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HEADER HYDROLASE 11-MAY-26 26QV
TITLE CRYSTAL STRUCTURE OF MONOALKYL PHTHALATE HYDROLASE FROM RHODOCOCCUS
TITLE 2 SP. EG-5
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MONO-ETHYLHEXYLPHTHALATE HYDROLASE;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOCOCCUS SP. EG-5;
SOURCE 3 ORGANISM_TAXID: 1747801;
SOURCE 4 GENE: MEHPH;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS MONO-BUTYL PHTHALATE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.AGGARWAL,K.JANGID,S.SINGH,A.K.SHARMA,P.KUMAR
REVDAT 1 10-JUN-26 26QV 0
JRNL AUTH S.AGGARWAL,K.JANGID,S.SINGH,A.K.SHARMA,P.KUMAR
JRNL TITL CRYSTAL STRUCTURE OF MONOALKYL PHTHALATE HYDROLASE FROM
JRNL TITL 2 RHODOCOCCUS SP. EG-5
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0425
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.38
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 83568
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NONE
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.251
REMARK 3 FREE R VALUE : 0.294
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.035
REMARK 3 FREE R VALUE TEST SET COUNT : 4208
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.08
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5811
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.72
REMARK 3 BIN R VALUE (WORKING SET) : 0.2610
REMARK 3 BIN FREE R VALUE SET COUNT : 316
REMARK 3 BIN FREE R VALUE : 0.3290
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 21922
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 254
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.39
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.73400
REMARK 3 B22 (A**2) : 6.46700
REMARK 3 B33 (A**2) : -9.20100
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.101
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.314
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.296
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.811
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.750
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 22410 ; 0.007 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): 21258 ; 0.001 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 30445 ; 1.438 ; 1.811
REMARK 3 BOND ANGLES OTHERS (DEGREES): 48878 ; 0.476 ; 1.747
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2848 ; 6.556 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 150 ;10.800 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3556 ;14.598 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3419 ; 0.058 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 26595 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 5061 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4548 ; 0.224 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 435 ; 0.224 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 10881 ; 0.180 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 442 ; 0.184 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): 2 ; 0.281 ; 0.200
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): 11452 ; 1.546 ; 1.717
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 11452 ; 1.546 ; 1.717
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 14280 ; 2.501 ; 3.082
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 14281 ; 2.501 ; 3.082
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 10958 ; 1.479 ; 1.812
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 10959 ; 1.479 ; 1.812
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 16165 ; 2.431 ; 3.300
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 16166 ; 2.431 ; 3.300
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 BULK SOLVENT
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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 THEIR
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 26QV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-MAY-26.
REMARK 100 THE DEPOSITION ID IS D_1300074154.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-MAY-23
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
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 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54184
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : RIGAKU HYPIX-6000HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSALISPRO
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 83596
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 27.380
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 11.23
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.2300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.11
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM MALONATE PH 7.0, 0.01M
REMARK 280 BARIUM CHLORIDE DI HYDRATE, 20% PEG 3350, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 2
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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z
REMARK 290 7555 -X+1/2,Y+1/2,-Z
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 88.80600
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 122.74600
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 88.80600
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 122.74600
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 88.80600
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 122.74600
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 88.80600
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 122.74600
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5
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 APPLY THE FOLLOWING TO CHAINS: A, B
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 APPLY THE FOLLOWING TO CHAINS: C, 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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, H
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, G
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: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J
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 ASN A 2
REMARK 465 ASP A 140
REMARK 465 ALA A 141
REMARK 465 LYS A 142
REMARK 465 PHE A 143
REMARK 465 ARG A 144
REMARK 465 ASP A 145
REMARK 465 VAL A 146
REMARK 465 SER A 298
REMARK 465 TYR A 299
REMARK 465 ALA A 300
REMARK 465 THR A 301
REMARK 465 ARG A 302
REMARK 465 ARG A 303
REMARK 465 MET B 1
REMARK 465 ASN B 2
REMARK 465 THR B 3
REMARK 465 ASP B 140
REMARK 465 ALA B 141
REMARK 465 LYS B 142
REMARK 465 PHE B 143
REMARK 465 ARG B 144
REMARK 465 ASP B 145
REMARK 465 VAL B 146
REMARK 465 TYR B 299
REMARK 465 ALA B 300
REMARK 465 THR B 301
REMARK 465 ARG B 302
REMARK 465 ARG B 303
REMARK 465 ASP C 140
REMARK 465 ALA C 141
REMARK 465 LYS C 142
REMARK 465 PHE C 143
REMARK 465 ARG C 144
REMARK 465 ASP C 145
REMARK 465 VAL C 146
REMARK 465 GLU C 147
REMARK 465 PHE C 148
REMARK 465 TYR C 149
REMARK 465 ASP C 150
REMARK 465 ALA C 151
REMARK 465 TYR C 299
REMARK 465 ALA C 300
REMARK 465 THR C 301
REMARK 465 ARG C 302
REMARK 465 ARG C 303
REMARK 465 MET D 1
REMARK 465 ASN D 2
REMARK 465 THR D 3
REMARK 465 THR D 139
REMARK 465 ASP D 140
REMARK 465 ALA D 141
REMARK 465 LYS D 142
REMARK 465 PHE D 143
REMARK 465 ARG D 144
REMARK 465 ASP D 145
REMARK 465 VAL D 146
REMARK 465 GLU D 147
REMARK 465 SER D 298
REMARK 465 TYR D 299
REMARK 465 ALA D 300
REMARK 465 THR D 301
REMARK 465 ARG D 302
REMARK 465 ARG D 303
REMARK 465 MET E 1
REMARK 465 ASN E 2
REMARK 465 ASP E 140
REMARK 465 ALA E 141
REMARK 465 LYS E 142
REMARK 465 PHE E 143
REMARK 465 ARG E 144
REMARK 465 ASP E 145
REMARK 465 VAL E 146
REMARK 465 GLU E 147
REMARK 465 TYR E 299
REMARK 465 ALA E 300
REMARK 465 THR E 301
REMARK 465 ARG E 302
REMARK 465 ARG E 303
REMARK 465 MET F 1
REMARK 465 ASN F 2
REMARK 465 THR F 3
REMARK 465 ASP F 4
REMARK 465 THR F 139
REMARK 465 ASP F 140
REMARK 465 ALA F 141
REMARK 465 LYS F 142
REMARK 465 PHE F 143
REMARK 465 ARG F 144
REMARK 465 ASP F 145
REMARK 465 VAL F 146
REMARK 465 GLU F 147
REMARK 465 TYR F 299
REMARK 465 ALA F 300
REMARK 465 THR F 301
REMARK 465 ARG F 302
REMARK 465 ARG F 303
REMARK 465 MET G 1
REMARK 465 ASN G 2
REMARK 465 ASP G 140
REMARK 465 ALA G 141
REMARK 465 LYS G 142
REMARK 465 PHE G 143
REMARK 465 ARG G 144
REMARK 465 ASP G 145
REMARK 465 VAL G 146
REMARK 465 GLU G 147
REMARK 465 TYR G 299
REMARK 465 ALA G 300
REMARK 465 THR G 301
REMARK 465 ARG G 302
REMARK 465 ARG G 303
REMARK 465 MET H 1
REMARK 465 ASN H 2
REMARK 465 THR H 3
REMARK 465 THR H 139
REMARK 465 ASP H 140
REMARK 465 ALA H 141
REMARK 465 LYS H 142
REMARK 465 PHE H 143
REMARK 465 ARG H 144
REMARK 465 ASP H 145
REMARK 465 VAL H 146
REMARK 465 GLU H 147
REMARK 465 TYR H 299
REMARK 465 ALA H 300
REMARK 465 THR H 301
REMARK 465 ARG H 302
REMARK 465 ARG H 303
REMARK 465 MET I 1
REMARK 465 ASN I 2
REMARK 465 THR I 3
REMARK 465 ASP I 4
REMARK 465 THR I 139
REMARK 465 ASP I 140
REMARK 465 ALA I 141
REMARK 465 LYS I 142
REMARK 465 PHE I 143
REMARK 465 ARG I 144
REMARK 465 ASP I 145
REMARK 465 VAL I 146
REMARK 465 ALA I 297
REMARK 465 SER I 298
REMARK 465 TYR I 299
REMARK 465 ALA I 300
REMARK 465 THR I 301
REMARK 465 ARG I 302
REMARK 465 ARG I 303
REMARK 465 MET J 1
REMARK 465 ASN J 2
REMARK 465 ALA J 141
REMARK 465 LYS J 142
REMARK 465 PHE J 143
REMARK 465 ARG J 144
REMARK 465 ASP J 145
REMARK 465 VAL J 146
REMARK 465 TYR J 299
REMARK 465 ALA J 300
REMARK 465 THR J 301
REMARK 465 ARG J 302
REMARK 465 ARG J 303
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 DISTANCE
REMARK 500 HG SER C 6 O ASP C 21 1.23
REMARK 500 HE1 HIS A 32 H LYS A 66 1.31
REMARK 500 O MET D 204 HE3 LYS D 208 1.55
REMARK 500 HH11 ARG G 91 OD2 ASP G 120 1.59
REMARK 500 HH21 ARG B 154 OD2 ASP E 84 1.60
REMARK 500 HD22 ASN J 197 O HOH J 402 1.60
REMARK 500 OE2 GLU B 193 HZ3 LYS C 88 1.60
REMARK 500 O LYS E 126 NH1 ARG E 295 2.03
REMARK 500 NH1 ARG J 91 OD2 ASP J 120 2.14
REMARK 500 OG SER F 6 O ASP F 21 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 HH12 ARG F 243 OE1 GLU J 229 4554 1.34
REMARK 500 NH1 ARG F 243 OE1 GLU J 229 4554 2.07
REMARK 500
REMARK 500 REMARK: NULL
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 PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 18 CG - CD - NE ANGL. DEV. = 13.2 DEGREES
REMARK 500 ARG A 295 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG B 295 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ASP D 4 CB - CA - C ANGL. DEV. = 14.1 DEGREES
REMARK 500 ARG D 295 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG F 18 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES
REMARK 500 MET F 204 CG - SD - CE ANGL. DEV. = 11.6 DEGREES
REMARK 500 LEU I 173 CB - CG - CD1 ANGL. DEV. = 15.0 DEGREES
REMARK 500 MET J 40 CG - SD - CE ANGL. DEV. = 12.3 DEGREES
REMARK 500 ARG J 280 CG - CD - NE ANGL. DEV. = -13.2 DEGREES
REMARK 500 ARG J 294 CG - CD - NE ANGL. DEV. = -14.2 DEGREES
REMARK 500 ARG J 295 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 LEU A 5 -74.83 -64.01
REMARK 500 SER A 6 50.38 -103.12
REMARK 500 SER A 108 -129.92 57.39
REMARK 500 PRO A 157 173.47 -53.25
REMARK 500 TYR A 209 -53.40 -122.77
REMARK 500 ASN A 231 48.06 -104.46
REMARK 500 SER B 108 -129.37 55.86
REMARK 500 SER C 6 112.69 -174.67
REMARK 500 SER C 108 -127.90 56.27
REMARK 500 ALA C 297 41.34 -106.69
REMARK 500 LEU D 5 -84.79 -112.88
REMARK 500 SER D 108 -130.65 53.11
REMARK 500 LEU E 5 -85.18 -60.76
REMARK 500 SER E 6 55.21 -94.79
REMARK 500 SER E 108 -129.41 53.90
REMARK 500 ASN E 231 43.86 -105.43
REMARK 500 SER F 108 -131.05 54.10
REMARK 500 ALA F 134 -25.05 59.36
REMARK 500 SER G 108 -128.25 53.48
REMARK 500 ASN G 231 41.44 -106.20
REMARK 500 SER H 6 49.97 -92.96
REMARK 500 SER H 108 -130.00 53.72
REMARK 500 ALA H 158 -7.34 100.06
REMARK 500 ASN H 231 43.91 -104.27
REMARK 500 ARG H 280 53.17 -142.33
REMARK 500 ALA H 297 43.35 -92.19
REMARK 500 SER I 108 -127.35 53.42
REMARK 500 ALA I 158 -11.92 100.68
REMARK 500 ASN I 231 46.22 -105.14
REMARK 500 LEU J 5 -59.14 -154.62
REMARK 500 SER J 108 -124.92 57.62
REMARK 500 TYR J 209 -51.56 -120.76
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 18 0.14 SIDE CHAIN
REMARK 500 ARG A 243 0.08 SIDE CHAIN
REMARK 500 ARG A 294 0.10 SIDE CHAIN
REMARK 500 ARG B 18 0.12 SIDE CHAIN
REMARK 500 ARG C 243 0.07 SIDE CHAIN
REMARK 500 ARG C 295 0.16 SIDE CHAIN
REMARK 500 ARG D 18 0.10 SIDE CHAIN
REMARK 500 ARG D 243 0.10 SIDE CHAIN
REMARK 500 ARG D 286 0.07 SIDE CHAIN
REMARK 500 ARG D 295 0.09 SIDE CHAIN
REMARK 500 ARG E 18 0.09 SIDE CHAIN
REMARK 500 ARG E 286 0.14 SIDE CHAIN
REMARK 500 ARG E 295 0.10 SIDE CHAIN
REMARK 500 ARG F 18 0.19 SIDE CHAIN
REMARK 500 ARG G 109 0.09 SIDE CHAIN
REMARK 500 ARG G 154 0.10 SIDE CHAIN
REMARK 500 ARG H 286 0.13 SIDE CHAIN
REMARK 500 ARG I 18 0.11 SIDE CHAIN
REMARK 500 ARG I 91 0.12 SIDE CHAIN
REMARK 500 ARG I 171 0.10 SIDE CHAIN
REMARK 500 ARG I 294 0.10 SIDE CHAIN
REMARK 500 ARG J 18 0.08 SIDE CHAIN
REMARK 500 ARG J 286 0.08 SIDE CHAIN
REMARK 500 ARG J 295 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 26QV A 1 303 UNP A0A0U5ADH4_9NOCA
DBREF2 26QV A A0A0U5ADH4 1 303
DBREF1 26QV B 1 303 UNP A0A0U5ADH4_9NOCA
DBREF2 26QV B A0A0U5ADH4 1 303
DBREF1 26QV C 1 303 UNP A0A0U5ADH4_9NOCA
DBREF2 26QV C A0A0U5ADH4 1 303
DBREF1 26QV D 1 303 UNP A0A0U5ADH4_9NOCA
DBREF2 26QV D A0A0U5ADH4 1 303
DBREF1 26QV E 1 303 UNP A0A0U5ADH4_9NOCA
DBREF2 26QV E A0A0U5ADH4 1 303
DBREF1 26QV F 1 303 UNP A0A0U5ADH4_9NOCA
DBREF2 26QV F A0A0U5ADH4 1 303
DBREF1 26QV G 1 303 UNP A0A0U5ADH4_9NOCA
DBREF2 26QV G A0A0U5ADH4 1 303
DBREF1 26QV H 1 303 UNP A0A0U5ADH4_9NOCA
DBREF2 26QV H A0A0U5ADH4 1 303
DBREF1 26QV I 1 303 UNP A0A0U5ADH4_9NOCA
DBREF2 26QV I A0A0U5ADH4 1 303
DBREF1 26QV J 1 303 UNP A0A0U5ADH4_9NOCA
DBREF2 26QV J A0A0U5ADH4 1 303
SEQRES 1 A 303 MET ASN THR ASP LEU SER VAL ASN TYR ILE SER VAL GLY
SEQRES 2 A 303 GLY ILE ARG THR ARG TYR ILE ASP GLN GLY GLU GLY PRO
SEQRES 3 A 303 VAL ILE LEU LEU ILE HIS GLY GLY HIS SER GLY MET SER
SEQRES 4 A 303 MET PRO VAL GLY GLY ASP GLY TRP ALA PRO VAL ILE ALA
SEQRES 5 A 303 PRO LEU VAL ASP LYS GLY PHE ARG VAL VAL THR PHE ASP
SEQRES 6 A 303 LYS LEU GLY GLN GLY GLU THR ASP LEU ALA PRO THR HIS
SEQRES 7 A 303 ALA GLU TRP THR PHE ASP ALA VAL VAL LYS HIS ALA ARG
SEQRES 8 A 303 GLY PHE ILE ASP ALA LEU GLY LEU GLU ASP MET ILE LEU
SEQRES 9 A 303 VAL GLY HIS SER ARG GLY GLY LEU LEU ALA SER LYS LEU
SEQRES 10 A 303 ALA LEU ASP MET PRO GLU SER THR LYS GLY LEU PHE ILE
SEQRES 11 A 303 VAL SER SER ALA THR LEU ALA GLY THR ASP ALA LYS PHE
SEQRES 12 A 303 ARG ASP VAL GLU PHE TYR ASP ALA ILE THR ARG SER LEU
SEQRES 13 A 303 PRO ALA ASP ALA SER PRO GLU GLU ILE CYS GLY ALA TYR
SEQRES 14 A 303 PHE ARG ALA LEU TYR VAL THR PRO VAL PRO GLN GLU GLN
SEQRES 15 A 303 ILE ASN ALA ALA ALA ALA LYS TYR VAL LYS GLU ASN HIS
SEQRES 16 A 303 GLN ASN ALA LEU LYS THR TYR PRO MET VAL GLU LYS LYS
SEQRES 17 A 303 TYR TRP GLU PRO SER LEU GLN ALA ALA LYS ASP ASP ILE
SEQRES 18 A 303 ARG ALA ARG LEU PHE ALA GLY GLU VAL ASN ILE PRO VAL
SEQRES 19 A 303 GLU VAL VAL TRP GLY ARG ASP ASP ARG SER ALA PRO VAL
SEQRES 20 A 303 ASP LEU GLY ILE ALA PHE TYR GLN LYS LEU ALA LEU VAL
SEQRES 21 A 303 SER GLU THR THR SER LEU HIS ILE LEU GLY THR ALA GLY
SEQRES 22 A 303 HIS ASN VAL PHE ALA GLU ARG THR GLU ASP PHE VAL ARG
SEQRES 23 A 303 ILE LEU ALA ASP TYR ALA GLY ARG ARG SER ALA SER TYR
SEQRES 24 A 303 ALA THR ARG ARG
SEQRES 1 B 303 MET ASN THR ASP LEU SER VAL ASN TYR ILE SER VAL GLY
SEQRES 2 B 303 GLY ILE ARG THR ARG TYR ILE ASP GLN GLY GLU GLY PRO
SEQRES 3 B 303 VAL ILE LEU LEU ILE HIS GLY GLY HIS SER GLY MET SER
SEQRES 4 B 303 MET PRO VAL GLY GLY ASP GLY TRP ALA PRO VAL ILE ALA
SEQRES 5 B 303 PRO LEU VAL ASP LYS GLY PHE ARG VAL VAL THR PHE ASP
SEQRES 6 B 303 LYS LEU GLY GLN GLY GLU THR ASP LEU ALA PRO THR HIS
SEQRES 7 B 303 ALA GLU TRP THR PHE ASP ALA VAL VAL LYS HIS ALA ARG
SEQRES 8 B 303 GLY PHE ILE ASP ALA LEU GLY LEU GLU ASP MET ILE LEU
SEQRES 9 B 303 VAL GLY HIS SER ARG GLY GLY LEU LEU ALA SER LYS LEU
SEQRES 10 B 303 ALA LEU ASP MET PRO GLU SER THR LYS GLY LEU PHE ILE
SEQRES 11 B 303 VAL SER SER ALA THR LEU ALA GLY THR ASP ALA LYS PHE
SEQRES 12 B 303 ARG ASP VAL GLU PHE TYR ASP ALA ILE THR ARG SER LEU
SEQRES 13 B 303 PRO ALA ASP ALA SER PRO GLU GLU ILE CYS GLY ALA TYR
SEQRES 14 B 303 PHE ARG ALA LEU TYR VAL THR PRO VAL PRO GLN GLU GLN
SEQRES 15 B 303 ILE ASN ALA ALA ALA ALA LYS TYR VAL LYS GLU ASN HIS
SEQRES 16 B 303 GLN ASN ALA LEU LYS THR TYR PRO MET VAL GLU LYS LYS
SEQRES 17 B 303 TYR TRP GLU PRO SER LEU GLN ALA ALA LYS ASP ASP ILE
SEQRES 18 B 303 ARG ALA ARG LEU PHE ALA GLY GLU VAL ASN ILE PRO VAL
SEQRES 19 B 303 GLU VAL VAL TRP GLY ARG ASP ASP ARG SER ALA PRO VAL
SEQRES 20 B 303 ASP LEU GLY ILE ALA PHE TYR GLN LYS LEU ALA LEU VAL
SEQRES 21 B 303 SER GLU THR THR SER LEU HIS ILE LEU GLY THR ALA GLY
SEQRES 22 B 303 HIS ASN VAL PHE ALA GLU ARG THR GLU ASP PHE VAL ARG
SEQRES 23 B 303 ILE LEU ALA ASP TYR ALA GLY ARG ARG SER ALA SER TYR
SEQRES 24 B 303 ALA THR ARG ARG
SEQRES 1 C 303 MET ASN THR ASP LEU SER VAL ASN TYR ILE SER VAL GLY
SEQRES 2 C 303 GLY ILE ARG THR ARG TYR ILE ASP GLN GLY GLU GLY PRO
SEQRES 3 C 303 VAL ILE LEU LEU ILE HIS GLY GLY HIS SER GLY MET SER
SEQRES 4 C 303 MET PRO VAL GLY GLY ASP GLY TRP ALA PRO VAL ILE ALA
SEQRES 5 C 303 PRO LEU VAL ASP LYS GLY PHE ARG VAL VAL THR PHE ASP
SEQRES 6 C 303 LYS LEU GLY GLN GLY GLU THR ASP LEU ALA PRO THR HIS
SEQRES 7 C 303 ALA GLU TRP THR PHE ASP ALA VAL VAL LYS HIS ALA ARG
SEQRES 8 C 303 GLY PHE ILE ASP ALA LEU GLY LEU GLU ASP MET ILE LEU
SEQRES 9 C 303 VAL GLY HIS SER ARG GLY GLY LEU LEU ALA SER LYS LEU
SEQRES 10 C 303 ALA LEU ASP MET PRO GLU SER THR LYS GLY LEU PHE ILE
SEQRES 11 C 303 VAL SER SER ALA THR LEU ALA GLY THR ASP ALA LYS PHE
SEQRES 12 C 303 ARG ASP VAL GLU PHE TYR ASP ALA ILE THR ARG SER LEU
SEQRES 13 C 303 PRO ALA ASP ALA SER PRO GLU GLU ILE CYS GLY ALA TYR
SEQRES 14 C 303 PHE ARG ALA LEU TYR VAL THR PRO VAL PRO GLN GLU GLN
SEQRES 15 C 303 ILE ASN ALA ALA ALA ALA LYS TYR VAL LYS GLU ASN HIS
SEQRES 16 C 303 GLN ASN ALA LEU LYS THR TYR PRO MET VAL GLU LYS LYS
SEQRES 17 C 303 TYR TRP GLU PRO SER LEU GLN ALA ALA LYS ASP ASP ILE
SEQRES 18 C 303 ARG ALA ARG LEU PHE ALA GLY GLU VAL ASN ILE PRO VAL
SEQRES 19 C 303 GLU VAL VAL TRP GLY ARG ASP ASP ARG SER ALA PRO VAL
SEQRES 20 C 303 ASP LEU GLY ILE ALA PHE TYR GLN LYS LEU ALA LEU VAL
SEQRES 21 C 303 SER GLU THR THR SER LEU HIS ILE LEU GLY THR ALA GLY
SEQRES 22 C 303 HIS ASN VAL PHE ALA GLU ARG THR GLU ASP PHE VAL ARG
SEQRES 23 C 303 ILE LEU ALA ASP TYR ALA GLY ARG ARG SER ALA SER TYR
SEQRES 24 C 303 ALA THR ARG ARG
SEQRES 1 D 303 MET ASN THR ASP LEU SER VAL ASN TYR ILE SER VAL GLY
SEQRES 2 D 303 GLY ILE ARG THR ARG TYR ILE ASP GLN GLY GLU GLY PRO
SEQRES 3 D 303 VAL ILE LEU LEU ILE HIS GLY GLY HIS SER GLY MET SER
SEQRES 4 D 303 MET PRO VAL GLY GLY ASP GLY TRP ALA PRO VAL ILE ALA
SEQRES 5 D 303 PRO LEU VAL ASP LYS GLY PHE ARG VAL VAL THR PHE ASP
SEQRES 6 D 303 LYS LEU GLY GLN GLY GLU THR ASP LEU ALA PRO THR HIS
SEQRES 7 D 303 ALA GLU TRP THR PHE ASP ALA VAL VAL LYS HIS ALA ARG
SEQRES 8 D 303 GLY PHE ILE ASP ALA LEU GLY LEU GLU ASP MET ILE LEU
SEQRES 9 D 303 VAL GLY HIS SER ARG GLY GLY LEU LEU ALA SER LYS LEU
SEQRES 10 D 303 ALA LEU ASP MET PRO GLU SER THR LYS GLY LEU PHE ILE
SEQRES 11 D 303 VAL SER SER ALA THR LEU ALA GLY THR ASP ALA LYS PHE
SEQRES 12 D 303 ARG ASP VAL GLU PHE TYR ASP ALA ILE THR ARG SER LEU
SEQRES 13 D 303 PRO ALA ASP ALA SER PRO GLU GLU ILE CYS GLY ALA TYR
SEQRES 14 D 303 PHE ARG ALA LEU TYR VAL THR PRO VAL PRO GLN GLU GLN
SEQRES 15 D 303 ILE ASN ALA ALA ALA ALA LYS TYR VAL LYS GLU ASN HIS
SEQRES 16 D 303 GLN ASN ALA LEU LYS THR TYR PRO MET VAL GLU LYS LYS
SEQRES 17 D 303 TYR TRP GLU PRO SER LEU GLN ALA ALA LYS ASP ASP ILE
SEQRES 18 D 303 ARG ALA ARG LEU PHE ALA GLY GLU VAL ASN ILE PRO VAL
SEQRES 19 D 303 GLU VAL VAL TRP GLY ARG ASP ASP ARG SER ALA PRO VAL
SEQRES 20 D 303 ASP LEU GLY ILE ALA PHE TYR GLN LYS LEU ALA LEU VAL
SEQRES 21 D 303 SER GLU THR THR SER LEU HIS ILE LEU GLY THR ALA GLY
SEQRES 22 D 303 HIS ASN VAL PHE ALA GLU ARG THR GLU ASP PHE VAL ARG
SEQRES 23 D 303 ILE LEU ALA ASP TYR ALA GLY ARG ARG SER ALA SER TYR
SEQRES 24 D 303 ALA THR ARG ARG
SEQRES 1 E 303 MET ASN THR ASP LEU SER VAL ASN TYR ILE SER VAL GLY
SEQRES 2 E 303 GLY ILE ARG THR ARG TYR ILE ASP GLN GLY GLU GLY PRO
SEQRES 3 E 303 VAL ILE LEU LEU ILE HIS GLY GLY HIS SER GLY MET SER
SEQRES 4 E 303 MET PRO VAL GLY GLY ASP GLY TRP ALA PRO VAL ILE ALA
SEQRES 5 E 303 PRO LEU VAL ASP LYS GLY PHE ARG VAL VAL THR PHE ASP
SEQRES 6 E 303 LYS LEU GLY GLN GLY GLU THR ASP LEU ALA PRO THR HIS
SEQRES 7 E 303 ALA GLU TRP THR PHE ASP ALA VAL VAL LYS HIS ALA ARG
SEQRES 8 E 303 GLY PHE ILE ASP ALA LEU GLY LEU GLU ASP MET ILE LEU
SEQRES 9 E 303 VAL GLY HIS SER ARG GLY GLY LEU LEU ALA SER LYS LEU
SEQRES 10 E 303 ALA LEU ASP MET PRO GLU SER THR LYS GLY LEU PHE ILE
SEQRES 11 E 303 VAL SER SER ALA THR LEU ALA GLY THR ASP ALA LYS PHE
SEQRES 12 E 303 ARG ASP VAL GLU PHE TYR ASP ALA ILE THR ARG SER LEU
SEQRES 13 E 303 PRO ALA ASP ALA SER PRO GLU GLU ILE CYS GLY ALA TYR
SEQRES 14 E 303 PHE ARG ALA LEU TYR VAL THR PRO VAL PRO GLN GLU GLN
SEQRES 15 E 303 ILE ASN ALA ALA ALA ALA LYS TYR VAL LYS GLU ASN HIS
SEQRES 16 E 303 GLN ASN ALA LEU LYS THR TYR PRO MET VAL GLU LYS LYS
SEQRES 17 E 303 TYR TRP GLU PRO SER LEU GLN ALA ALA LYS ASP ASP ILE
SEQRES 18 E 303 ARG ALA ARG LEU PHE ALA GLY GLU VAL ASN ILE PRO VAL
SEQRES 19 E 303 GLU VAL VAL TRP GLY ARG ASP ASP ARG SER ALA PRO VAL
SEQRES 20 E 303 ASP LEU GLY ILE ALA PHE TYR GLN LYS LEU ALA LEU VAL
SEQRES 21 E 303 SER GLU THR THR SER LEU HIS ILE LEU GLY THR ALA GLY
SEQRES 22 E 303 HIS ASN VAL PHE ALA GLU ARG THR GLU ASP PHE VAL ARG
SEQRES 23 E 303 ILE LEU ALA ASP TYR ALA GLY ARG ARG SER ALA SER TYR
SEQRES 24 E 303 ALA THR ARG ARG
SEQRES 1 F 303 MET ASN THR ASP LEU SER VAL ASN TYR ILE SER VAL GLY
SEQRES 2 F 303 GLY ILE ARG THR ARG TYR ILE ASP GLN GLY GLU GLY PRO
SEQRES 3 F 303 VAL ILE LEU LEU ILE HIS GLY GLY HIS SER GLY MET SER
SEQRES 4 F 303 MET PRO VAL GLY GLY ASP GLY TRP ALA PRO VAL ILE ALA
SEQRES 5 F 303 PRO LEU VAL ASP LYS GLY PHE ARG VAL VAL THR PHE ASP
SEQRES 6 F 303 LYS LEU GLY GLN GLY GLU THR ASP LEU ALA PRO THR HIS
SEQRES 7 F 303 ALA GLU TRP THR PHE ASP ALA VAL VAL LYS HIS ALA ARG
SEQRES 8 F 303 GLY PHE ILE ASP ALA LEU GLY LEU GLU ASP MET ILE LEU
SEQRES 9 F 303 VAL GLY HIS SER ARG GLY GLY LEU LEU ALA SER LYS LEU
SEQRES 10 F 303 ALA LEU ASP MET PRO GLU SER THR LYS GLY LEU PHE ILE
SEQRES 11 F 303 VAL SER SER ALA THR LEU ALA GLY THR ASP ALA LYS PHE
SEQRES 12 F 303 ARG ASP VAL GLU PHE TYR ASP ALA ILE THR ARG SER LEU
SEQRES 13 F 303 PRO ALA ASP ALA SER PRO GLU GLU ILE CYS GLY ALA TYR
SEQRES 14 F 303 PHE ARG ALA LEU TYR VAL THR PRO VAL PRO GLN GLU GLN
SEQRES 15 F 303 ILE ASN ALA ALA ALA ALA LYS TYR VAL LYS GLU ASN HIS
SEQRES 16 F 303 GLN ASN ALA LEU LYS THR TYR PRO MET VAL GLU LYS LYS
SEQRES 17 F 303 TYR TRP GLU PRO SER LEU GLN ALA ALA LYS ASP ASP ILE
SEQRES 18 F 303 ARG ALA ARG LEU PHE ALA GLY GLU VAL ASN ILE PRO VAL
SEQRES 19 F 303 GLU VAL VAL TRP GLY ARG ASP ASP ARG SER ALA PRO VAL
SEQRES 20 F 303 ASP LEU GLY ILE ALA PHE TYR GLN LYS LEU ALA LEU VAL
SEQRES 21 F 303 SER GLU THR THR SER LEU HIS ILE LEU GLY THR ALA GLY
SEQRES 22 F 303 HIS ASN VAL PHE ALA GLU ARG THR GLU ASP PHE VAL ARG
SEQRES 23 F 303 ILE LEU ALA ASP TYR ALA GLY ARG ARG SER ALA SER TYR
SEQRES 24 F 303 ALA THR ARG ARG
SEQRES 1 G 303 MET ASN THR ASP LEU SER VAL ASN TYR ILE SER VAL GLY
SEQRES 2 G 303 GLY ILE ARG THR ARG TYR ILE ASP GLN GLY GLU GLY PRO
SEQRES 3 G 303 VAL ILE LEU LEU ILE HIS GLY GLY HIS SER GLY MET SER
SEQRES 4 G 303 MET PRO VAL GLY GLY ASP GLY TRP ALA PRO VAL ILE ALA
SEQRES 5 G 303 PRO LEU VAL ASP LYS GLY PHE ARG VAL VAL THR PHE ASP
SEQRES 6 G 303 LYS LEU GLY GLN GLY GLU THR ASP LEU ALA PRO THR HIS
SEQRES 7 G 303 ALA GLU TRP THR PHE ASP ALA VAL VAL LYS HIS ALA ARG
SEQRES 8 G 303 GLY PHE ILE ASP ALA LEU GLY LEU GLU ASP MET ILE LEU
SEQRES 9 G 303 VAL GLY HIS SER ARG GLY GLY LEU LEU ALA SER LYS LEU
SEQRES 10 G 303 ALA LEU ASP MET PRO GLU SER THR LYS GLY LEU PHE ILE
SEQRES 11 G 303 VAL SER SER ALA THR LEU ALA GLY THR ASP ALA LYS PHE
SEQRES 12 G 303 ARG ASP VAL GLU PHE TYR ASP ALA ILE THR ARG SER LEU
SEQRES 13 G 303 PRO ALA ASP ALA SER PRO GLU GLU ILE CYS GLY ALA TYR
SEQRES 14 G 303 PHE ARG ALA LEU TYR VAL THR PRO VAL PRO GLN GLU GLN
SEQRES 15 G 303 ILE ASN ALA ALA ALA ALA LYS TYR VAL LYS GLU ASN HIS
SEQRES 16 G 303 GLN ASN ALA LEU LYS THR TYR PRO MET VAL GLU LYS LYS
SEQRES 17 G 303 TYR TRP GLU PRO SER LEU GLN ALA ALA LYS ASP ASP ILE
SEQRES 18 G 303 ARG ALA ARG LEU PHE ALA GLY GLU VAL ASN ILE PRO VAL
SEQRES 19 G 303 GLU VAL VAL TRP GLY ARG ASP ASP ARG SER ALA PRO VAL
SEQRES 20 G 303 ASP LEU GLY ILE ALA PHE TYR GLN LYS LEU ALA LEU VAL
SEQRES 21 G 303 SER GLU THR THR SER LEU HIS ILE LEU GLY THR ALA GLY
SEQRES 22 G 303 HIS ASN VAL PHE ALA GLU ARG THR GLU ASP PHE VAL ARG
SEQRES 23 G 303 ILE LEU ALA ASP TYR ALA GLY ARG ARG SER ALA SER TYR
SEQRES 24 G 303 ALA THR ARG ARG
SEQRES 1 H 303 MET ASN THR ASP LEU SER VAL ASN TYR ILE SER VAL GLY
SEQRES 2 H 303 GLY ILE ARG THR ARG TYR ILE ASP GLN GLY GLU GLY PRO
SEQRES 3 H 303 VAL ILE LEU LEU ILE HIS GLY GLY HIS SER GLY MET SER
SEQRES 4 H 303 MET PRO VAL GLY GLY ASP GLY TRP ALA PRO VAL ILE ALA
SEQRES 5 H 303 PRO LEU VAL ASP LYS GLY PHE ARG VAL VAL THR PHE ASP
SEQRES 6 H 303 LYS LEU GLY GLN GLY GLU THR ASP LEU ALA PRO THR HIS
SEQRES 7 H 303 ALA GLU TRP THR PHE ASP ALA VAL VAL LYS HIS ALA ARG
SEQRES 8 H 303 GLY PHE ILE ASP ALA LEU GLY LEU GLU ASP MET ILE LEU
SEQRES 9 H 303 VAL GLY HIS SER ARG GLY GLY LEU LEU ALA SER LYS LEU
SEQRES 10 H 303 ALA LEU ASP MET PRO GLU SER THR LYS GLY LEU PHE ILE
SEQRES 11 H 303 VAL SER SER ALA THR LEU ALA GLY THR ASP ALA LYS PHE
SEQRES 12 H 303 ARG ASP VAL GLU PHE TYR ASP ALA ILE THR ARG SER LEU
SEQRES 13 H 303 PRO ALA ASP ALA SER PRO GLU GLU ILE CYS GLY ALA TYR
SEQRES 14 H 303 PHE ARG ALA LEU TYR VAL THR PRO VAL PRO GLN GLU GLN
SEQRES 15 H 303 ILE ASN ALA ALA ALA ALA LYS TYR VAL LYS GLU ASN HIS
SEQRES 16 H 303 GLN ASN ALA LEU LYS THR TYR PRO MET VAL GLU LYS LYS
SEQRES 17 H 303 TYR TRP GLU PRO SER LEU GLN ALA ALA LYS ASP ASP ILE
SEQRES 18 H 303 ARG ALA ARG LEU PHE ALA GLY GLU VAL ASN ILE PRO VAL
SEQRES 19 H 303 GLU VAL VAL TRP GLY ARG ASP ASP ARG SER ALA PRO VAL
SEQRES 20 H 303 ASP LEU GLY ILE ALA PHE TYR GLN LYS LEU ALA LEU VAL
SEQRES 21 H 303 SER GLU THR THR SER LEU HIS ILE LEU GLY THR ALA GLY
SEQRES 22 H 303 HIS ASN VAL PHE ALA GLU ARG THR GLU ASP PHE VAL ARG
SEQRES 23 H 303 ILE LEU ALA ASP TYR ALA GLY ARG ARG SER ALA SER TYR
SEQRES 24 H 303 ALA THR ARG ARG
SEQRES 1 I 303 MET ASN THR ASP LEU SER VAL ASN TYR ILE SER VAL GLY
SEQRES 2 I 303 GLY ILE ARG THR ARG TYR ILE ASP GLN GLY GLU GLY PRO
SEQRES 3 I 303 VAL ILE LEU LEU ILE HIS GLY GLY HIS SER GLY MET SER
SEQRES 4 I 303 MET PRO VAL GLY GLY ASP GLY TRP ALA PRO VAL ILE ALA
SEQRES 5 I 303 PRO LEU VAL ASP LYS GLY PHE ARG VAL VAL THR PHE ASP
SEQRES 6 I 303 LYS LEU GLY GLN GLY GLU THR ASP LEU ALA PRO THR HIS
SEQRES 7 I 303 ALA GLU TRP THR PHE ASP ALA VAL VAL LYS HIS ALA ARG
SEQRES 8 I 303 GLY PHE ILE ASP ALA LEU GLY LEU GLU ASP MET ILE LEU
SEQRES 9 I 303 VAL GLY HIS SER ARG GLY GLY LEU LEU ALA SER LYS LEU
SEQRES 10 I 303 ALA LEU ASP MET PRO GLU SER THR LYS GLY LEU PHE ILE
SEQRES 11 I 303 VAL SER SER ALA THR LEU ALA GLY THR ASP ALA LYS PHE
SEQRES 12 I 303 ARG ASP VAL GLU PHE TYR ASP ALA ILE THR ARG SER LEU
SEQRES 13 I 303 PRO ALA ASP ALA SER PRO GLU GLU ILE CYS GLY ALA TYR
SEQRES 14 I 303 PHE ARG ALA LEU TYR VAL THR PRO VAL PRO GLN GLU GLN
SEQRES 15 I 303 ILE ASN ALA ALA ALA ALA LYS TYR VAL LYS GLU ASN HIS
SEQRES 16 I 303 GLN ASN ALA LEU LYS THR TYR PRO MET VAL GLU LYS LYS
SEQRES 17 I 303 TYR TRP GLU PRO SER LEU GLN ALA ALA LYS ASP ASP ILE
SEQRES 18 I 303 ARG ALA ARG LEU PHE ALA GLY GLU VAL ASN ILE PRO VAL
SEQRES 19 I 303 GLU VAL VAL TRP GLY ARG ASP ASP ARG SER ALA PRO VAL
SEQRES 20 I 303 ASP LEU GLY ILE ALA PHE TYR GLN LYS LEU ALA LEU VAL
SEQRES 21 I 303 SER GLU THR THR SER LEU HIS ILE LEU GLY THR ALA GLY
SEQRES 22 I 303 HIS ASN VAL PHE ALA GLU ARG THR GLU ASP PHE VAL ARG
SEQRES 23 I 303 ILE LEU ALA ASP TYR ALA GLY ARG ARG SER ALA SER TYR
SEQRES 24 I 303 ALA THR ARG ARG
SEQRES 1 J 303 MET ASN THR ASP LEU SER VAL ASN TYR ILE SER VAL GLY
SEQRES 2 J 303 GLY ILE ARG THR ARG TYR ILE ASP GLN GLY GLU GLY PRO
SEQRES 3 J 303 VAL ILE LEU LEU ILE HIS GLY GLY HIS SER GLY MET SER
SEQRES 4 J 303 MET PRO VAL GLY GLY ASP GLY TRP ALA PRO VAL ILE ALA
SEQRES 5 J 303 PRO LEU VAL ASP LYS GLY PHE ARG VAL VAL THR PHE ASP
SEQRES 6 J 303 LYS LEU GLY GLN GLY GLU THR ASP LEU ALA PRO THR HIS
SEQRES 7 J 303 ALA GLU TRP THR PHE ASP ALA VAL VAL LYS HIS ALA ARG
SEQRES 8 J 303 GLY PHE ILE ASP ALA LEU GLY LEU GLU ASP MET ILE LEU
SEQRES 9 J 303 VAL GLY HIS SER ARG GLY GLY LEU LEU ALA SER LYS LEU
SEQRES 10 J 303 ALA LEU ASP MET PRO GLU SER THR LYS GLY LEU PHE ILE
SEQRES 11 J 303 VAL SER SER ALA THR LEU ALA GLY THR ASP ALA LYS PHE
SEQRES 12 J 303 ARG ASP VAL GLU PHE TYR ASP ALA ILE THR ARG SER LEU
SEQRES 13 J 303 PRO ALA ASP ALA SER PRO GLU GLU ILE CYS GLY ALA TYR
SEQRES 14 J 303 PHE ARG ALA LEU TYR VAL THR PRO VAL PRO GLN GLU GLN
SEQRES 15 J 303 ILE ASN ALA ALA ALA ALA LYS TYR VAL LYS GLU ASN HIS
SEQRES 16 J 303 GLN ASN ALA LEU LYS THR TYR PRO MET VAL GLU LYS LYS
SEQRES 17 J 303 TYR TRP GLU PRO SER LEU GLN ALA ALA LYS ASP ASP ILE
SEQRES 18 J 303 ARG ALA ARG LEU PHE ALA GLY GLU VAL ASN ILE PRO VAL
SEQRES 19 J 303 GLU VAL VAL TRP GLY ARG ASP ASP ARG SER ALA PRO VAL
SEQRES 20 J 303 ASP LEU GLY ILE ALA PHE TYR GLN LYS LEU ALA LEU VAL
SEQRES 21 J 303 SER GLU THR THR SER LEU HIS ILE LEU GLY THR ALA GLY
SEQRES 22 J 303 HIS ASN VAL PHE ALA GLU ARG THR GLU ASP PHE VAL ARG
SEQRES 23 J 303 ILE LEU ALA ASP TYR ALA GLY ARG ARG SER ALA SER TYR
SEQRES 24 J 303 ALA THR ARG ARG
FORMUL 11 HOH *254(H2 O)
HELIX 1 AA1 GLY A 43 GLY A 46 5 4
HELIX 2 AA2 TRP A 47 LYS A 57 1 11
HELIX 3 AA3 THR A 77 TRP A 81 5 5
HELIX 4 AA4 THR A 82 LEU A 97 1 16
HELIX 5 AA5 ARG A 109 MET A 121 1 13
HELIX 6 AA6 SER A 133 GLY A 138 1 6
HELIX 7 AA7 PHE A 148 LEU A 156 1 9
HELIX 8 AA8 SER A 161 ALA A 172 1 12
HELIX 9 AA9 PRO A 179 VAL A 191 1 13
HELIX 10 AB1 LYS A 192 GLU A 206 1 15
HELIX 11 AB2 TYR A 209 PHE A 226 1 18
HELIX 12 AB3 PRO A 246 LEU A 259 1 14
HELIX 13 AB4 ASN A 275 ARG A 280 1 6
HELIX 14 AB5 ARG A 280 SER A 296 1 17
HELIX 15 AB6 GLY B 43 GLY B 46 5 4
HELIX 16 AB7 TRP B 47 LYS B 57 1 11
HELIX 17 AB8 THR B 77 TRP B 81 5 5
HELIX 18 AB9 THR B 82 LEU B 97 1 16
HELIX 19 AC1 ARG B 109 MET B 121 1 13
HELIX 20 AC2 SER B 133 GLY B 138 1 6
HELIX 21 AC3 PHE B 148 LEU B 156 1 9
HELIX 22 AC4 SER B 161 ARG B 171 1 11
HELIX 23 AC5 PRO B 179 VAL B 191 1 13
HELIX 24 AC6 LYS B 192 GLU B 206 1 15
HELIX 25 AC7 TYR B 209 GLY B 228 1 20
HELIX 26 AC8 PRO B 246 LEU B 259 1 14
HELIX 27 AC9 ASN B 275 ARG B 280 1 6
HELIX 28 AD1 ARG B 280 SER B 296 1 17
HELIX 29 AD2 GLY C 43 GLY C 46 5 4
HELIX 30 AD3 TRP C 47 LYS C 57 1 11
HELIX 31 AD4 THR C 77 TRP C 81 5 5
HELIX 32 AD5 THR C 82 GLY C 98 1 17
HELIX 33 AD6 ARG C 109 MET C 121 1 13
HELIX 34 AD7 SER C 133 GLY C 138 1 6
HELIX 35 AD8 ILE C 152 LEU C 156 5 5
HELIX 36 AD9 SER C 161 TYR C 174 1 14
HELIX 37 AE1 PRO C 179 VAL C 191 1 13
HELIX 38 AE2 LYS C 192 GLU C 206 1 15
HELIX 39 AE3 TYR C 209 PHE C 226 1 18
HELIX 40 AE4 PRO C 246 LEU C 259 1 14
HELIX 41 AE5 ASN C 275 ARG C 280 1 6
HELIX 42 AE6 ARG C 280 SER C 296 1 17
HELIX 43 AE7 GLY D 43 GLY D 46 5 4
HELIX 44 AE8 TRP D 47 LYS D 57 1 11
HELIX 45 AE9 THR D 77 TRP D 81 5 5
HELIX 46 AF1 THR D 82 GLY D 98 1 17
HELIX 47 AF2 ARG D 109 MET D 121 1 13
HELIX 48 AF3 SER D 133 GLY D 138 1 6
HELIX 49 AF4 TYR D 149 LEU D 156 1 8
HELIX 50 AF5 SER D 161 ARG D 171 1 11
HELIX 51 AF6 PRO D 179 VAL D 191 1 13
HELIX 52 AF7 LYS D 192 GLU D 206 1 15
HELIX 53 AF8 TYR D 209 PHE D 226 1 18
HELIX 54 AF9 PRO D 246 LEU D 259 1 14
HELIX 55 AG1 ASN D 275 ARG D 280 1 6
HELIX 56 AG2 ARG D 280 SER D 296 1 17
HELIX 57 AG3 GLY E 43 GLY E 46 5 4
HELIX 58 AG4 TRP E 47 LYS E 57 1 11
HELIX 59 AG5 THR E 77 TRP E 81 5 5
HELIX 60 AG6 THR E 82 LEU E 97 1 16
HELIX 61 AG7 ARG E 109 MET E 121 1 13
HELIX 62 AG8 SER E 133 GLY E 138 1 6
HELIX 63 AG9 TYR E 149 LEU E 156 1 8
HELIX 64 AH1 SER E 161 TYR E 174 1 14
HELIX 65 AH2 PRO E 179 VAL E 191 1 13
HELIX 66 AH3 LYS E 192 GLU E 206 1 15
HELIX 67 AH4 TYR E 209 PHE E 226 1 18
HELIX 68 AH5 PRO E 246 LEU E 259 1 14
HELIX 69 AH6 ASN E 275 ARG E 280 1 6
HELIX 70 AH7 ARG E 280 SER E 296 1 17
HELIX 71 AH8 GLY F 43 GLY F 46 5 4
HELIX 72 AH9 TRP F 47 LYS F 57 1 11
HELIX 73 AI1 THR F 77 TRP F 81 5 5
HELIX 74 AI2 THR F 82 GLY F 98 1 17
HELIX 75 AI3 ARG F 109 MET F 121 1 13
HELIX 76 AI4 TYR F 149 SER F 155 1 7
HELIX 77 AI5 SER F 161 ARG F 171 1 11
HELIX 78 AI6 PRO F 179 VAL F 191 1 13
HELIX 79 AI7 LYS F 192 GLU F 206 1 15
HELIX 80 AI8 TYR F 209 PHE F 226 1 18
HELIX 81 AI9 PRO F 246 LEU F 259 1 14
HELIX 82 AJ1 ASN F 275 ARG F 280 1 6
HELIX 83 AJ2 ARG F 280 SER F 296 1 17
HELIX 84 AJ3 GLY G 43 GLY G 46 5 4
HELIX 85 AJ4 TRP G 47 LYS G 57 1 11
HELIX 86 AJ5 THR G 77 TRP G 81 5 5
HELIX 87 AJ6 THR G 82 LEU G 97 1 16
HELIX 88 AJ7 ARG G 109 MET G 121 1 13
HELIX 89 AJ8 SER G 133 GLY G 138 1 6
HELIX 90 AJ9 TYR G 149 LEU G 156 1 8
HELIX 91 AK1 SER G 161 TYR G 174 1 14
HELIX 92 AK2 PRO G 179 VAL G 191 1 13
HELIX 93 AK3 LYS G 192 GLU G 206 1 15
HELIX 94 AK4 TYR G 209 PHE G 226 1 18
HELIX 95 AK5 PRO G 246 LEU G 259 1 14
HELIX 96 AK6 ASN G 275 ARG G 280 1 6
HELIX 97 AK7 ARG G 280 SER G 296 1 17
HELIX 98 AK8 GLY H 43 GLY H 46 5 4
HELIX 99 AK9 TRP H 47 LYS H 57 1 11
HELIX 100 AL1 THR H 77 TRP H 81 5 5
HELIX 101 AL2 THR H 82 LEU H 97 1 16
HELIX 102 AL3 ARG H 109 MET H 121 1 13
HELIX 103 AL4 SER H 133 GLY H 138 1 6
HELIX 104 AL5 TYR H 149 LEU H 156 1 8
HELIX 105 AL6 SER H 161 ALA H 172 1 12
HELIX 106 AL7 PRO H 179 VAL H 191 1 13
HELIX 107 AL8 LYS H 192 GLU H 206 1 15
HELIX 108 AL9 TYR H 209 PHE H 226 1 18
HELIX 109 AM1 PRO H 246 LEU H 259 1 14
HELIX 110 AM2 ASN H 275 ARG H 280 1 6
HELIX 111 AM3 ARG H 280 SER H 296 1 17
HELIX 112 AM4 GLY I 43 GLY I 46 5 4
HELIX 113 AM5 TRP I 47 LYS I 57 1 11
HELIX 114 AM6 THR I 77 TRP I 81 5 5
HELIX 115 AM7 THR I 82 GLY I 98 1 17
HELIX 116 AM8 ARG I 109 MET I 121 1 13
HELIX 117 AM9 SER I 133 GLY I 138 1 6
HELIX 118 AN1 PHE I 148 LEU I 156 1 9
HELIX 119 AN2 SER I 161 ARG I 171 1 11
HELIX 120 AN3 PRO I 179 VAL I 191 1 13
HELIX 121 AN4 LYS I 192 GLU I 206 1 15
HELIX 122 AN5 TYR I 209 ALA I 227 1 19
HELIX 123 AN6 PRO I 246 LEU I 259 1 14
HELIX 124 AN7 ASN I 275 ARG I 280 1 6
HELIX 125 AN8 ARG I 280 ARG I 294 1 15
HELIX 126 AN9 GLY J 43 GLY J 46 5 4
HELIX 127 AO1 TRP J 47 LYS J 57 1 11
HELIX 128 AO2 THR J 77 TRP J 81 5 5
HELIX 129 AO3 THR J 82 LEU J 97 1 16
HELIX 130 AO4 ARG J 109 MET J 121 1 13
HELIX 131 AO5 SER J 133 GLY J 138 1 6
HELIX 132 AO6 PHE J 148 SER J 155 1 8
HELIX 133 AO7 SER J 161 ARG J 171 1 11
HELIX 134 AO8 PRO J 179 VAL J 191 1 13
HELIX 135 AO9 LYS J 192 GLU J 206 1 15
HELIX 136 AP1 TYR J 209 PHE J 226 1 18
HELIX 137 AP2 PRO J 246 LEU J 259 1 14
HELIX 138 AP3 ASN J 275 ARG J 280 1 6
HELIX 139 AP4 ARG J 280 SER J 296 1 17
SHEET 1 AA116 VAL A 7 VAL A 12 0
SHEET 2 AA116 ILE A 15 GLN A 22 -1 O THR A 17 N ILE A 10
SHEET 3 AA116 ARG A 60 PHE A 64 -1 O THR A 63 N ILE A 20
SHEET 4 AA116 VAL A 27 ILE A 31 1 N LEU A 30 O VAL A 62
SHEET 5 AA116 MET A 102 HIS A 107 1 O VAL A 105 N ILE A 31
SHEET 6 AA116 THR A 125 VAL A 131 1 O GLY A 127 N LEU A 104
SHEET 7 AA116 VAL A 234 GLY A 239 1 O VAL A 237 N ILE A 130
SHEET 8 AA116 THR A 263 LEU A 269 1 O SER A 265 N VAL A 236
SHEET 9 AA116 THR B 263 LEU B 269 -1 O ILE B 268 N THR A 264
SHEET 10 AA116 VAL B 234 GLY B 239 1 N VAL B 236 O SER B 265
SHEET 11 AA116 THR B 125 VAL B 131 1 N ILE B 130 O GLU B 235
SHEET 12 AA116 MET B 102 HIS B 107 1 N LEU B 104 O GLY B 127
SHEET 13 AA116 VAL B 27 ILE B 31 1 N ILE B 31 O VAL B 105
SHEET 14 AA116 ARG B 60 PHE B 64 1 O ARG B 60 N ILE B 28
SHEET 15 AA116 ILE B 15 GLY B 23 -1 N ILE B 20 O THR B 63
SHEET 16 AA116 VAL B 7 VAL B 12 -1 N ILE B 10 O THR B 17
SHEET 1 AA216 ASN C 8 VAL C 12 0
SHEET 2 AA216 ILE C 15 GLY C 23 -1 O ILE C 15 N VAL C 12
SHEET 3 AA216 ARG C 60 PHE C 64 -1 O VAL C 61 N GLN C 22
SHEET 4 AA216 VAL C 27 ILE C 31 1 N ILE C 28 O ARG C 60
SHEET 5 AA216 MET C 102 HIS C 107 1 O ILE C 103 N LEU C 29
SHEET 6 AA216 THR C 125 VAL C 131 1 O GLY C 127 N LEU C 104
SHEET 7 AA216 VAL C 234 GLY C 239 1 O VAL C 237 N ILE C 130
SHEET 8 AA216 THR C 263 LEU C 269 1 O HIS C 267 N TRP C 238
SHEET 9 AA216 THR D 263 LEU D 269 -1 O LEU D 266 N LEU C 266
SHEET 10 AA216 VAL D 234 GLY D 239 1 N VAL D 236 O SER D 265
SHEET 11 AA216 THR D 125 VAL D 131 1 N ILE D 130 O VAL D 237
SHEET 12 AA216 MET D 102 HIS D 107 1 N LEU D 104 O GLY D 127
SHEET 13 AA216 VAL D 27 ILE D 31 1 N ILE D 31 O VAL D 105
SHEET 14 AA216 ARG D 60 PHE D 64 1 O ARG D 60 N ILE D 28
SHEET 15 AA216 ILE D 15 GLN D 22 -1 N GLN D 22 O VAL D 61
SHEET 16 AA216 VAL D 7 VAL D 12 -1 N ILE D 10 O THR D 17
SHEET 1 AA316 VAL E 7 VAL E 12 0
SHEET 2 AA316 ILE E 15 GLN E 22 -1 O THR E 17 N ILE E 10
SHEET 3 AA316 ARG E 60 PHE E 64 -1 O VAL E 61 N GLN E 22
SHEET 4 AA316 VAL E 27 ILE E 31 1 N LEU E 30 O VAL E 62
SHEET 5 AA316 MET E 102 HIS E 107 1 O VAL E 105 N LEU E 29
SHEET 6 AA316 THR E 125 VAL E 131 1 O GLY E 127 N LEU E 104
SHEET 7 AA316 VAL E 234 GLY E 239 1 O VAL E 237 N ILE E 130
SHEET 8 AA316 THR E 263 LEU E 269 1 O HIS E 267 N TRP E 238
SHEET 9 AA316 THR H 263 LEU H 269 -1 O LEU H 266 N LEU E 266
SHEET 10 AA316 VAL H 234 GLY H 239 1 N TRP H 238 O HIS H 267
SHEET 11 AA316 THR H 125 VAL H 131 1 N ILE H 130 O GLU H 235
SHEET 12 AA316 MET H 102 HIS H 107 1 N LEU H 104 O PHE H 129
SHEET 13 AA316 VAL H 27 ILE H 31 1 N ILE H 31 O VAL H 105
SHEET 14 AA316 ARG H 60 PHE H 64 1 O VAL H 62 N LEU H 30
SHEET 15 AA316 ILE H 15 GLN H 22 -1 N ILE H 20 O THR H 63
SHEET 16 AA316 VAL H 7 VAL H 12 -1 N ILE H 10 O THR H 17
SHEET 1 AA416 VAL F 7 VAL F 12 0
SHEET 2 AA416 ILE F 15 GLY F 23 -1 O THR F 17 N ILE F 10
SHEET 3 AA416 ARG F 60 PHE F 64 -1 O THR F 63 N ILE F 20
SHEET 4 AA416 VAL F 27 ILE F 31 1 N LEU F 30 O VAL F 62
SHEET 5 AA416 MET F 102 HIS F 107 1 O VAL F 105 N ILE F 31
SHEET 6 AA416 THR F 125 VAL F 131 1 O GLY F 127 N LEU F 104
SHEET 7 AA416 VAL F 234 GLY F 239 1 O VAL F 237 N ILE F 130
SHEET 8 AA416 THR F 263 LEU F 269 1 O HIS F 267 N TRP F 238
SHEET 9 AA416 THR G 263 LEU G 269 -1 O LEU G 266 N LEU F 266
SHEET 10 AA416 VAL G 234 GLY G 239 1 N TRP G 238 O HIS G 267
SHEET 11 AA416 THR G 125 VAL G 131 1 N ILE G 130 O VAL G 237
SHEET 12 AA416 MET G 102 HIS G 107 1 N LEU G 104 O GLY G 127
SHEET 13 AA416 VAL G 27 ILE G 31 1 N ILE G 31 O VAL G 105
SHEET 14 AA416 ARG G 60 PHE G 64 1 O VAL G 62 N ILE G 28
SHEET 15 AA416 ILE G 15 GLY G 23 -1 N GLN G 22 O VAL G 61
SHEET 16 AA416 VAL G 7 VAL G 12 -1 N ILE G 10 O THR G 17
SHEET 1 AA516 VAL I 7 VAL I 12 0
SHEET 2 AA516 ILE I 15 GLN I 22 -1 O ILE I 15 N VAL I 12
SHEET 3 AA516 ARG I 60 PHE I 64 -1 O THR I 63 N ILE I 20
SHEET 4 AA516 VAL I 27 ILE I 31 1 N ILE I 28 O ARG I 60
SHEET 5 AA516 MET I 102 HIS I 107 1 O VAL I 105 N ILE I 31
SHEET 6 AA516 THR I 125 VAL I 131 1 O GLY I 127 N LEU I 104
SHEET 7 AA516 VAL I 234 GLY I 239 1 O VAL I 237 N ILE I 130
SHEET 8 AA516 THR I 263 LEU I 269 1 O HIS I 267 N TRP I 238
SHEET 9 AA516 THR J 263 LEU J 269 -1 O LEU J 266 N LEU I 266
SHEET 10 AA516 VAL J 234 GLY J 239 1 N TRP J 238 O LEU J 269
SHEET 11 AA516 THR J 125 VAL J 131 1 N ILE J 130 O VAL J 237
SHEET 12 AA516 MET J 102 HIS J 107 1 N LEU J 104 O GLY J 127
SHEET 13 AA516 VAL J 27 ILE J 31 1 N LEU J 29 O VAL J 105
SHEET 14 AA516 ARG J 60 PHE J 64 1 O VAL J 62 N LEU J 30
SHEET 15 AA516 ILE J 15 GLN J 22 -1 N GLN J 22 O VAL J 61
SHEET 16 AA516 VAL J 7 VAL J 12 -1 N VAL J 12 O ILE J 15
CRYST1 177.612 245.492 191.658 90.00 90.00 90.00 C 2 2 2 80
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 0.005630 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004073 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005218 0.00000
TER 4393 ALA A 297
TER 8783 SER B 298
TER 13142 SER C 298
TER 17492 ALA D 297
TER 21881 SER E 298
TER 26230 SER F 298
TER 30619 SER G 298
TER 34980 SER H 298
TER 39323 SER I 296
TER 43739 SER J 298
MASTER 605 0 0 139 80 0 0 622176 10 0 240
END |