAG
SEQADV 3QMV HIS C -12 UNP O54157 EXPRESSION TAG
SEQADV 3QMV SER C -11 UNP O54157 EXPRESSION TAG
SEQADV 3QMV SER C -10 UNP O54157 EXPRESSION TAG
SEQADV 3QMV GLY C -9 UNP O54157 EXPRESSION TAG
SEQADV 3QMV VAL C -8 UNP O54157 EXPRESSION TAG
SEQADV 3QMV ASP C -7 UNP O54157 EXPRESSION TAG
SEQADV 3QMV LEU C -6 UNP O54157 EXPRESSION TAG
SEQADV 3QMV GLY C -5 UNP O54157 EXPRESSION TAG
SEQADV 3QMV THR C -4 UNP O54157 EXPRESSION TAG
SEQADV 3QMV GLU C -3 UNP O54157 EXPRESSION TAG
SEQADV 3QMV ASN C -2 UNP O54157 EXPRESSION TAG
SEQADV 3QMV LEU C -1 UNP O54157 EXPRESSION TAG
SEQADV 3QMV TYR C 0 UNP O54157 EXPRESSION TAG
SEQADV 3QMV PHE C 1 UNP O54157 EXPRESSION TAG
SEQADV 3QMV GLN C 2 UNP O54157 EXPRESSION TAG
SEQADV 3QMV SER C 3 UNP O54157 EXPRESSION TAG
SEQADV 3QMV ASN C 4 UNP O54157 EXPRESSION TAG
SEQADV 3QMV ALA C 5 UNP O54157 EXPRESSION TAG
SEQADV 3QMV MSE D -18 UNP O54157 EXPRESSION TAG
SEQADV 3QMV HIS D -17 UNP O54157 EXPRESSION TAG
SEQADV 3QMV HIS D -16 UNP O54157 EXPRESSION TAG
SEQADV 3QMV HIS D -15 UNP O54157 EXPRESSION TAG
SEQADV 3QMV HIS D -14 UNP O54157 EXPRESSION TAG
SEQADV 3QMV HIS D -13 UNP O54157 EXPRESSION TAG
SEQADV 3QMV HIS D -12 UNP O54157 EXPRESSION TAG
SEQADV 3QMV SER D -11 UNP O54157 EXPRESSION TAG
SEQADV 3QMV SER D -10 UNP O54157 EXPRESSION TAG
SEQADV 3QMV GLY D -9 UNP O54157 EXPRESSION TAG
SEQADV 3QMV VAL D -8 UNP O54157 EXPRESSION TAG
SEQADV 3QMV ASP D -7 UNP O54157 EXPRESSION TAG
SEQADV 3QMV LEU D -6 UNP O54157 EXPRESSION TAG
SEQADV 3QMV GLY D -5 UNP O54157 EXPRESSION TAG
SEQADV 3QMV THR D -4 UNP O54157 EXPRESSION TAG
SEQADV 3QMV GLU D -3 UNP O54157 EXPRESSION TAG
SEQADV 3QMV ASN D -2 UNP O54157 EXPRESSION TAG
SEQADV 3QMV LEU D -1 UNP O54157 EXPRESSION TAG
SEQADV 3QMV TYR D 0 UNP O54157 EXPRESSION TAG
SEQADV 3QMV PHE D 1 UNP O54157 EXPRESSION TAG
SEQADV 3QMV GLN D 2 UNP O54157 EXPRESSION TAG
SEQADV 3QMV SER D 3 UNP O54157 EXPRESSION TAG
SEQADV 3QMV ASN D 4 UNP O54157 EXPRESSION TAG
SEQADV 3QMV ALA D 5 UNP O54157 EXPRESSION TAG
SEQRES 1 A 280 MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 280 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA LEU LEU
SEQRES 3 A 280 SER GLN ARG SER ALA TRP PHE PRO ARG PRO VAL ALA ALA
SEQRES 4 A 280 PRO ALA ALA GLU PRO PRO ASP PRO ALA ALA ALA PRO LEU
SEQRES 5 A 280 ARG LEU VAL CYS PHE PRO TYR ALA GLY GLY THR VAL SER
SEQRES 6 A 280 ALA PHE ARG GLY TRP GLN GLU ARG LEU GLY ASP GLU VAL
SEQRES 7 A 280 ALA VAL VAL PRO VAL GLN LEU PRO GLY ARG GLY LEU ARG
SEQRES 8 A 280 LEU ARG GLU ARG PRO TYR ASP THR MSE GLU PRO LEU ALA
SEQRES 9 A 280 GLU ALA VAL ALA ASP ALA LEU GLU GLU HIS ARG LEU THR
SEQRES 10 A 280 HIS ASP TYR ALA LEU PHE GLY HIS SER MSE GLY ALA LEU
SEQRES 11 A 280 LEU ALA TYR GLU VAL ALA CYS VAL LEU ARG ARG ARG GLY
SEQRES 12 A 280 ALA PRO ARG PRO ARG HIS LEU PHE VAL SER GLY SER ARG
SEQRES 13 A 280 ALA PRO HIS LEU TYR GLY ASP ARG ALA ASP HIS THR LEU
SEQRES 14 A 280 SER ASP THR ALA LEU ARG GLU VAL ILE ARG ASP LEU GLY
SEQRES 15 A 280 GLY LEU ASP ASP ALA ASP THR LEU GLY ALA ALA TYR PHE
SEQRES 16 A 280 ASP ARG ARG LEU PRO VAL LEU ARG ALA ASP LEU ARG ALA
SEQRES 17 A 280 CYS GLU ARG TYR ASP TRP HIS PRO ARG PRO PRO LEU ASP
SEQRES 18 A 280 CYS PRO THR THR ALA PHE SER ALA ALA ALA ASP PRO ILE
SEQRES 19 A 280 ALA THR PRO GLU MSE VAL GLU ALA TRP ARG PRO TYR THR
SEQRES 20 A 280 THR GLY SER PHE LEU ARG ARG HIS LEU PRO GLY ASN HIS
SEQRES 21 A 280 PHE PHE LEU ASN GLY GLY PRO SER ARG ASP ARG LEU LEU
SEQRES 22 A 280 ALA HIS LEU GLY THR GLU LEU
SEQRES 1 B 280 MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 B 280 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA LEU LEU
SEQRES 3 B 280 SER GLN ARG SER ALA TRP PHE PRO ARG PRO VAL ALA ALA
SEQRES 4 B 280 PRO ALA ALA GLU PRO PRO ASP PRO ALA ALA ALA PRO LEU
SEQRES 5 B 280 ARG LEU VAL CYS PHE PRO TYR ALA GLY GLY THR VAL SER
SEQRES 6 B 280 ALA PHE ARG GLY TRP GLN GLU ARG LEU GLY ASP GLU VAL
SEQRES 7 B 280 ALA VAL VAL PRO VAL GLN LEU PRO GLY ARG GLY LEU ARG
SEQRES 8 B 280 LEU ARG GLU ARG PRO TYR ASP THR MSE GLU PRO LEU ALA
SEQRES 9 B 280 GLU ALA VAL ALA ASP ALA LEU GLU GLU HIS ARG LEU THR
SEQRES 10 B 280 HIS ASP TYR ALA LEU PHE GLY HIS SER MSE GLY ALA LEU
SEQRES 11 B 280 LEU ALA TYR GLU VAL ALA CYS VAL LEU ARG ARG ARG GLY
SEQRES 12 B 280 ALA PRO ARG PRO ARG HIS LEU PHE VAL SER GLY SER ARG
SEQRES 13 B 280 ALA PRO HIS LEU TYR GLY ASP ARG ALA ASP HIS THR LEU
SEQRES 14 B 280 SER ASP THR ALA LEU ARG GLU VAL ILE ARG ASP LEU GLY
SEQRES 15 B 280 GLY LEU ASP ASP ALA ASP THR LEU GLY ALA ALA TYR PHE
SEQRES 16 B 280 ASP ARG ARG LEU PRO VAL LEU ARG ALA ASP LEU ARG ALA
SEQRES 17 B 280 CYS GLU ARG TYR ASP TRP HIS PRO ARG PRO PRO LEU ASP
SEQRES 18 B 280 CYS PRO THR THR ALA PHE SER ALA ALA ALA ASP PRO ILE
SEQRES 19 B 280 ALA THR PRO GLU MSE VAL GLU ALA TRP ARG PRO TYR THR
SEQRES 20 B 280 THR GLY SER PHE LEU ARG ARG HIS LEU PRO GLY ASN HIS
SEQRES 21 B 280 PHE PHE LEU ASN GLY GLY PRO SER ARG ASP ARG LEU LEU
SEQRES 22 B 280 ALA HIS LEU GLY THR GLU LEU
SEQRES 1 C 280 MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 C 280 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA LEU LEU
SEQRES 3 C 280 SER GLN ARG SER ALA TRP PHE PRO ARG PRO VAL ALA ALA
SEQRES 4 C 280 PRO ALA ALA GLU PRO PRO ASP PRO ALA ALA ALA PRO LEU
SEQRES 5 C 280 ARG LEU VAL CYS PHE PRO TYR ALA GLY GLY THR VAL SER
SEQRES 6 C 280 ALA PHE ARG GLY TRP GLN GLU ARG LEU GLY ASP GLU VAL
SEQRES 7 C 280 ALA VAL VAL PRO VAL GLN LEU PRO GLY ARG GLY LEU ARG
SEQRES 8 C 280 LEU ARG GLU ARG PRO TYR ASP THR MSE GLU PRO LEU ALA
SEQRES 9 C 280 GLU ALA VAL ALA ASP ALA LEU GLU GLU HIS ARG LEU THR
SEQRES 10 C 280 HIS ASP TYR ALA LEU PHE GLY HIS SER MSE GLY ALA LEU
SEQRES 11 C 280 LEU ALA TYR GLU VAL ALA CYS VAL LEU ARG ARG ARG GLY
SEQRES 12 C 280 ALA PRO ARG PRO ARG HIS LEU PHE VAL SER GLY SER ARG
SEQRES 13 C 280 ALA PRO HIS LEU TYR GLY ASP ARG ALA ASP HIS THR LEU
SEQRES 14 C 280 SER ASP THR ALA LEU ARG GLU VAL ILE ARG ASP LEU GLY
SEQRES 15 C 280 GLY LEU ASP ASP ALA ASP THR LEU GLY ALA ALA TYR PHE
SEQRES 16 C 280 ASP ARG ARG LEU PRO VAL LEU ARG ALA ASP LEU ARG ALA
SEQRES 17 C 280 CYS GLU ARG TYR ASP TRP HIS PRO ARG PRO PRO LEU ASP
SEQRES 18 C 280 CYS PRO THR THR ALA PHE SER ALA ALA ALA ASP PRO ILE
SEQRES 19 C 280 ALA THR PRO GLU MSE VAL GLU ALA TRP ARG PRO TYR THR
SEQRES 20 C 280 THR GLY SER PHE LEU ARG ARG HIS LEU PRO GLY ASN HIS
SEQRES 21 C 280 PHE PHE LEU ASN GLY GLY PRO SER ARG ASP ARG LEU LEU
SEQRES 22 C 280 ALA HIS LEU GLY THR GLU LEU
SEQRES 1 D 280 MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 D 280 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA LEU LEU
SEQRES 3 D 280 SER GLN ARG SER ALA TRP PHE PRO ARG PRO VAL ALA ALA
SEQRES 4 D 280 PRO ALA ALA GLU PRO PRO ASP PRO ALA ALA ALA PRO LEU
SEQRES 5 D 280 ARG LEU VAL CYS PHE PRO TYR ALA GLY GLY THR VAL SER
SEQRES 6 D 280 ALA PHE ARG GLY TRP GLN GLU ARG LEU GLY ASP GLU VAL
SEQRES 7 D 280 ALA VAL VAL PRO VAL GLN LEU PRO GLY ARG GLY LEU ARG
SEQRES 8 D 280 LEU ARG GLU ARG PRO TYR ASP THR MSE GLU PRO LEU ALA
SEQRES 9 D 280 GLU ALA VAL ALA ASP ALA LEU GLU GLU HIS ARG LEU THR
SEQRES 10 D 280 HIS ASP TYR ALA LEU PHE GLY HIS SER MSE GLY ALA LEU
SEQRES 11 D 280 LEU ALA TYR GLU VAL ALA CYS VAL LEU ARG ARG ARG GLY
SEQRES 12 D 280 ALA PRO ARG PRO ARG HIS LEU PHE VAL SER GLY SER ARG
SEQRES 13 D 280 ALA PRO HIS LEU TYR GLY ASP ARG ALA ASP HIS THR LEU
SEQRES 14 D 280 SER ASP THR ALA LEU ARG GLU VAL ILE ARG ASP LEU GLY
SEQRES 15 D 280 GLY LEU ASP ASP ALA ASP THR LEU GLY ALA ALA TYR PHE
SEQRES 16 D 280 ASP ARG ARG LEU PRO VAL LEU ARG ALA ASP LEU ARG ALA
SEQRES 17 D 280 CYS GLU ARG TYR ASP TRP HIS PRO ARG PRO PRO LEU ASP
SEQRES 18 D 280 CYS PRO THR THR ALA PHE SER ALA ALA ALA ASP PRO ILE
SEQRES 19 D 280 ALA THR PRO GLU MSE VAL GLU ALA TRP ARG PRO TYR THR
SEQRES 20 D 280 THR GLY SER PHE LEU ARG ARG HIS LEU PRO GLY ASN HIS
SEQRES 21 D 280 PHE PHE LEU ASN GLY GLY PRO SER ARG ASP ARG LEU LEU
SEQRES 22 D 280 ALA HIS LEU GLY THR GLU LEU
MODRES 3QMV MSE A 81 MET SELENOMETHIONINE
MODRES 3QMV MSE A 108 MET SELENOMETHIONINE
MODRES 3QMV MSE A 220 MET SELENOMETHIONINE
MODRES 3QMV MSE B 81 MET SELENOMETHIONINE
MODRES 3QMV MSE B 108 MET SELENOMETHIONINE
MODRES 3QMV MSE B 220 MET SELENOMETHIONINE
MODRES 3QMV MSE C 81 MET SELENOMETHIONINE
MODRES 3QMV MSE C 108 MET SELENOMETHIONINE
MODRES 3QMV MSE C 220 MET SELENOMETHIONINE
MODRES 3QMV MSE D 81 MET SELENOMETHIONINE
MODRES 3QMV MSE D 108 MET SELENOMETHIONINE
MODRES 3QMV MSE D 220 MET SELENOMETHIONINE
HET MSE A 81 8
HET MSE A 108 8
HET MSE A 220 8
HET MSE B 81 8
HET MSE B 108 8
HET MSE B 220 8
HET MSE C 81 8
HET MSE C 108 8
HET MSE C 220 8
HET MSE D 81 8
HET MSE D 108 8
HET MSE D 220 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 12(C5 H11 N O2 SE)
FORMUL 5 HOH *452(H2 O)
HELIX 1 1 GLN A 9 PHE A 14 1 6
HELIX 2 2 THR A 44 ARG A 49 5 6
HELIX 3 3 GLY A 50 GLY A 56 1 7
HELIX 4 4 ARG A 69 LEU A 73 5 5
HELIX 5 5 THR A 80 HIS A 95 1 16
HELIX 6 6 SER A 107 ARG A 123 1 17
HELIX 7 7 ALA A 138 TYR A 142 5 5
HELIX 8 8 ALA A 146 LEU A 150 5 5
HELIX 9 9 SER A 151 GLY A 163 1 13
HELIX 10 10 ARG A 179 ARG A 192 1 14
HELIX 11 11 THR A 217 ALA A 223 1 7
HELIX 12 12 TRP A 224 THR A 228 5 5
HELIX 13 13 PHE A 242 GLY A 246 5 5
HELIX 14 14 GLY A 247 THR A 259 1 13
HELIX 15 15 GLN B 9 PHE B 14 1 6
HELIX 16 16 THR B 44 ARG B 49 5 6
HELIX 17 17 GLY B 50 GLY B 56 1 7
HELIX 18 18 ARG B 69 LEU B 73 5 5
HELIX 19 19 THR B 80 HIS B 95 1 16
HELIX 20 20 SER B 107 ARG B 123 1 17
HELIX 21 21 ALA B 138 TYR B 142 5 5
HELIX 22 22 ALA B 146 LEU B 150 5 5
HELIX 23 23 SER B 151 GLY B 163 1 13
HELIX 24 24 ASP B 167 THR B 170 5 4
HELIX 25 25 LEU B 171 ARG B 192 1 22
HELIX 26 26 THR B 217 ALA B 223 1 7
HELIX 27 27 TRP B 224 THR B 228 5 5
HELIX 28 28 PHE B 242 ASN B 245 5 4
HELIX 29 29 GLY B 246 LEU B 261 1 16
HELIX 30 30 GLY C -5 LEU C -1 5 5
HELIX 31 31 ASN C 4 SER C 8 5 5
HELIX 32 32 GLN C 9 PHE C 14 1 6
HELIX 33 33 THR C 44 ARG C 49 5 6
HELIX 34 34 GLY C 50 GLY C 56 1 7
HELIX 35 35 ARG C 69 LEU C 73 5 5
HELIX 36 36 THR C 80 HIS C 95 1 16
HELIX 37 37 SER C 107 ARG C 123 1 17
HELIX 38 38 ALA C 138 TYR C 142 5 5
HELIX 39 39 ALA C 146 LEU C 150 5 5
HELIX 40 40 SER C 151 GLY C 163 1 13
HELIX 41 41 ASP C 167 GLY C 172 1 6
HELIX 42 42 ALA C 173 ARG C 178 1 6
HELIX 43 43 ARG C 179 ARG C 192 1 14
HELIX 44 44 THR C 217 ALA C 223 1 7
HELIX 45 45 TRP C 224 THR C 228 5 5
HELIX 46 46 PHE C 242 GLY C 246 5 5
HELIX 47 47 GLY C 247 LEU C 261 1 15
HELIX 48 48 GLY D -5 LEU D -1 5 5
HELIX 49 49 ALA D 5 SER D 8 5 4
HELIX 50 50 GLN D 9 PHE D 14 1 6
HELIX 51 51 THR D 44 ARG D 49 5 6
HELIX 52 52 GLY D 50 GLY D 56 1 7
HELIX 53 53 ARG D 69 LEU D 73 5 5
HELIX 54 54 THR D 80 HIS D 95 1 16
HELIX 55 55 SER D 107 ARG D 123 1 17
HELIX 56 56 ALA D 138 TYR D 142 5 5
HELIX 57 57 ALA D 146 LEU D 150 5 5
HELIX 58 58 SER D 151 GLY D 163 1 13
HELIX 59 59 ASP D 167 GLY D 172 1 6
HELIX 60 60 GLY D 172 ARG D 178 1 7
HELIX 61 61 ARG D 179 ARG D 192 1 14
HELIX 62 62 THR D 217 ALA D 223 1 7
HELIX 63 63 TRP D 224 THR D 228 5 5
HELIX 64 64 PHE D 242 GLY D 246 5 5
HELIX 65 65 GLY D 247 GLU D 260 1 14
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 35 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 212 1 O THR A 206 N LEU A 131
SHEET 6 A 6 PHE A 232 ASN A 240 1 O LEU A 237 N SER A 209
SHEET 1 B 6 ALA B 60 PRO B 63 0
SHEET 2 B 6 ARG B 34 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 VAL B 36
SHEET 4 B 6 LEU B 131 SER B 134 1 O PHE B 132 N LEU B 103
SHEET 5 B 6 THR B 205 ALA B 212 1 O PHE B 208 N VAL B 133
SHEET 6 B 6 PHE B 232 ASN B 240 1 O LEU B 237 N SER B 209
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 VAL C 62
SHEET 3 C 6 TYR C 101 HIS C 106 1 O ALA C 102 N VAL C 36
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 210 1 O THR C 206 N LEU C 131
SHEET 6 C 6 PHE C 232 LEU C 237 1 O LEU C 233 N ALA C 207
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 VAL D 62
SHEET 3 D 6 TYR D 101 HIS D 106 1 O PHE D 104 N VAL D 36
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 233 N ALA D 207
LINK C THR A 80 N MSE A 81 1555 1555 1.33
LINK C MSE A 81 N GLU A 82 1555 1555 1.33
LINK C ASER A 107 N MSE A 108 1555 1555 1.31
LINK C BSER A 107 N MSE A 108 1555 1555 1.31
LINK C MSE A 108 N GLY A 109 1555 1555 1.33
LINK C GLU A 219 N MSE A 220 1555 1555 1.33
LINK C MSE A 220 N VAL A 221 1555 1555 1.33
LINK C THR B 80 N MSE B 81 1555 1555 1.33
LINK C MSE B 81 N GLU B 82 1555 1555 1.34
LINK C ASER B 107 N MSE B 108 1555 1555 1.31
LINK C BSER B 107 N MSE B 108 1555 1555 1.31
LINK C MSE B 108 N GLY B 109 1555 1555 1.33
LINK C GLU B 219 N MSE B 220 1555 1555 1.33
LINK C MSE B 220 N VAL B 221 1555 1555 1.34
LINK C THR C 80 N MSE C 81 1555 1555 1.33
LINK C MSE C 81 N GLU C 82 1555 1555 1.33
LINK C SER C 107 N MSE C 108 1555 1555 1.32
LINK C MSE C 108 N GLY C 109 1555 1555 1.32
LINK C GLU C 219 N MSE C 220 1555 1555 1.33
LINK C MSE C 220 N VAL C 221 1555 1555 1.33
LINK C THR D 80 N MSE D 81 1555 1555 1.34
LINK C MSE D 81 N GLU D 82 1555 1555 1.33
LINK C ASER D 107 N MSE D 108 1555 1555 1.31
LINK C BSER D 107 N MSE D 108 1555 1555 1.31
LINK C MSE D 108 N GLY D 109 1555 1555 1.34
LINK C GLU D 219 N MSE D 220 1555 1555 1.33
LINK C MSE D 220 N VAL D 221 1555 1555 1.33
CISPEP 1 GLU C 24 PRO C 25 0 16.67
CISPEP 2 GLU D 24 PRO D 25 0 -3.83
CRYST1 74.813 79.399 87.438 90.00 90.12 90.00 P 1 21 1 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 0.013367 0.000000 0.000029 0.00000
SCALE2 0.000000 0.012595 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011437 0.00000
TER 1944 LEU A 261
TER 3947 LEU B 261
TER 6075 LEU C 261
TER 8180 LEU D 261
MASTER 372 0 12 65 24 0 0 6 8540 4 123 88
END |