| content |
HEADER HYDROLASE 11-FEB-04 1VA4
TITLE PSEUDOMONAS FLUORESCENS ARYL ESTERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ARYLESTERASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: ARYL-ESTER HYDROLASE;
COMPND 5 EC: 3.1.1.2;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS FLUORESCENS;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 STRAIN: SIK WI;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: DH5-ALPHA;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PUE1251
KEYWDS ALPHA/BETA HYDROLASE, ESTERASE, NON-COFACTOR DEPENDENT
KEYWDS 2 HALOPEROXIDASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.D.CHEESEMAN,A.TOCILJ,S.PARK,J.D.SCHRAG,R.J.KAZLAUSKAS
REVDAT 1 06-JUL-04 1VA4 0
JRNL AUTH J.D.CHEESEMAN,A.TOCILJ,S.PARK,J.D.SCHRAG,
JRNL AUTH 2 R.J.KAZLAUSKAS
JRNL TITL STRUCTURE OF AN ARYL ESTERASE FROM PSEUDOMONAS
JRNL TITL 2 FLUORESCENS
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 60 1237 2004
JRNL REFN ASTM ABCRE6 DK ISSN 0907-4449
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
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) : 48.53
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.2
REMARK 3 NUMBER OF REFLECTIONS : 271452
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) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.202
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 27113
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 : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 11847
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3170
REMARK 3 BIN FREE R VALUE SET COUNT : 1314
REMARK 3 BIN FREE R VALUE : 0.3430
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 14196
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.67
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) : -0.02000
REMARK 3 B12 (A**2) : 0.01000
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): 0.089
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.090
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.052
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.770
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.948
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 13126 ; 0.023 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 17764 ; 1.590 ; 1.950
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1620 ; 5.553 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1932 ; 0.132 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10044 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 6639 ; 0.214 ; 0.200
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): 1219 ; 0.127 ; 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): 27 ; 0.149 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 11 ; 0.125 ; 0.200
REMARK 3 SYMMETRY H-BOND 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): 8046 ; 0.852 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12888 ; 1.489 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5080 ; 2.729 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4876 ; 4.273 ; 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 : 0
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 0
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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: NULL
REMARK 4
REMARK 4 1VA4 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-FEB-2004.
REMARK 100 THE RCSB ID CODE IS RCSB006397.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-APR-2003
REMARK 200 TEMPERATURE (KELVIN) : 93.0
REMARK 200 PH : 7.50
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 : NULL
REMARK 200 OPTICS : OSMIC MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU HTC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTAL CLEAR
REMARK 200 DATA SCALING SOFTWARE : D*TREK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 271452
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 48.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.2
REMARK 200 DATA REDUNDANCY : 5.040
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06600
REMARK 200 FOR THE DATA SET : 14.0000
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) : 1.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 65.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.43
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.24700
REMARK 200 FOR SHELL : 3.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1A8S
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: 1% PEG 400, 1.65M (NH4)2SO4, 0.1M
REMARK 280 HEPES , PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,2/3+Z
REMARK 290 3555 -X+Y,-X,1/3+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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 86.58667
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 43.29333
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 6 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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 350 BIOMOLECULE: 2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMOLECULE: 3
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMOLECULE: 4
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMOLECULE: 5
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
REMARK 350 BIOMT1 5 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 5 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 5 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMOLECULE: 6
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F
REMARK 350 BIOMT1 6 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 6 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 6 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 272
REMARK 465 SER A 273
REMARK 465 HIS A 274
REMARK 465 HIS A 275
REMARK 465 HIS A 276
REMARK 465 HIS A 277
REMARK 465 HIS A 278
REMARK 465 HIS A 279
REMARK 465 GLY B 272
REMARK 465 SER B 273
REMARK 465 HIS B 274
REMARK 465 HIS B 275
REMARK 465 HIS B 276
REMARK 465 HIS B 277
REMARK 465 HIS B 278
REMARK 465 HIS B 279
REMARK 465 GLY C 272
REMARK 465 SER C 273
REMARK 465 HIS C 274
REMARK 465 HIS C 275
REMARK 465 HIS C 276
REMARK 465 HIS C 277
REMARK 465 HIS C 278
REMARK 465 HIS C 279
REMARK 465 GLY D 272
REMARK 465 SER D 273
REMARK 465 HIS D 274
REMARK 465 HIS D 275
REMARK 465 HIS D 276
REMARK 465 HIS D 277
REMARK 465 HIS D 278
REMARK 465 HIS D 279
REMARK 465 GLY E 272
REMARK 465 SER E 273
REMARK 465 HIS E 274
REMARK 465 HIS E 275
REMARK 465 HIS E 276
REMARK 465 HIS E 277
REMARK 465 HIS E 278
REMARK 465 HIS E 279
REMARK 465 GLY F 272
REMARK 465 SER F 273
REMARK 465 HIS F 274
REMARK 465 HIS F 275
REMARK 465 HIS F 276
REMARK 465 HIS F 277
REMARK 465 HIS F 278
REMARK 465 HIS F 279
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI
REMARK 500 CD2 LEU B 124 O HOH 1576 1.08
REMARK 500 O HOH 947 O HOH 1642 1.82
REMARK 500 CB THR B 122 O HOH 1553 1.87
REMARK 500 O HOH 1214 O HOH 1562 2.11
REMARK 500 CG LEU B 124 O HOH 1576 2.19
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 THR A 145 OG1 - CB - CG2 ANGL. DEV. = -9.9 DEGREES
REMARK 500 THR B 122 OG1 - CB - CG2 ANGL. DEV. = -9.6 DEGREES
REMARK 525
REMARK 525 SOLVENT
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH 1520 DISTANCE = 5.29 ANGSTROMS
REMARK 525 HOH 1575 DISTANCE = 5.85 ANGSTROMS
DBREF 1VA4 A 1 271 SWS P22862 ESTE_PSEFL 1 271
DBREF 1VA4 B 1 271 SWS P22862 ESTE_PSEFL 1 271
DBREF 1VA4 C 1 271 SWS P22862 ESTE_PSEFL 1 271
DBREF 1VA4 D 1 271 SWS P22862 ESTE_PSEFL 1 271
DBREF 1VA4 E 1 271 SWS P22862 ESTE_PSEFL 1 271
DBREF 1VA4 F 1 271 SWS P22862 ESTE_PSEFL 1 271
SEQADV 1VA4 GLY A 272 SWS P22862 HIS TAG
SEQADV 1VA4 SER A 273 SWS P22862 HIS TAG
SEQADV 1VA4 HIS A 274 SWS P22862 HIS TAG
SEQADV 1VA4 HIS A 275 SWS P22862 HIS TAG
SEQADV 1VA4 HIS A 276 SWS P22862 HIS TAG
SEQADV 1VA4 HIS A 277 SWS P22862 HIS TAG
SEQADV 1VA4 HIS A 278 SWS P22862 HIS TAG
SEQADV 1VA4 HIS A 279 SWS P22862 HIS TAG
SEQADV 1VA4 GLY B 272 SWS P22862 HIS TAG
SEQADV 1VA4 SER B 273 SWS P22862 HIS TAG
SEQADV 1VA4 HIS B 274 SWS P22862 HIS TAG
SEQADV 1VA4 HIS B 275 SWS P22862 HIS TAG
SEQADV 1VA4 HIS B 276 SWS P22862 HIS TAG
SEQADV 1VA4 HIS B 277 SWS P22862 HIS TAG
SEQADV 1VA4 HIS B 278 SWS P22862 HIS TAG
SEQADV 1VA4 HIS B 279 SWS P22862 HIS TAG
SEQADV 1VA4 GLY C 272 SWS P22862 HIS TAG
SEQADV 1VA4 SER C 273 SWS P22862 HIS TAG
SEQADV 1VA4 HIS C 274 SWS P22862 HIS TAG
SEQADV 1VA4 HIS C 275 SWS P22862 HIS TAG
SEQADV 1VA4 HIS C 276 SWS P22862 HIS TAG
SEQADV 1VA4 HIS C 277 SWS P22862 HIS TAG
SEQADV 1VA4 HIS C 278 SWS P22862 HIS TAG
SEQADV 1VA4 HIS C 279 SWS P22862 HIS TAG
SEQADV 1VA4 GLY D 272 SWS P22862 HIS TAG
SEQADV 1VA4 SER D 273 SWS P22862 HIS TAG
SEQADV 1VA4 HIS D 274 SWS P22862 HIS TAG
SEQADV 1VA4 HIS D 275 SWS P22862 HIS TAG
SEQADV 1VA4 HIS D 276 SWS P22862 HIS TAG
SEQADV 1VA4 HIS D 277 SWS P22862 HIS TAG
SEQADV 1VA4 HIS D 278 SWS P22862 HIS TAG
SEQADV 1VA4 HIS D 279 SWS P22862 HIS TAG
SEQADV 1VA4 GLY E 272 SWS P22862 HIS TAG
SEQADV 1VA4 SER E 273 SWS P22862 HIS TAG
SEQADV 1VA4 HIS E 274 SWS P22862 HIS TAG
SEQADV 1VA4 HIS E 275 SWS P22862 HIS TAG
SEQADV 1VA4 HIS E 276 SWS P22862 HIS TAG
SEQADV 1VA4 HIS E 277 SWS P22862 HIS TAG
SEQADV 1VA4 HIS E 278 SWS P22862 HIS TAG
SEQADV 1VA4 HIS E 279 SWS P22862 HIS TAG
SEQADV 1VA4 GLY F 272 SWS P22862 HIS TAG
SEQADV 1VA4 SER F 273 SWS P22862 HIS TAG
SEQADV 1VA4 HIS F 274 SWS P22862 HIS TAG
SEQADV 1VA4 HIS F 275 SWS P22862 HIS TAG
SEQADV 1VA4 HIS F 276 SWS P22862 HIS TAG
SEQADV 1VA4 HIS F 277 SWS P22862 HIS TAG
SEQADV 1VA4 HIS F 278 SWS P22862 HIS TAG
SEQADV 1VA4 HIS F 279 SWS P22862 HIS TAG
SEQRES 1 A 279 SER THR PHE VAL ALA LYS ASP GLY THR GLN ILE TYR PHE
SEQRES 2 A 279 LYS ASP TRP GLY SER GLY LYS PRO VAL LEU PHE SER HIS
SEQRES 3 A 279 GLY TRP LEU LEU ASP ALA ASP MET TRP GLU TYR GLN MET
SEQRES 4 A 279 GLU TYR LEU SER SER ARG GLY TYR ARG THR ILE ALA PHE
SEQRES 5 A 279 ASP ARG ARG GLY PHE GLY ARG SER ASP GLN PRO TRP THR
SEQRES 6 A 279 GLY ASN ASP TYR ASP THR PHE ALA ASP ASP ILE ALA GLN
SEQRES 7 A 279 LEU ILE GLU HIS LEU ASP LEU LYS GLU VAL THR LEU VAL
SEQRES 8 A 279 GLY PHE SER MET GLY GLY GLY ASP VAL ALA ARG TYR ILE
SEQRES 9 A 279 ALA ARG HIS GLY SER ALA ARG VAL ALA GLY LEU VAL LEU
SEQRES 10 A 279 LEU GLY ALA VAL THR PRO LEU PHE GLY GLN LYS PRO ASP
SEQRES 11 A 279 TYR PRO GLN GLY VAL PRO LEU ASP VAL PHE ALA ARG PHE
SEQRES 12 A 279 LYS THR GLU LEU LEU LYS ASP ARG ALA GLN PHE ILE SER
SEQRES 13 A 279 ASP PHE ASN ALA PRO PHE TYR GLY ILE ASN LYS GLY GLN
SEQRES 14 A 279 VAL VAL SER GLN GLY VAL GLN THR GLN THR LEU GLN ILE
SEQRES 15 A 279 ALA LEU LEU ALA SER LEU LYS ALA THR VAL ASP CYS VAL
SEQRES 16 A 279 THR ALA PHE ALA GLU THR ASP PHE ARG PRO ASP MET ALA
SEQRES 17 A 279 LYS ILE ASP VAL PRO THR LEU VAL ILE HIS GLY ASP GLY
SEQRES 18 A 279 ASP GLN ILE VAL PRO PHE GLU THR THR GLY LYS VAL ALA
SEQRES 19 A 279 ALA GLU LEU ILE LYS GLY ALA GLU LEU LYS VAL TYR LYS
SEQRES 20 A 279 ASP ALA PRO HIS GLY PHE ALA VAL THR HIS ALA GLN GLN
SEQRES 21 A 279 LEU ASN GLU ASP LEU LEU ALA PHE LEU LYS ARG GLY SER
SEQRES 22 A 279 HIS HIS HIS HIS HIS HIS
SEQRES 1 B 279 SER THR PHE VAL ALA LYS ASP GLY THR GLN ILE TYR PHE
SEQRES 2 B 279 LYS ASP TRP GLY SER GLY LYS PRO VAL LEU PHE SER HIS
SEQRES 3 B 279 GLY TRP LEU LEU ASP ALA ASP MET TRP GLU TYR GLN MET
SEQRES 4 B 279 GLU TYR LEU SER SER ARG GLY TYR ARG THR ILE ALA PHE
SEQRES 5 B 279 ASP ARG ARG GLY PHE GLY ARG SER ASP GLN PRO TRP THR
SEQRES 6 B 279 GLY ASN ASP TYR ASP THR PHE ALA ASP ASP ILE ALA GLN
SEQRES 7 B 279 LEU ILE GLU HIS LEU ASP LEU LYS GLU VAL THR LEU VAL
SEQRES 8 B 279 GLY PHE SER MET GLY GLY GLY ASP VAL ALA ARG TYR ILE
SEQRES 9 B 279 ALA ARG HIS GLY SER ALA ARG VAL ALA GLY LEU VAL LEU
SEQRES 10 B 279 LEU GLY ALA VAL THR PRO LEU PHE GLY GLN LYS PRO ASP
SEQRES 11 B 279 TYR PRO GLN GLY VAL PRO LEU ASP VAL PHE ALA ARG PHE
SEQRES 12 B 279 LYS THR GLU LEU LEU LYS ASP ARG ALA GLN PHE ILE SER
SEQRES 13 B 279 ASP PHE ASN ALA PRO PHE TYR GLY ILE ASN LYS GLY GLN
SEQRES 14 B 279 VAL VAL SER GLN GLY VAL GLN THR GLN THR LEU GLN ILE
SEQRES 15 B 279 ALA LEU LEU ALA SER LEU LYS ALA THR VAL ASP CYS VAL
SEQRES 16 B 279 THR ALA PHE ALA GLU THR ASP PHE ARG PRO ASP MET ALA
SEQRES 17 B 279 LYS ILE ASP VAL PRO THR LEU VAL ILE HIS GLY ASP GLY
SEQRES 18 B 279 ASP GLN ILE VAL PRO PHE GLU THR THR GLY LYS VAL ALA
SEQRES 19 B 279 ALA GLU LEU ILE LYS GLY ALA GLU LEU LYS VAL TYR LYS
SEQRES 20 B 279 ASP ALA PRO HIS GLY PHE ALA VAL THR HIS ALA GLN GLN
SEQRES 21 B 279 LEU ASN GLU ASP LEU LEU ALA PHE LEU LYS ARG GLY SER
SEQRES 22 B 279 HIS HIS HIS HIS HIS HIS
SEQRES 1 C 279 SER THR PHE VAL ALA LYS ASP GLY THR GLN ILE TYR PHE
SEQRES 2 C 279 LYS ASP TRP GLY SER GLY LYS PRO VAL LEU PHE SER HIS
SEQRES 3 C 279 GLY TRP LEU LEU ASP ALA ASP MET TRP GLU TYR GLN MET
SEQRES 4 C 279 GLU TYR LEU SER SER ARG GLY TYR ARG THR ILE ALA PHE
SEQRES 5 C 279 ASP ARG ARG GLY PHE GLY ARG SER ASP GLN PRO TRP THR
SEQRES 6 C 279 GLY ASN ASP TYR ASP THR PHE ALA ASP ASP ILE ALA GLN
SEQRES 7 C 279 LEU ILE GLU HIS LEU ASP LEU LYS GLU VAL THR LEU VAL
SEQRES 8 C 279 GLY PHE SER MET GLY GLY GLY ASP VAL ALA ARG TYR ILE
SEQRES 9 C 279 ALA ARG HIS GLY SER ALA ARG VAL ALA GLY LEU VAL LEU
SEQRES 10 C 279 LEU GLY ALA VAL THR PRO LEU PHE GLY GLN LYS PRO ASP
SEQRES 11 C 279 TYR PRO GLN GLY VAL PRO LEU ASP VAL PHE ALA ARG PHE
SEQRES 12 C 279 LYS THR GLU LEU LEU LYS ASP ARG ALA GLN PHE ILE SER
SEQRES 13 C 279 ASP PHE ASN ALA PRO PHE TYR GLY ILE ASN LYS GLY GLN
SEQRES 14 C 279 VAL VAL SER GLN GLY VAL GLN THR GLN THR LEU GLN ILE
SEQRES 15 C 279 ALA LEU LEU ALA SER LEU LYS ALA THR VAL ASP CYS VAL
SEQRES 16 C 279 THR ALA PHE ALA GLU THR ASP PHE ARG PRO ASP MET ALA
SEQRES 17 C 279 LYS ILE ASP VAL PRO THR LEU VAL ILE HIS GLY ASP GLY
SEQRES 18 C 279 ASP GLN ILE VAL PRO PHE GLU THR THR GLY LYS VAL ALA
SEQRES 19 C 279 ALA GLU LEU ILE LYS GLY ALA GLU LEU LYS VAL TYR LYS
SEQRES 20 C 279 ASP ALA PRO HIS GLY PHE ALA VAL THR HIS ALA GLN GLN
SEQRES 21 C 279 LEU ASN GLU ASP LEU LEU ALA PHE LEU LYS ARG GLY SER
SEQRES 22 C 279 HIS HIS HIS HIS HIS HIS
SEQRES 1 D 279 SER THR PHE VAL ALA LYS ASP GLY THR GLN ILE TYR PHE
SEQRES 2 D 279 LYS ASP TRP GLY SER GLY LYS PRO VAL LEU PHE SER HIS
SEQRES 3 D 279 GLY TRP LEU LEU ASP ALA ASP MET TRP GLU TYR GLN MET
SEQRES 4 D 279 GLU TYR LEU SER SER ARG GLY TYR ARG THR ILE ALA PHE
SEQRES 5 D 279 ASP ARG ARG GLY PHE GLY ARG SER ASP GLN PRO TRP THR
SEQRES 6 D 279 GLY ASN ASP TYR ASP THR PHE ALA ASP ASP ILE ALA GLN
SEQRES 7 D 279 LEU ILE GLU HIS LEU ASP LEU LYS GLU VAL THR LEU VAL
SEQRES 8 D 279 GLY PHE SER MET GLY GLY GLY ASP VAL ALA ARG TYR ILE
SEQRES 9 D 279 ALA ARG HIS GLY SER ALA ARG VAL ALA GLY LEU VAL LEU
SEQRES 10 D 279 LEU GLY ALA VAL THR PRO LEU PHE GLY GLN LYS PRO ASP
SEQRES 11 D 279 TYR PRO GLN GLY VAL PRO LEU ASP VAL PHE ALA ARG PHE
SEQRES 12 D 279 LYS THR GLU LEU LEU LYS ASP ARG ALA GLN PHE ILE SER
SEQRES 13 D 279 ASP PHE ASN ALA PRO PHE TYR GLY ILE ASN LYS GLY GLN
SEQRES 14 D 279 VAL VAL SER GLN GLY VAL GLN THR GLN THR LEU GLN ILE
SEQRES 15 D 279 ALA LEU LEU ALA SER LEU LYS ALA THR VAL ASP CYS VAL
SEQRES 16 D 279 THR ALA PHE ALA GLU THR ASP PHE ARG PRO ASP MET ALA
SEQRES 17 D 279 LYS ILE ASP VAL PRO THR LEU VAL ILE HIS GLY ASP GLY
SEQRES 18 D 279 ASP GLN ILE VAL PRO PHE GLU THR THR GLY LYS VAL ALA
SEQRES 19 D 279 ALA GLU LEU ILE LYS GLY ALA GLU LEU LYS VAL TYR LYS
SEQRES 20 D 279 ASP ALA PRO HIS GLY PHE ALA VAL THR HIS ALA GLN GLN
SEQRES 21 D 279 LEU ASN GLU ASP LEU LEU ALA PHE LEU LYS ARG GLY SER
SEQRES 22 D 279 HIS HIS HIS HIS HIS HIS
SEQRES 1 E 279 SER THR PHE VAL ALA LYS ASP GLY THR GLN ILE TYR PHE
SEQRES 2 E 279 LYS ASP TRP GLY SER GLY LYS PRO VAL LEU PHE SER HIS
SEQRES 3 E 279 GLY TRP LEU LEU ASP ALA ASP MET TRP GLU TYR GLN MET
SEQRES 4 E 279 GLU TYR LEU SER SER ARG GLY TYR ARG THR ILE ALA PHE
SEQRES 5 E 279 ASP ARG ARG GLY PHE GLY ARG SER ASP GLN PRO TRP THR
SEQRES 6 E 279 GLY ASN ASP TYR ASP THR PHE ALA ASP ASP ILE ALA GLN
SEQRES 7 E 279 LEU ILE GLU HIS LEU ASP LEU LYS GLU VAL THR LEU VAL
SEQRES 8 E 279 GLY PHE SER MET GLY GLY GLY ASP VAL ALA ARG TYR ILE
SEQRES 9 E 279 ALA ARG HIS GLY SER ALA ARG VAL ALA GLY LEU VAL LEU
SEQRES 10 E 279 LEU GLY ALA VAL THR PRO LEU PHE GLY GLN LYS PRO ASP
SEQRES 11 E 279 TYR PRO GLN GLY VAL PRO LEU ASP VAL PHE ALA ARG PHE
SEQRES 12 E 279 LYS THR GLU LEU LEU LYS ASP ARG ALA GLN PHE ILE SER
SEQRES 13 E 279 ASP PHE ASN ALA PRO PHE TYR GLY ILE ASN LYS GLY GLN
SEQRES 14 E 279 VAL VAL SER GLN GLY VAL GLN THR GLN THR LEU GLN ILE
SEQRES 15 E 279 ALA LEU LEU ALA SER LEU LYS ALA THR VAL ASP CYS VAL
SEQRES 16 E 279 THR ALA PHE ALA GLU THR ASP PHE ARG PRO ASP MET ALA
SEQRES 17 E 279 LYS ILE ASP VAL PRO THR LEU VAL ILE HIS GLY ASP GLY
SEQRES 18 E 279 ASP GLN ILE VAL PRO PHE GLU THR THR GLY LYS VAL ALA
SEQRES 19 E 279 ALA GLU LEU ILE LYS GLY ALA GLU LEU LYS VAL TYR LYS
SEQRES 20 E 279 ASP ALA PRO HIS GLY PHE ALA VAL THR HIS ALA GLN GLN
SEQRES 21 E 279 LEU ASN GLU ASP LEU LEU ALA PHE LEU LYS ARG GLY SER
SEQRES 22 E 279 HIS HIS HIS HIS HIS HIS
SEQRES 1 F 279 SER THR PHE VAL ALA LYS ASP GLY THR GLN ILE TYR PHE
SEQRES 2 F 279 LYS ASP TRP GLY SER GLY LYS PRO VAL LEU PHE SER HIS
SEQRES 3 F 279 GLY TRP LEU LEU ASP ALA ASP MET TRP GLU TYR GLN MET
SEQRES 4 F 279 GLU TYR LEU SER SER ARG GLY TYR ARG THR ILE ALA PHE
SEQRES 5 F 279 ASP ARG ARG GLY PHE GLY ARG SER ASP GLN PRO TRP THR
SEQRES 6 F 279 GLY ASN ASP TYR ASP THR PHE ALA ASP ASP ILE ALA GLN
SEQRES 7 F 279 LEU ILE GLU HIS LEU ASP LEU LYS GLU VAL THR LEU VAL
SEQRES 8 F 279 GLY PHE SER MET GLY GLY GLY ASP VAL ALA ARG TYR ILE
SEQRES 9 F 279 ALA ARG HIS GLY SER ALA ARG VAL ALA GLY LEU VAL LEU
SEQRES 10 F 279 LEU GLY ALA VAL THR PRO LEU PHE GLY GLN LYS PRO ASP
SEQRES 11 F 279 TYR PRO GLN GLY VAL PRO LEU ASP VAL PHE ALA ARG PHE
SEQRES 12 F 279 LYS THR GLU LEU LEU LYS ASP ARG ALA GLN PHE ILE SER
SEQRES 13 F 279 ASP PHE ASN ALA PRO PHE TYR GLY ILE ASN LYS GLY GLN
SEQRES 14 F 279 VAL VAL SER GLN GLY VAL GLN THR GLN THR LEU GLN ILE
SEQRES 15 F 279 ALA LEU LEU ALA SER LEU LYS ALA THR VAL ASP CYS VAL
SEQRES 16 F 279 THR ALA PHE ALA GLU THR ASP PHE ARG PRO ASP MET ALA
SEQRES 17 F 279 LYS ILE ASP VAL PRO THR LEU VAL ILE HIS GLY ASP GLY
SEQRES 18 F 279 ASP GLN ILE VAL PRO PHE GLU THR THR GLY LYS VAL ALA
SEQRES 19 F 279 ALA GLU LEU ILE LYS GLY ALA GLU LEU LYS VAL TYR LYS
SEQRES 20 F 279 ASP ALA PRO HIS GLY PHE ALA VAL THR HIS ALA GLN GLN
SEQRES 21 F 279 LEU ASN GLU ASP LEU LEU ALA PHE LEU LYS ARG GLY SER
SEQRES 22 F 279 HIS HIS HIS HIS HIS HIS
HET GOL 1 6
HET GOL 2 6
HET GOL 3 6
HET GOL 4 6
HET GOL 5 6
HET GOL 6 6
HET GOL 7 6
HET GOL 8 6
HET GOL 9 6
HET GOL 10 6
HET GOL 11 6
HET GOL 12 6
HET GOL 13 6
HET GOL 14 6
HET GOL 15 6
HET GOL 16 6
HET GOL 17 6
HET GOL 18 6
HET GOL 19 6
HET GOL 20 6
HETNAM GOL GLYCEROL
FORMUL 7 GOL 20(C3 H8 O3)
FORMUL 27 HOH *1362(H2 O1)
HELIX 1 1 ASP A 31 MET A 34 5 4
HELIX 2 2 TRP A 35 SER A 44 1 10
HELIX 3 3 ASP A 68 ASP A 84 1 17
HELIX 4 4 MET A 95 GLY A 108 1 14
HELIX 5 5 PRO A 136 GLY A 164 1 29
HELIX 6 6 ILE A 165 GLY A 168 5 4
HELIX 7 7 SER A 172 ALA A 186 1 15
HELIX 8 8 SER A 187 THR A 201 1 15
HELIX 9 9 PHE A 203 ILE A 210 1 8
HELIX 10 10 PRO A 226 THR A 229 5 4
HELIX 11 11 THR A 230 ILE A 238 1 9
HELIX 12 12 GLY A 252 HIS A 257 1 6
HELIX 13 13 HIS A 257 LYS A 270 1 14
HELIX 14 14 ASP B 31 MET B 34 5 4
HELIX 15 15 TRP B 35 SER B 44 1 10
HELIX 16 16 ASP B 68 ASP B 84 1 17
HELIX 17 17 MET B 95 GLY B 108 1 14
HELIX 18 18 PRO B 136 GLY B 164 1 29
HELIX 19 19 SER B 172 ALA B 186 1 15
HELIX 20 20 SER B 187 THR B 201 1 15
HELIX 21 21 PHE B 203 ILE B 210 1 8
HELIX 22 22 PRO B 226 THR B 229 5 4
HELIX 23 23 THR B 230 ILE B 238 1 9
HELIX 24 24 GLY B 252 HIS B 257 1 6
HELIX 25 25 HIS B 257 ARG B 271 1 15
HELIX 26 26 ASP C 31 MET C 34 5 4
HELIX 27 27 TRP C 35 SER C 44 1 10
HELIX 28 28 ASP C 68 ASP C 84 1 17
HELIX 29 29 MET C 95 GLY C 108 1 14
HELIX 30 30 PRO C 136 GLY C 164 1 29
HELIX 31 31 ILE C 165 GLY C 168 5 4
HELIX 32 32 SER C 172 ALA C 186 1 15
HELIX 33 33 SER C 187 THR C 201 1 15
HELIX 34 34 PHE C 203 ILE C 210 1 8
HELIX 35 35 PRO C 226 THR C 229 5 4
HELIX 36 36 THR C 230 ILE C 238 1 9
HELIX 37 37 GLY C 252 HIS C 257 1 6
HELIX 38 38 HIS C 257 LYS C 270 1 14
HELIX 39 39 ASP D 31 MET D 34 5 4
HELIX 40 40 TRP D 35 SER D 44 1 10
HELIX 41 41 ASP D 68 LEU D 83 1 16
HELIX 42 42 MET D 95 GLY D 108 1 14
HELIX 43 43 PRO D 136 GLY D 164 1 29
HELIX 44 44 ILE D 165 GLY D 168 5 4
HELIX 45 45 SER D 172 ALA D 186 1 15
HELIX 46 46 SER D 187 THR D 201 1 15
HELIX 47 47 PHE D 203 ILE D 210 1 8
HELIX 48 48 PRO D 226 THR D 229 5 4
HELIX 49 49 THR D 230 ILE D 238 1 9
HELIX 50 50 GLY D 252 HIS D 257 1 6
HELIX 51 51 HIS D 257 ARG D 271 1 15
HELIX 52 52 ASP E 31 MET E 34 5 4
HELIX 53 53 TRP E 35 SER E 44 1 10
HELIX 54 54 ASP E 68 ASP E 84 1 17
HELIX 55 55 MET E 95 GLY E 108 1 14
HELIX 56 56 PRO E 136 GLY E 164 1 29
HELIX 57 57 ILE E 165 GLY E 168 5 4
HELIX 58 58 SER E 172 ALA E 186 1 15
HELIX 59 59 SER E 187 THR E 201 1 15
HELIX 60 60 PHE E 203 ILE E 210 1 8
HELIX 61 61 PRO E 226 THR E 229 5 4
HELIX 62 62 THR E 230 ILE E 238 1 9
HELIX 63 63 GLY E 252 HIS E 257 1 6
HELIX 64 64 HIS E 257 LYS E 270 1 14
HELIX 65 65 ASP F 31 MET F 34 5 4
HELIX 66 66 TRP F 35 SER F 44 1 10
HELIX 67 67 ASP F 68 ASP F 84 1 17
HELIX 68 68 MET F 95 GLY F 108 1 14
HELIX 69 69 PRO F 136 GLY F 164 1 29
HELIX 70 70 ILE F 165 GLY F 168 5 4
HELIX 71 71 SER F 172 ALA F 186 1 15
HELIX 72 72 SER F 187 THR F 201 1 15
HELIX 73 73 PHE F 203 ILE F 210 1 8
HELIX 74 74 PRO F 226 THR F 229 5 4
HELIX 75 75 THR F 230 ILE F 238 1 9
HELIX 76 76 GLY F 252 HIS F 257 1 6
HELIX 77 77 HIS F 257 LYS F 270 1 14
SHEET 1 A 8 THR A 2 VAL A 4 0
SHEET 2 A 8 GLN A 10 TRP A 16 -1 O ILE A 11 N PHE A 3
SHEET 3 A 8 ARG A 48 PHE A 52 -1 O THR A 49 N TRP A 16
SHEET 4 A 8 PRO A 21 SER A 25 1 N VAL A 22 O ILE A 50
SHEET 5 A 8 VAL A 88 PHE A 93 1 O VAL A 91 N SER A 25
SHEET 6 A 8 VAL A 112 LEU A 118 1 O LEU A 118 N GLY A 92
SHEET 7 A 8 THR A 214 GLY A 219 1 O ILE A 217 N LEU A 117
SHEET 8 A 8 GLU A 242 TYR A 246 1 O GLU A 242 N VAL A 216
SHEET 1 B 8 THR B 2 VAL B 4 0
SHEET 2 B 8 GLN B 10 TRP B 16 -1 O ILE B 11 N PHE B 3
SHEET 3 B 8 ARG B 48 PHE B 52 -1 O THR B 49 N TRP B 16
SHEET 4 B 8 PRO B 21 SER B 25 1 N PHE B 24 O ILE B 50
SHEET 5 B 8 VAL B 88 PHE B 93 1 O VAL B 91 N LEU B 23
SHEET 6 B 8 VAL B 112 LEU B 118 1 O LEU B 118 N GLY B 92
SHEET 7 B 8 THR B 214 GLY B 219 1 O ILE B 217 N LEU B 117
SHEET 8 B 8 GLU B 242 TYR B 246 1 O GLU B 242 N VAL B 216
SHEET 1 C 8 THR C 2 VAL C 4 0
SHEET 2 C 8 GLN C 10 TRP C 16 -1 O ILE C 11 N PHE C 3
SHEET 3 C 8 ARG C 48 PHE C 52 -1 O THR C 49 N TRP C 16
SHEET 4 C 8 PRO C 21 SER C 25 1 N PHE C 24 O ILE C 50
SHEET 5 C 8 VAL C 88 PHE C 93 1 O VAL C 91 N SER C 25
SHEET 6 C 8 VAL C 112 LEU C 118 1 O LEU C 118 N GLY C 92
SHEET 7 C 8 THR C 214 GLY C 219 1 O ILE C 217 N LEU C 117
SHEET 8 C 8 GLU C 242 TYR C 246 1 O GLU C 242 N VAL C 216
SHEET 1 D 8 THR D 2 VAL D 4 0
SHEET 2 D 8 GLN D 10 TRP D 16 -1 O ILE D 11 N PHE D 3
SHEET 3 D 8 TYR D 47 PHE D 52 -1 O THR D 49 N TRP D 16
SHEET 4 D 8 LYS D 20 SER D 25 1 N PHE D 24 O ILE D 50
SHEET 5 D 8 VAL D 88 PHE D 93 1 O VAL D 91 N SER D 25
SHEET 6 D 8 VAL D 112 LEU D 118 1 O LEU D 118 N GLY D 92
SHEET 7 D 8 THR D 214 GLY D 219 1 O LEU D 215 N LEU D 117
SHEET 8 D 8 GLU D 242 TYR D 246 1 O GLU D 242 N VAL D 216
SHEET 1 E 8 THR E 2 VAL E 4 0
SHEET 2 E 8 GLN E 10 TRP E 16 -1 O ILE E 11 N PHE E 3
SHEET 3 E 8 TYR E 47 PHE E 52 -1 O THR E 49 N TRP E 16
SHEET 4 E 8 LYS E 20 SER E 25 1 N PHE E 24 O ILE E 50
SHEET 5 E 8 VAL E 88 PHE E 93 1 O VAL E 91 N SER E 25
SHEET 6 E 8 VAL E 112 LEU E 118 1 O LEU E 118 N GLY E 92
SHEET 7 E 8 THR E 214 GLY E 219 1 O LEU E 215 N LEU E 117
SHEET 8 E 8 GLU E 242 TYR E 246 1 O GLU E 242 N VAL E 216
SHEET 1 F 8 THR F 2 VAL F 4 0
SHEET 2 F 8 GLN F 10 TRP F 16 -1 O ILE F 11 N PHE F 3
SHEET 3 F 8 ARG F 48 PHE F 52 -1 O THR F 49 N TRP F 16
SHEET 4 F 8 PRO F 21 SER F 25 1 N VAL F 22 O ILE F 50
SHEET 5 F 8 VAL F 88 PHE F 93 1 O VAL F 91 N SER F 25
SHEET 6 F 8 VAL F 112 LEU F 118 1 O LEU F 118 N GLY F 92
SHEET 7 F 8 THR F 214 GLY F 219 1 O LEU F 215 N LEU F 117
SHEET 8 F 8 GLU F 242 TYR F 246 1 O GLU F 242 N VAL F 216
CISPEP 1 THR A 122 PRO A 123 0 0.39
CISPEP 2 THR B 122 PRO B 123 0 2.00
CISPEP 3 THR C 122 PRO C 123 0 -3.56
CISPEP 4 THR D 122 PRO D 123 0 2.34
CISPEP 5 THR E 122 PRO E 123 0 -0.04
CISPEP 6 THR F 122 PRO F 123 0 -1.76
CRYST1 146.040 146.040 129.880 90.00 90.00 120.00 P 32 18
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 0.006847 0.003953 0.000000 0.00000
SCALE2 0.000000 0.007907 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007699 0.00000
TER 2120 ARG A 271
TER 4240 ARG B 271
TER 6360 ARG C 271
TER 8480 ARG D 271
TER 10600 ARG E 271
TER 12720 ARG F 271
MASTER 337 0 20 77 48 0 0 614196 6 120 132
END |