| content |
HEADER HYDROLASE 05-NOV-20 7AVR
TITLE THE TETRAMERIC STRUCTURE OF HALOALKANE DEHALOGENASE DPAA FROM
TITLE 2 PARAGLACIECOLA AGARILYTICA NO2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE 1;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 SYNONYM: HALOALKANE DEHALOGENASE DPAA;
COMPND 5 EC: 3.8.1.5;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PARAGLACIECOLA AGARILYTICA NO2;
SOURCE 3 ORGANISM_TAXID: 1125747;
SOURCE 4 GENE: DHMA1, GAGA_3124;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS HALOALKANE DEHALOGENASE, ENZYME, TETRAMER, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.MAZUR,P.KOLENKO,T.PRUDNIKOVA,P.GRINKEVICH,I.KUTA SMATANOVA
REVDAT 1 17-MAR-21 7AVR 0
JRNL AUTH A.MAZUR,T.PRUDNIKOVA,P.GRINKEVICH,J.R.MESTERS,D.MRAZOVA,
JRNL AUTH 2 R.CHALOUPKOVA,J.DAMBORSKY,M.KUTY,P.KOLENKO,I.KUTA SMATANOVA
JRNL TITL THE TETRAMERIC STRUCTURE OF THE NOVEL HALOALKANE
JRNL TITL 2 DEHALOGENASE DPAA FROM PARAGLACIECOLA AGARILYTICA NO2.
JRNL REF ACTA CRYSTALLOGR D STRUCT V. 77 347 2021
JRNL REF 2 BIOL
JRNL REFN ISSN 2059-7983
JRNL PMID 33645538
JRNL DOI 10.1107/S2059798321000486
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0189
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.44
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 182376
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) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 9496
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 13173
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.07
REMARK 3 BIN R VALUE (WORKING SET) : 0.0880
REMARK 3 BIN FREE R VALUE SET COUNT : 673
REMARK 3 BIN FREE R VALUE : 0.1180
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 18745
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 18
REMARK 3 SOLVENT ATOMS : 2008
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.06000
REMARK 3 B22 (A**2) : 0.25000
REMARK 3 B33 (A**2) : -0.18000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.035
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.030
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 : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 19269 ; 0.020 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 17587 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 26149 ; 1.769 ; 1.957
REMARK 3 BOND ANGLES OTHERS (DEGREES): 40893 ; 3.875 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2395 ; 6.127 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 899 ;35.803 ;24.839
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3181 ;13.557 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 80 ;21.643 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2808 ; 0.122 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 21591 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 3917 ; 0.017 ; 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): 9562 ; 3.290 ; 2.666
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 9561 ; 3.290 ; 2.665
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11945 ; 4.119 ; 3.988
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 11946 ; 4.119 ; 3.989
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 9707 ; 3.454 ; 2.816
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 9708 ; 3.453 ; 2.816
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 14199 ; 4.353 ; 4.160
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 22958 ; 6.242 ;32.170
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 22267 ; 6.038 ;31.793
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 28
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 3 299 B 3 299 19296 0.10 0.05
REMARK 3 2 A 3 299 C 3 299 19400 0.10 0.05
REMARK 3 3 A 3 298 D 3 298 19352 0.09 0.05
REMARK 3 4 A 3 299 E 3 299 19278 0.10 0.05
REMARK 3 5 A 3 298 F 3 298 19324 0.10 0.05
REMARK 3 6 A 3 299 G 3 299 19414 0.09 0.05
REMARK 3 7 A 3 301 H 3 301 19752 0.08 0.05
REMARK 3 8 B 3 299 C 3 299 19246 0.10 0.05
REMARK 3 9 B 3 298 D 3 298 19100 0.10 0.05
REMARK 3 10 B 3 300 E 3 300 19672 0.08 0.05
REMARK 3 11 B 3 298 F 3 298 19076 0.10 0.05
REMARK 3 12 B 3 299 G 3 299 19374 0.09 0.05
REMARK 3 13 B 3 299 H 3 299 19092 0.10 0.05
REMARK 3 14 C 3 298 D 3 298 19358 0.09 0.05
REMARK 3 15 C 3 299 E 3 299 19324 0.10 0.05
REMARK 3 16 C 2 298 F 2 298 19330 0.10 0.05
REMARK 3 17 C 2 300 G 2 300 19794 0.08 0.05
REMARK 3 18 C 3 299 H 3 299 19194 0.10 0.05
REMARK 3 19 D 3 298 E 3 298 19216 0.09 0.05
REMARK 3 20 D 3 298 F 3 298 19780 0.06 0.05
REMARK 3 21 D 3 298 G 3 298 19350 0.08 0.05
REMARK 3 22 D 3 298 H 3 298 19260 0.09 0.05
REMARK 3 23 E 3 298 F 3 298 19248 0.09 0.05
REMARK 3 24 E 3 299 G 3 299 19426 0.09 0.05
REMARK 3 25 E 3 299 H 3 299 19200 0.10 0.05
REMARK 3 26 F 2 298 G 2 298 19314 0.09 0.05
REMARK 3 27 F 3 298 H 3 298 19270 0.10 0.05
REMARK 3 28 G 3 299 H 3 299 19280 0.10 0.05
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 : 1.20
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 THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 7AVR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-NOV-20.
REMARK 100 THE DEPOSITION ID IS D_1292112003.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-SEP-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.918409
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 191831
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 47.440
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 1.790
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
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 : 1.300
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: 2XT0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M NA HEPES, 4% W/V PEG 400, 2 M
REMARK 280 (NH4)2SO4, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 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+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 58.69250
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 77.75300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 58.69250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 77.75300
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42190 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -113.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -165.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH F 682 LIES ON A SPECIAL POSITION.
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 THR A 2
REMARK 465 HIS A 302
REMARK 465 HIS A 303
REMARK 465 HIS A 304
REMARK 465 HIS A 305
REMARK 465 HIS A 306
REMARK 465 HIS A 307
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 ILE B 301
REMARK 465 HIS B 302
REMARK 465 HIS B 303
REMARK 465 HIS B 304
REMARK 465 HIS B 305
REMARK 465 HIS B 306
REMARK 465 HIS B 307
REMARK 465 MET C 1
REMARK 465 ILE C 301
REMARK 465 HIS C 302
REMARK 465 HIS C 303
REMARK 465 HIS C 304
REMARK 465 HIS C 305
REMARK 465 HIS C 306
REMARK 465 HIS C 307
REMARK 465 MET D 1
REMARK 465 THR D 2
REMARK 465 MET D 300
REMARK 465 ILE D 301
REMARK 465 HIS D 302
REMARK 465 HIS D 303
REMARK 465 HIS D 304
REMARK 465 HIS D 305
REMARK 465 HIS D 306
REMARK 465 HIS D 307
REMARK 465 MET E 1
REMARK 465 THR E 2
REMARK 465 ILE E 301
REMARK 465 HIS E 302
REMARK 465 HIS E 303
REMARK 465 HIS E 304
REMARK 465 HIS E 305
REMARK 465 HIS E 306
REMARK 465 HIS E 307
REMARK 465 MET F 1
REMARK 465 MET F 300
REMARK 465 ILE F 301
REMARK 465 HIS F 302
REMARK 465 HIS F 303
REMARK 465 HIS F 304
REMARK 465 HIS F 305
REMARK 465 HIS F 306
REMARK 465 HIS F 307
REMARK 465 MET G 1
REMARK 465 ILE G 301
REMARK 465 HIS G 302
REMARK 465 HIS G 303
REMARK 465 HIS G 304
REMARK 465 HIS G 305
REMARK 465 HIS G 306
REMARK 465 HIS G 307
REMARK 465 MET H 1
REMARK 465 THR H 2
REMARK 465 HIS H 302
REMARK 465 HIS H 303
REMARK 465 HIS H 304
REMARK 465 HIS H 305
REMARK 465 HIS H 306
REMARK 465 HIS H 307
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 SER F 34 OG
REMARK 470 ASP H 46 CG OD1 OD2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ASP C 28 CG
REMARK 480 ASP D 140 CG
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 ASP E 140 CB - CG - OD1 ANGL. DEV. = -6.8 DEGREES
REMARK 500 ASP E 140 CB - CG - OD2 ANGL. DEV. = 6.3 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 PRO A 20 45.20 -90.39
REMARK 500 SER A 34 -12.87 78.60
REMARK 500 PRO A 58 56.87 -103.74
REMARK 500 THR A 59 -166.65 -107.27
REMARK 500 ASP A 125 -137.20 52.31
REMARK 500 MET A 138 63.38 -162.60
REMARK 500 ASN A 149 101.62 -36.16
REMARK 500 ASN A 238 -35.27 -131.74
REMARK 500 MET A 300 38.29 -90.25
REMARK 500 PRO B 20 44.58 -89.76
REMARK 500 GLU B 33 -136.29 47.92
REMARK 500 PRO B 58 57.19 -105.08
REMARK 500 THR B 59 -164.53 -106.96
REMARK 500 ASN B 118 75.89 -104.17
REMARK 500 ASP B 125 -136.66 54.01
REMARK 500 MET B 138 49.30 -151.77
REMARK 500 ASN B 149 100.11 -19.33
REMARK 500 PRO C 20 43.58 -88.95
REMARK 500 SER C 34 -12.88 79.11
REMARK 500 PRO C 58 54.85 -103.11
REMARK 500 THR C 59 -165.01 -106.98
REMARK 500 ASP C 125 -137.96 53.80
REMARK 500 MET C 138 49.52 -153.09
REMARK 500 ASN C 149 106.38 -36.47
REMARK 500 TRP C 240 128.63 -36.68
REMARK 500 PRO D 20 45.72 -91.04
REMARK 500 SER D 34 -15.39 79.58
REMARK 500 PRO D 58 57.89 -103.74
REMARK 500 THR D 59 -167.64 -108.76
REMARK 500 ASP D 125 -136.81 53.04
REMARK 500 MET D 138 53.76 -153.29
REMARK 500 ASN D 149 100.87 -22.39
REMARK 500 PRO E 20 43.80 -89.15
REMARK 500 GLU E 33 -132.84 50.36
REMARK 500 GLU E 33 -131.65 50.36
REMARK 500 PRO E 58 57.79 -104.32
REMARK 500 THR E 59 -164.21 -108.40
REMARK 500 ASP E 125 -138.46 54.29
REMARK 500 MET E 138 49.67 -152.27
REMARK 500 ASN E 149 100.53 -24.35
REMARK 500 PRO F 20 46.02 -91.49
REMARK 500 SER F 34 -15.84 78.96
REMARK 500 PRO F 58 56.87 -104.37
REMARK 500 THR F 59 -164.62 -109.53
REMARK 500 ASP F 125 -138.88 55.49
REMARK 500 MET F 138 48.99 -151.28
REMARK 500 ASN F 149 98.72 -19.19
REMARK 500 PRO G 20 43.28 -86.99
REMARK 500 SER G 34 -10.61 76.54
REMARK 500 PRO G 58 56.33 -105.89
REMARK 500
REMARK 500 THIS ENTRY HAS 62 RAMACHANDRAN OUTLIERS.
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 A 756 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH A 757 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH A 758 DISTANCE = 5.98 ANGSTROMS
REMARK 525 HOH A 759 DISTANCE = 6.35 ANGSTROMS
REMARK 525 HOH A 760 DISTANCE = 6.48 ANGSTROMS
REMARK 525 HOH A 761 DISTANCE = 6.52 ANGSTROMS
REMARK 525 HOH A 762 DISTANCE = 6.55 ANGSTROMS
REMARK 525 HOH A 763 DISTANCE = 6.94 ANGSTROMS
REMARK 525 HOH A 764 DISTANCE = 7.37 ANGSTROMS
REMARK 525 HOH B 732 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH B 733 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH B 734 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH B 735 DISTANCE = 5.98 ANGSTROMS
REMARK 525 HOH B 736 DISTANCE = 6.04 ANGSTROMS
REMARK 525 HOH B 737 DISTANCE = 6.04 ANGSTROMS
REMARK 525 HOH B 738 DISTANCE = 6.05 ANGSTROMS
REMARK 525 HOH B 739 DISTANCE = 6.07 ANGSTROMS
REMARK 525 HOH B 740 DISTANCE = 6.64 ANGSTROMS
REMARK 525 HOH B 741 DISTANCE = 6.97 ANGSTROMS
REMARK 525 HOH B 742 DISTANCE = 7.00 ANGSTROMS
REMARK 525 HOH B 743 DISTANCE = 7.12 ANGSTROMS
REMARK 525 HOH B 744 DISTANCE = 8.90 ANGSTROMS
REMARK 525 HOH C 766 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH C 767 DISTANCE = 5.87 ANGSTROMS
REMARK 525 HOH C 768 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH C 769 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH C 770 DISTANCE = 6.08 ANGSTROMS
REMARK 525 HOH C 771 DISTANCE = 6.16 ANGSTROMS
REMARK 525 HOH C 772 DISTANCE = 6.33 ANGSTROMS
REMARK 525 HOH C 773 DISTANCE = 6.47 ANGSTROMS
REMARK 525 HOH C 774 DISTANCE = 6.54 ANGSTROMS
REMARK 525 HOH C 775 DISTANCE = 6.58 ANGSTROMS
REMARK 525 HOH C 776 DISTANCE = 6.60 ANGSTROMS
REMARK 525 HOH C 777 DISTANCE = 6.81 ANGSTROMS
REMARK 525 HOH C 778 DISTANCE = 6.94 ANGSTROMS
REMARK 525 HOH C 779 DISTANCE = 7.03 ANGSTROMS
REMARK 525 HOH C 780 DISTANCE = 7.04 ANGSTROMS
REMARK 525 HOH C 781 DISTANCE = 7.10 ANGSTROMS
REMARK 525 HOH C 782 DISTANCE = 7.22 ANGSTROMS
REMARK 525 HOH C 783 DISTANCE = 7.29 ANGSTROMS
REMARK 525 HOH C 784 DISTANCE = 7.78 ANGSTROMS
REMARK 525 HOH C 785 DISTANCE = 7.87 ANGSTROMS
REMARK 525 HOH C 786 DISTANCE = 7.96 ANGSTROMS
REMARK 525 HOH C 787 DISTANCE = 8.69 ANGSTROMS
REMARK 525 HOH C 788 DISTANCE = 8.75 ANGSTROMS
REMARK 525 HOH C 789 DISTANCE = 9.55 ANGSTROMS
REMARK 525 HOH C 790 DISTANCE = 10.67 ANGSTROMS
REMARK 525 HOH C 791 DISTANCE = 15.76 ANGSTROMS
REMARK 525 HOH D 710 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH D 711 DISTANCE = 6.16 ANGSTROMS
REMARK 525 HOH D 712 DISTANCE = 6.22 ANGSTROMS
REMARK 525 HOH D 713 DISTANCE = 6.59 ANGSTROMS
REMARK 525 HOH D 714 DISTANCE = 6.61 ANGSTROMS
REMARK 525 HOH D 715 DISTANCE = 6.64 ANGSTROMS
REMARK 525 HOH D 716 DISTANCE = 7.23 ANGSTROMS
REMARK 525 HOH D 717 DISTANCE = 9.65 ANGSTROMS
REMARK 525 HOH E 736 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH E 737 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH E 738 DISTANCE = 5.88 ANGSTROMS
REMARK 525 HOH E 739 DISTANCE = 5.94 ANGSTROMS
REMARK 525 HOH E 740 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH E 741 DISTANCE = 5.99 ANGSTROMS
REMARK 525 HOH E 742 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH E 743 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH E 744 DISTANCE = 6.14 ANGSTROMS
REMARK 525 HOH E 745 DISTANCE = 6.15 ANGSTROMS
REMARK 525 HOH E 746 DISTANCE = 6.17 ANGSTROMS
REMARK 525 HOH E 747 DISTANCE = 6.21 ANGSTROMS
REMARK 525 HOH E 748 DISTANCE = 6.24 ANGSTROMS
REMARK 525 HOH E 749 DISTANCE = 6.34 ANGSTROMS
REMARK 525 HOH E 750 DISTANCE = 6.41 ANGSTROMS
REMARK 525 HOH E 751 DISTANCE = 6.57 ANGSTROMS
REMARK 525 HOH E 752 DISTANCE = 6.72 ANGSTROMS
REMARK 525 HOH E 753 DISTANCE = 6.77 ANGSTROMS
REMARK 525 HOH E 754 DISTANCE = 6.87 ANGSTROMS
REMARK 525 HOH E 755 DISTANCE = 6.91 ANGSTROMS
REMARK 525 HOH E 756 DISTANCE = 7.32 ANGSTROMS
REMARK 525 HOH E 757 DISTANCE = 7.44 ANGSTROMS
REMARK 525 HOH E 758 DISTANCE = 7.72 ANGSTROMS
REMARK 525 HOH E 759 DISTANCE = 7.81 ANGSTROMS
REMARK 525 HOH E 760 DISTANCE = 7.84 ANGSTROMS
REMARK 525 HOH E 761 DISTANCE = 7.97 ANGSTROMS
REMARK 525 HOH E 762 DISTANCE = 8.44 ANGSTROMS
REMARK 525 HOH E 763 DISTANCE = 8.62 ANGSTROMS
REMARK 525 HOH E 764 DISTANCE = 9.12 ANGSTROMS
REMARK 525 HOH F 777 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH F 778 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH F 779 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH F 780 DISTANCE = 5.93 ANGSTROMS
REMARK 525 HOH F 781 DISTANCE = 6.05 ANGSTROMS
REMARK 525 HOH F 782 DISTANCE = 6.17 ANGSTROMS
REMARK 525 HOH F 783 DISTANCE = 6.27 ANGSTROMS
REMARK 525 HOH F 784 DISTANCE = 6.31 ANGSTROMS
REMARK 525 HOH F 785 DISTANCE = 6.56 ANGSTROMS
REMARK 525 HOH F 786 DISTANCE = 6.62 ANGSTROMS
REMARK 525 HOH F 787 DISTANCE = 6.76 ANGSTROMS
REMARK 525 HOH F 788 DISTANCE = 7.04 ANGSTROMS
REMARK 525 HOH F 789 DISTANCE = 7.08 ANGSTROMS
REMARK 525 HOH F 790 DISTANCE = 7.20 ANGSTROMS
REMARK 525 HOH F 791 DISTANCE = 7.32 ANGSTROMS
REMARK 525 HOH F 792 DISTANCE = 7.53 ANGSTROMS
REMARK 525 HOH F 793 DISTANCE = 7.66 ANGSTROMS
REMARK 525 HOH F 794 DISTANCE = 7.92 ANGSTROMS
REMARK 525 HOH F 795 DISTANCE = 8.04 ANGSTROMS
REMARK 525 HOH F 796 DISTANCE = 8.48 ANGSTROMS
REMARK 525 HOH F 797 DISTANCE = 8.60 ANGSTROMS
REMARK 525 HOH F 798 DISTANCE = 11.19 ANGSTROMS
REMARK 525 HOH G 714 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH G 715 DISTANCE = 5.99 ANGSTROMS
REMARK 525 HOH G 716 DISTANCE = 6.05 ANGSTROMS
REMARK 525 HOH G 717 DISTANCE = 6.05 ANGSTROMS
REMARK 525 HOH G 718 DISTANCE = 6.07 ANGSTROMS
REMARK 525 HOH G 719 DISTANCE = 6.15 ANGSTROMS
REMARK 525 HOH G 720 DISTANCE = 6.22 ANGSTROMS
REMARK 525 HOH G 721 DISTANCE = 6.27 ANGSTROMS
REMARK 525 HOH G 722 DISTANCE = 6.50 ANGSTROMS
REMARK 525 HOH G 723 DISTANCE = 6.52 ANGSTROMS
REMARK 525 HOH G 724 DISTANCE = 6.63 ANGSTROMS
REMARK 525 HOH G 725 DISTANCE = 6.68 ANGSTROMS
REMARK 525 HOH G 726 DISTANCE = 7.10 ANGSTROMS
REMARK 525 HOH G 727 DISTANCE = 7.73 ANGSTROMS
REMARK 525 HOH G 728 DISTANCE = 8.01 ANGSTROMS
REMARK 525 HOH G 729 DISTANCE = 8.46 ANGSTROMS
REMARK 525 HOH G 730 DISTANCE = 9.45 ANGSTROMS
REMARK 525 HOH G 731 DISTANCE = 9.90 ANGSTROMS
REMARK 525 HOH H 687 DISTANCE = 5.88 ANGSTROMS
REMARK 525 HOH H 688 DISTANCE = 6.20 ANGSTROMS
REMARK 525 HOH H 689 DISTANCE = 6.26 ANGSTROMS
REMARK 525 HOH H 690 DISTANCE = 6.33 ANGSTROMS
REMARK 525 HOH H 691 DISTANCE = 6.69 ANGSTROMS
REMARK 525 HOH H 692 DISTANCE = 6.84 ANGSTROMS
REMARK 525 HOH H 693 DISTANCE = 7.91 ANGSTROMS
REMARK 525 HOH H 694 DISTANCE = 8.03 ANGSTROMS
REMARK 525 HOH H 695 DISTANCE = 8.10 ANGSTROMS
REMARK 525 HOH H 696 DISTANCE = 8.42 ANGSTROMS
REMARK 525 HOH H 697 DISTANCE = 9.44 ANGSTROMS
REMARK 525 HOH H 698 DISTANCE = 10.03 ANGSTROMS
REMARK 525 HOH H 699 DISTANCE = 10.32 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL E 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL E 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL F 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL F 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL F 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL F 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL F 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL F 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL G 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL G 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL G 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL H 401
DBREF 7AVR A 3 301 UNP K6XNL5 K6XNL5_9ALTE 3 301
DBREF 7AVR B 3 301 UNP K6XNL5 K6XNL5_9ALTE 3 301
DBREF 7AVR C 3 301 UNP K6XNL5 K6XNL5_9ALTE 3 301
DBREF 7AVR D 3 301 UNP K6XNL5 K6XNL5_9ALTE 3 301
DBREF 7AVR E 3 301 UNP K6XNL5 K6XNL5_9ALTE 3 301
DBREF 7AVR F 3 301 UNP K6XNL5 K6XNL5_9ALTE 3 301
DBREF 7AVR G 3 301 UNP K6XNL5 K6XNL5_9ALTE 3 301
DBREF 7AVR H 3 301 UNP K6XNL5 K6XNL5_9ALTE 3 301
SEQADV 7AVR MET A 1 UNP K6XNL5 INITIATING METHIONINE
SEQADV 7AVR THR A 2 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS A 302 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS A 303 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS A 304 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS A 305 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS A 306 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS A 307 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR MET B 1 UNP K6XNL5 INITIATING METHIONINE
SEQADV 7AVR THR B 2 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS B 302 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS B 303 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS B 304 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS B 305 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS B 306 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS B 307 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR MET C 1 UNP K6XNL5 INITIATING METHIONINE
SEQADV 7AVR THR C 2 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS C 302 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS C 303 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS C 304 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS C 305 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS C 306 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS C 307 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR MET D 1 UNP K6XNL5 INITIATING METHIONINE
SEQADV 7AVR THR D 2 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS D 302 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS D 303 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS D 304 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS D 305 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS D 306 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS D 307 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR MET E 1 UNP K6XNL5 INITIATING METHIONINE
SEQADV 7AVR THR E 2 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS E 302 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS E 303 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS E 304 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS E 305 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS E 306 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS E 307 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR MET F 1 UNP K6XNL5 INITIATING METHIONINE
SEQADV 7AVR THR F 2 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS F 302 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS F 303 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS F 304 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS F 305 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS F 306 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS F 307 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR MET G 1 UNP K6XNL5 INITIATING METHIONINE
SEQADV 7AVR THR G 2 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS G 302 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS G 303 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS G 304 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS G 305 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS G 306 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS G 307 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR MET H 1 UNP K6XNL5 INITIATING METHIONINE
SEQADV 7AVR THR H 2 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS H 302 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS H 303 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS H 304 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS H 305 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS H 306 UNP K6XNL5 EXPRESSION TAG
SEQADV 7AVR HIS H 307 UNP K6XNL5 EXPRESSION TAG
SEQRES 1 A 307 MET THR ILE LYS ALA LEU ARG THR PRO GLU GLU ARG PHE
SEQRES 2 A 307 SER VAL LEU PRO ALA PHE PRO TYR GLN PRO ASN TYR VAL
SEQRES 3 A 307 ASP ASP LEU GLY GLY TYR GLU SER LEU ARG MET ALA TYR
SEQRES 4 A 307 ILE ASP GLU GLY ASP LYS ASP SER GLU TYR THR PHE LEU
SEQRES 5 A 307 CYS LEU HIS GLY GLU PRO THR TRP SER TYR LEU TYR ARG
SEQRES 6 A 307 LYS MET ILE PRO VAL PHE THR ASP ALA GLY HIS ARG VAL
SEQRES 7 A 307 VAL ALA PRO ASP LEU PHE GLY PHE GLY ARG SER ASP LYS
SEQRES 8 A 307 PRO ILE GLU ASP SER VAL TYR ASN PHE GLU PHE HIS ARG
SEQRES 9 A 307 ASN SER LEU ILE GLN LEU ILE GLU HIS LEU ASP LEU LYS
SEQRES 10 A 307 ASN ILE VAL LEU VAL CYS GLN ASP TRP GLY GLY GLY LEU
SEQRES 11 A 307 GLY LEU THR ILE PRO MET ASP MET GLN ASP ARG PHE LYS
SEQRES 12 A 307 LYS LEU ILE VAL MET ASN THR THR ILE SER ASN GLY GLU
SEQRES 13 A 307 PRO LEU ALA GLU ALA ALA VAL GLN TRP MET ALA PHE ASN
SEQRES 14 A 307 GLU THR ILE SER GLU LEU PRO VAL ALA GLY LEU VAL ALA
SEQRES 15 A 307 CYS ASP ALA GLY ALA ALA VAL ASN VAL MET ASP ALA LEU
SEQRES 16 A 307 ALA TYR ASP ALA PRO PHE PRO ASN LYS ASN TYR LYS VAL
SEQRES 17 A 307 GLY VAL LYS ARG PHE PRO GLN MET ILE PRO THR ASN ALA
SEQRES 18 A 307 ASP ASP ASP ALA VAL LYS TYR GLY LEU ARG ALA ILE GLU
SEQRES 19 A 307 PHE TRP SER ASN GLU TRP SER GLY GLU SER PHE MET ALA
SEQRES 20 A 307 ILE GLY MET LYS ASP ALA VAL LEU GLY GLU ALA ALA MET
SEQRES 21 A 307 MET GLN LEU LYS THR VAL ILE LYS GLY CYS PRO GLU PRO
SEQRES 22 A 307 MET LYS ILE GLU GLU ALA GLY HIS PHE VAL GLN GLU TYR
SEQRES 23 A 307 GLY VAL GLU VAL ALA GLU GLN ALA LEU ALA SER PHE THR
SEQRES 24 A 307 MET ILE HIS HIS HIS HIS HIS HIS
SEQRES 1 B 307 MET THR ILE LYS ALA LEU ARG THR PRO GLU GLU ARG PHE
SEQRES 2 B 307 SER VAL LEU PRO ALA PHE PRO TYR GLN PRO ASN TYR VAL
SEQRES 3 B 307 ASP ASP LEU GLY GLY TYR GLU SER LEU ARG MET ALA TYR
SEQRES 4 B 307 ILE ASP GLU GLY ASP LYS ASP SER GLU TYR THR PHE LEU
SEQRES 5 B 307 CYS LEU HIS GLY GLU PRO THR TRP SER TYR LEU TYR ARG
SEQRES 6 B 307 LYS MET ILE PRO VAL PHE THR ASP ALA GLY HIS ARG VAL
SEQRES 7 B 307 VAL ALA PRO ASP LEU PHE GLY PHE GLY ARG SER ASP LYS
SEQRES 8 B 307 PRO ILE GLU ASP SER VAL TYR ASN PHE GLU PHE HIS ARG
SEQRES 9 B 307 ASN SER LEU ILE GLN LEU ILE GLU HIS LEU ASP LEU LYS
SEQRES 10 B 307 ASN ILE VAL LEU VAL CYS GLN ASP TRP GLY GLY GLY LEU
SEQRES 11 B 307 GLY LEU THR ILE PRO MET ASP MET GLN ASP ARG PHE LYS
SEQRES 12 B 307 LYS LEU ILE VAL MET ASN THR THR ILE SER ASN GLY GLU
SEQRES 13 B 307 PRO LEU ALA GLU ALA ALA VAL GLN TRP MET ALA PHE ASN
SEQRES 14 B 307 GLU THR ILE SER GLU LEU PRO VAL ALA GLY LEU VAL ALA
SEQRES 15 B 307 CYS ASP ALA GLY ALA ALA VAL ASN VAL MET ASP ALA LEU
SEQRES 16 B 307 ALA TYR ASP ALA PRO PHE PRO ASN LYS ASN TYR LYS VAL
SEQRES 17 B 307 GLY VAL LYS ARG PHE PRO GLN MET ILE PRO THR ASN ALA
SEQRES 18 B 307 ASP ASP ASP ALA VAL LYS TYR GLY LEU ARG ALA ILE GLU
SEQRES 19 B 307 PHE TRP SER ASN GLU TRP SER GLY GLU SER PHE MET ALA
SEQRES 20 B 307 ILE GLY MET LYS ASP ALA VAL LEU GLY GLU ALA ALA MET
SEQRES 21 B 307 MET GLN LEU LYS THR VAL ILE LYS GLY CYS PRO GLU PRO
SEQRES 22 B 307 MET LYS ILE GLU GLU ALA GLY HIS PHE VAL GLN GLU TYR
SEQRES 23 B 307 GLY VAL GLU VAL ALA GLU GLN ALA LEU ALA SER PHE THR
SEQRES 24 B 307 MET ILE HIS HIS HIS HIS HIS HIS
SEQRES 1 C 307 MET THR ILE LYS ALA LEU ARG THR PRO GLU GLU ARG PHE
SEQRES 2 C 307 SER VAL LEU PRO ALA PHE PRO TYR GLN PRO ASN TYR VAL
SEQRES 3 C 307 ASP ASP LEU GLY GLY TYR GLU SER LEU ARG MET ALA TYR
SEQRES 4 C 307 ILE ASP GLU GLY ASP LYS ASP SER GLU TYR THR PHE LEU
SEQRES 5 C 307 CYS LEU HIS GLY GLU PRO THR TRP SER TYR LEU TYR ARG
SEQRES 6 C 307 LYS MET ILE PRO VAL PHE THR ASP ALA GLY HIS ARG VAL
SEQRES 7 C 307 VAL ALA PRO ASP LEU PHE GLY PHE GLY ARG SER ASP LYS
SEQRES 8 C 307 PRO ILE GLU ASP SER VAL TYR ASN PHE GLU PHE HIS ARG
SEQRES 9 C 307 ASN SER LEU ILE GLN LEU ILE GLU HIS LEU ASP LEU LYS
SEQRES 10 C 307 ASN ILE VAL LEU VAL CYS GLN ASP TRP GLY GLY GLY LEU
SEQRES 11 C 307 GLY LEU THR ILE PRO MET ASP MET GLN ASP ARG PHE LYS
SEQRES 12 C 307 LYS LEU ILE VAL MET ASN THR THR ILE SER ASN GLY GLU
SEQRES 13 C 307 PRO LEU ALA GLU ALA ALA VAL GLN TRP MET ALA PHE ASN
SEQRES 14 C 307 GLU THR ILE SER GLU LEU PRO VAL ALA GLY LEU VAL ALA
SEQRES 15 C 307 CYS ASP ALA GLY ALA ALA VAL ASN VAL MET ASP ALA LEU
SEQRES 16 C 307 ALA TYR ASP ALA PRO PHE PRO ASN LYS ASN TYR LYS VAL
SEQRES 17 C 307 GLY VAL LYS ARG PHE PRO GLN MET ILE PRO THR ASN ALA
SEQRES 18 C 307 ASP ASP ASP ALA VAL LYS TYR GLY LEU ARG ALA ILE GLU
SEQRES 19 C 307 PHE TRP SER ASN GLU TRP SER GLY GLU SER PHE MET ALA
SEQRES 20 C 307 ILE GLY MET LYS ASP ALA VAL LEU GLY GLU ALA ALA MET
SEQRES 21 C 307 MET GLN LEU LYS THR VAL ILE LYS GLY CYS PRO GLU PRO
SEQRES 22 C 307 MET LYS ILE GLU GLU ALA GLY HIS PHE VAL GLN GLU TYR
SEQRES 23 C 307 GLY VAL GLU VAL ALA GLU GLN ALA LEU ALA SER PHE THR
SEQRES 24 C 307 MET ILE HIS HIS HIS HIS HIS HIS
SEQRES 1 D 307 MET THR ILE LYS ALA LEU ARG THR PRO GLU GLU ARG PHE
SEQRES 2 D 307 SER VAL LEU PRO ALA PHE PRO TYR GLN PRO ASN TYR VAL
SEQRES 3 D 307 ASP ASP LEU GLY GLY TYR GLU SER LEU ARG MET ALA TYR
SEQRES 4 D 307 ILE ASP GLU GLY ASP LYS ASP SER GLU TYR THR PHE LEU
SEQRES 5 D 307 CYS LEU HIS GLY GLU PRO THR TRP SER TYR LEU TYR ARG
SEQRES 6 D 307 LYS MET ILE PRO VAL PHE THR ASP ALA GLY HIS ARG VAL
SEQRES 7 D 307 VAL ALA PRO ASP LEU PHE GLY PHE GLY ARG SER ASP LYS
SEQRES 8 D 307 PRO ILE GLU ASP SER VAL TYR ASN PHE GLU PHE HIS ARG
SEQRES 9 D 307 ASN SER LEU ILE GLN LEU ILE GLU HIS LEU ASP LEU LYS
SEQRES 10 D 307 ASN ILE VAL LEU VAL CYS GLN ASP TRP GLY GLY GLY LEU
SEQRES 11 D 307 GLY LEU THR ILE PRO MET ASP MET GLN ASP ARG PHE LYS
SEQRES 12 D 307 LYS LEU ILE VAL MET ASN THR THR ILE SER ASN GLY GLU
SEQRES 13 D 307 PRO LEU ALA GLU ALA ALA VAL GLN TRP MET ALA PHE ASN
SEQRES 14 D 307 GLU THR ILE SER GLU LEU PRO VAL ALA GLY LEU VAL ALA
SEQRES 15 D 307 CYS ASP ALA GLY ALA ALA VAL ASN VAL MET ASP ALA LEU
SEQRES 16 D 307 ALA TYR ASP ALA PRO PHE PRO ASN LYS ASN TYR LYS VAL
SEQRES 17 D 307 GLY VAL LYS ARG PHE PRO GLN MET ILE PRO THR ASN ALA
SEQRES 18 D 307 ASP ASP ASP ALA VAL LYS TYR GLY LEU ARG ALA ILE GLU
SEQRES 19 D 307 PHE TRP SER ASN GLU TRP SER GLY GLU SER PHE MET ALA
SEQRES 20 D 307 ILE GLY MET LYS ASP ALA VAL LEU GLY GLU ALA ALA MET
SEQRES 21 D 307 MET GLN LEU LYS THR VAL ILE LYS GLY CYS PRO GLU PRO
SEQRES 22 D 307 MET LYS ILE GLU GLU ALA GLY HIS PHE VAL GLN GLU TYR
SEQRES 23 D 307 GLY VAL GLU VAL ALA GLU GLN ALA LEU ALA SER PHE THR
SEQRES 24 D 307 MET ILE HIS HIS HIS HIS HIS HIS
SEQRES 1 E 307 MET THR ILE LYS ALA LEU ARG THR PRO GLU GLU ARG PHE
SEQRES 2 E 307 SER VAL LEU PRO ALA PHE PRO TYR GLN PRO ASN TYR VAL
SEQRES 3 E 307 ASP ASP LEU GLY GLY TYR GLU SER LEU ARG MET ALA TYR
SEQRES 4 E 307 ILE ASP GLU GLY ASP LYS ASP SER GLU TYR THR PHE LEU
SEQRES 5 E 307 CYS LEU HIS GLY GLU PRO THR TRP SER TYR LEU TYR ARG
SEQRES 6 E 307 LYS MET ILE PRO VAL PHE THR ASP ALA GLY HIS ARG VAL
SEQRES 7 E 307 VAL ALA PRO ASP LEU PHE GLY PHE GLY ARG SER ASP LYS
SEQRES 8 E 307 PRO ILE GLU ASP SER VAL TYR ASN PHE GLU PHE HIS ARG
SEQRES 9 E 307 ASN SER LEU ILE GLN LEU ILE GLU HIS LEU ASP LEU LYS
SEQRES 10 E 307 ASN ILE VAL LEU VAL CYS GLN ASP TRP GLY GLY GLY LEU
SEQRES 11 E 307 GLY LEU THR ILE PRO MET ASP MET GLN ASP ARG PHE LYS
SEQRES 12 E 307 LYS LEU ILE VAL MET ASN THR THR ILE SER ASN GLY GLU
SEQRES 13 E 307 PRO LEU ALA GLU ALA ALA VAL GLN TRP MET ALA PHE ASN
SEQRES 14 E 307 GLU THR ILE SER GLU LEU PRO VAL ALA GLY LEU VAL ALA
SEQRES 15 E 307 CYS ASP ALA GLY ALA ALA VAL ASN VAL MET ASP ALA LEU
SEQRES 16 E 307 ALA TYR ASP ALA PRO PHE PRO ASN LYS ASN TYR LYS VAL
SEQRES 17 E 307 GLY VAL LYS ARG PHE PRO GLN MET ILE PRO THR ASN ALA
SEQRES 18 E 307 ASP ASP ASP ALA VAL LYS TYR GLY LEU ARG ALA ILE GLU
SEQRES 19 E 307 PHE TRP SER ASN GLU TRP SER GLY GLU SER PHE MET ALA
SEQRES 20 E 307 ILE GLY MET LYS ASP ALA VAL LEU GLY GLU ALA ALA MET
SEQRES 21 E 307 MET GLN LEU LYS THR VAL ILE LYS GLY CYS PRO GLU PRO
SEQRES 22 E 307 MET LYS ILE GLU GLU ALA GLY HIS PHE VAL GLN GLU TYR
SEQRES 23 E 307 GLY VAL GLU VAL ALA GLU GLN ALA LEU ALA SER PHE THR
SEQRES 24 E 307 MET ILE HIS HIS HIS HIS HIS HIS
SEQRES 1 F 307 MET THR ILE LYS ALA LEU ARG THR PRO GLU GLU ARG PHE
SEQRES 2 F 307 SER VAL LEU PRO ALA PHE PRO TYR GLN PRO ASN TYR VAL
SEQRES 3 F 307 ASP ASP LEU GLY GLY TYR GLU SER LEU ARG MET ALA TYR
SEQRES 4 F 307 ILE ASP GLU GLY ASP LYS ASP SER GLU TYR THR PHE LEU
SEQRES 5 F 307 CYS LEU HIS GLY GLU PRO THR TRP SER TYR LEU TYR ARG
SEQRES 6 F 307 LYS MET ILE PRO VAL PHE THR ASP ALA GLY HIS ARG VAL
SEQRES 7 F 307 VAL ALA PRO ASP LEU PHE GLY PHE GLY ARG SER ASP LYS
SEQRES 8 F 307 PRO ILE GLU ASP SER VAL TYR ASN PHE GLU PHE HIS ARG
SEQRES 9 F 307 ASN SER LEU ILE GLN LEU ILE GLU HIS LEU ASP LEU LYS
SEQRES 10 F 307 ASN ILE VAL LEU VAL CYS GLN ASP TRP GLY GLY GLY LEU
SEQRES 11 F 307 GLY LEU THR ILE PRO MET ASP MET GLN ASP ARG PHE LYS
SEQRES 12 F 307 LYS LEU ILE VAL MET ASN THR THR ILE SER ASN GLY GLU
SEQRES 13 F 307 PRO LEU ALA GLU ALA ALA VAL GLN TRP MET ALA PHE ASN
SEQRES 14 F 307 GLU THR ILE SER GLU LEU PRO VAL ALA GLY LEU VAL ALA
SEQRES 15 F 307 CYS ASP ALA GLY ALA ALA VAL ASN VAL MET ASP ALA LEU
SEQRES 16 F 307 ALA TYR ASP ALA PRO PHE PRO ASN LYS ASN TYR LYS VAL
SEQRES 17 F 307 GLY VAL LYS ARG PHE PRO GLN MET ILE PRO THR ASN ALA
SEQRES 18 F 307 ASP ASP ASP ALA VAL LYS TYR GLY LEU ARG ALA ILE GLU
SEQRES 19 F 307 PHE TRP SER ASN GLU TRP SER GLY GLU SER PHE MET ALA
SEQRES 20 F 307 ILE GLY MET LYS ASP ALA VAL LEU GLY GLU ALA ALA MET
SEQRES 21 F 307 MET GLN LEU LYS THR VAL ILE LYS GLY CYS PRO GLU PRO
SEQRES 22 F 307 MET LYS ILE GLU GLU ALA GLY HIS PHE VAL GLN GLU TYR
SEQRES 23 F 307 GLY VAL GLU VAL ALA GLU GLN ALA LEU ALA SER PHE THR
SEQRES 24 F 307 MET ILE HIS HIS HIS HIS HIS HIS
SEQRES 1 G 307 MET THR ILE LYS ALA LEU ARG THR PRO GLU GLU ARG PHE
SEQRES 2 G 307 SER VAL LEU PRO ALA PHE PRO TYR GLN PRO ASN TYR VAL
SEQRES 3 G 307 ASP ASP LEU GLY GLY TYR GLU SER LEU ARG MET ALA TYR
SEQRES 4 G 307 ILE ASP GLU GLY ASP LYS ASP SER GLU TYR THR PHE LEU
SEQRES 5 G 307 CYS LEU HIS GLY GLU PRO THR TRP SER TYR LEU TYR ARG
SEQRES 6 G 307 LYS MET ILE PRO VAL PHE THR ASP ALA GLY HIS ARG VAL
SEQRES 7 G 307 VAL ALA PRO ASP LEU PHE GLY PHE GLY ARG SER ASP LYS
SEQRES 8 G 307 PRO ILE GLU ASP SER VAL TYR ASN PHE GLU PHE HIS ARG
SEQRES 9 G 307 ASN SER LEU ILE GLN LEU ILE GLU HIS LEU ASP LEU LYS
SEQRES 10 G 307 ASN ILE VAL LEU VAL CYS GLN ASP TRP GLY GLY GLY LEU
SEQRES 11 G 307 GLY LEU THR ILE PRO MET ASP MET GLN ASP ARG PHE LYS
SEQRES 12 G 307 LYS LEU ILE VAL MET ASN THR THR ILE SER ASN GLY GLU
SEQRES 13 G 307 PRO LEU ALA GLU ALA ALA VAL GLN TRP MET ALA PHE ASN
SEQRES 14 G 307 GLU THR ILE SER GLU LEU PRO VAL ALA GLY LEU VAL ALA
SEQRES 15 G 307 CYS ASP ALA GLY ALA ALA VAL ASN VAL MET ASP ALA LEU
SEQRES 16 G 307 ALA TYR ASP ALA PRO PHE PRO ASN LYS ASN TYR LYS VAL
SEQRES 17 G 307 GLY VAL LYS ARG PHE PRO GLN MET ILE PRO THR ASN ALA
SEQRES 18 G 307 ASP ASP ASP ALA VAL LYS TYR GLY LEU ARG ALA ILE GLU
SEQRES 19 G 307 PHE TRP SER ASN GLU TRP SER GLY GLU SER PHE MET ALA
SEQRES 20 G 307 ILE GLY MET LYS ASP ALA VAL LEU GLY GLU ALA ALA MET
SEQRES 21 G 307 MET GLN LEU LYS THR VAL ILE LYS GLY CYS PRO GLU PRO
SEQRES 22 G 307 MET LYS ILE GLU GLU ALA GLY HIS PHE VAL GLN GLU TYR
SEQRES 23 G 307 GLY VAL GLU VAL ALA GLU GLN ALA LEU ALA SER PHE THR
SEQRES 24 G 307 MET ILE HIS HIS HIS HIS HIS HIS
SEQRES 1 H 307 MET THR ILE LYS ALA LEU ARG THR PRO GLU GLU ARG PHE
SEQRES 2 H 307 SER VAL LEU PRO ALA PHE PRO TYR GLN PRO ASN TYR VAL
SEQRES 3 H 307 ASP ASP LEU GLY GLY TYR GLU SER LEU ARG MET ALA TYR
SEQRES 4 H 307 ILE ASP GLU GLY ASP LYS ASP SER GLU TYR THR PHE LEU
SEQRES 5 H 307 CYS LEU HIS GLY GLU PRO THR TRP SER TYR LEU TYR ARG
SEQRES 6 H 307 LYS MET ILE PRO VAL PHE THR ASP ALA GLY HIS ARG VAL
SEQRES 7 H 307 VAL ALA PRO ASP LEU PHE GLY PHE GLY ARG SER ASP LYS
SEQRES 8 H 307 PRO ILE GLU ASP SER VAL TYR ASN PHE GLU PHE HIS ARG
SEQRES 9 H 307 ASN SER LEU ILE GLN LEU ILE GLU HIS LEU ASP LEU LYS
SEQRES 10 H 307 ASN ILE VAL LEU VAL CYS GLN ASP TRP GLY GLY GLY LEU
SEQRES 11 H 307 GLY LEU THR ILE PRO MET ASP MET GLN ASP ARG PHE LYS
SEQRES 12 H 307 LYS LEU ILE VAL MET ASN THR THR ILE SER ASN GLY GLU
SEQRES 13 H 307 PRO LEU ALA GLU ALA ALA VAL GLN TRP MET ALA PHE ASN
SEQRES 14 H 307 GLU THR ILE SER GLU LEU PRO VAL ALA GLY LEU VAL ALA
SEQRES 15 H 307 CYS ASP ALA GLY ALA ALA VAL ASN VAL MET ASP ALA LEU
SEQRES 16 H 307 ALA TYR ASP ALA PRO PHE PRO ASN LYS ASN TYR LYS VAL
SEQRES 17 H 307 GLY VAL LYS ARG PHE PRO GLN MET ILE PRO THR ASN ALA
SEQRES 18 H 307 ASP ASP ASP ALA VAL LYS TYR GLY LEU ARG ALA ILE GLU
SEQRES 19 H 307 PHE TRP SER ASN GLU TRP SER GLY GLU SER PHE MET ALA
SEQRES 20 H 307 ILE GLY MET LYS ASP ALA VAL LEU GLY GLU ALA ALA MET
SEQRES 21 H 307 MET GLN LEU LYS THR VAL ILE LYS GLY CYS PRO GLU PRO
SEQRES 22 H 307 MET LYS ILE GLU GLU ALA GLY HIS PHE VAL GLN GLU TYR
SEQRES 23 H 307 GLY VAL GLU VAL ALA GLU GLN ALA LEU ALA SER PHE THR
SEQRES 24 H 307 MET ILE HIS HIS HIS HIS HIS HIS
HET CL A 401 1
HET CL B 401 1
HET CL C 401 1
HET CL C 402 1
HET CL C 403 1
HET CL D 401 1
HET CL E 401 1
HET CL E 402 1
HET CL F 401 1
HET CL F 402 1
HET CL F 403 1
HET CL F 404 1
HET CL F 405 1
HET CL F 406 1
HET CL G 401 1
HET CL G 402 1
HET CL G 403 1
HET CL H 401 1
HETNAM CL CHLORIDE ION
FORMUL 9 CL 18(CL 1-)
FORMUL 27 HOH *2008(H2 O)
HELIX 1 AA1 PRO A 9 SER A 14 5 6
HELIX 2 AA2 TRP A 60 ARG A 65 5 6
HELIX 3 AA3 MET A 67 ASP A 73 1 7
HELIX 4 AA4 GLU A 94 TYR A 98 5 5
HELIX 5 AA5 ASN A 99 LEU A 114 1 16
HELIX 6 AA6 ASP A 125 LEU A 132 1 8
HELIX 7 AA7 THR A 133 MET A 138 5 6
HELIX 8 AA8 ALA A 159 GLU A 170 1 12
HELIX 9 AA9 PRO A 176 GLY A 186 1 11
HELIX 10 AB1 ALA A 187 VAL A 189 5 3
HELIX 11 AB2 ASN A 190 ALA A 199 1 10
HELIX 12 AB3 ASN A 203 TYR A 206 5 4
HELIX 13 AB4 LYS A 207 MET A 216 1 10
HELIX 14 AB5 ASP A 223 GLU A 239 1 17
HELIX 15 AB6 GLY A 256 THR A 265 1 10
HELIX 16 AB7 PHE A 282 GLU A 285 5 4
HELIX 17 AB8 TYR A 286 PHE A 298 1 13
HELIX 18 AB9 PRO B 9 SER B 14 5 6
HELIX 19 AC1 TRP B 60 ARG B 65 5 6
HELIX 20 AC2 MET B 67 ALA B 74 1 8
HELIX 21 AC3 GLU B 94 TYR B 98 5 5
HELIX 22 AC4 ASN B 99 LEU B 114 1 16
HELIX 23 AC5 ASP B 125 LEU B 132 1 8
HELIX 24 AC6 THR B 133 ASP B 140 5 8
HELIX 25 AC7 ALA B 159 ILE B 172 1 14
HELIX 26 AC8 PRO B 176 GLY B 186 1 11
HELIX 27 AC9 ALA B 187 VAL B 189 5 3
HELIX 28 AD1 ASN B 190 ALA B 199 1 10
HELIX 29 AD2 ASN B 203 TYR B 206 5 4
HELIX 30 AD3 LYS B 207 ILE B 217 1 11
HELIX 31 AD4 ASP B 223 GLU B 239 1 17
HELIX 32 AD5 GLY B 256 THR B 265 1 10
HELIX 33 AD6 PHE B 282 GLU B 285 5 4
HELIX 34 AD7 TYR B 286 PHE B 298 1 13
HELIX 35 AD8 PRO C 9 SER C 14 5 6
HELIX 36 AD9 TRP C 60 ARG C 65 5 6
HELIX 37 AE1 MET C 67 ALA C 74 1 8
HELIX 38 AE2 GLU C 94 TYR C 98 5 5
HELIX 39 AE3 ASN C 99 LEU C 114 1 16
HELIX 40 AE4 ASP C 125 LEU C 132 1 8
HELIX 41 AE5 THR C 133 MET C 138 5 6
HELIX 42 AE6 ALA C 159 ILE C 172 1 14
HELIX 43 AE7 PRO C 176 GLY C 186 1 11
HELIX 44 AE8 ALA C 187 VAL C 189 5 3
HELIX 45 AE9 ASN C 190 ALA C 199 1 10
HELIX 46 AF1 ASN C 203 TYR C 206 5 4
HELIX 47 AF2 LYS C 207 ILE C 217 1 11
HELIX 48 AF3 ASP C 223 GLU C 239 1 17
HELIX 49 AF4 GLY C 256 THR C 265 1 10
HELIX 50 AF5 PHE C 282 GLU C 285 5 4
HELIX 51 AF6 TYR C 286 PHE C 298 1 13
HELIX 52 AF7 PRO D 9 SER D 14 5 6
HELIX 53 AF8 TRP D 60 ARG D 65 5 6
HELIX 54 AF9 MET D 67 ALA D 74 1 8
HELIX 55 AG1 GLU D 94 TYR D 98 5 5
HELIX 56 AG2 ASN D 99 LEU D 114 1 16
HELIX 57 AG3 ASP D 125 LEU D 132 1 8
HELIX 58 AG4 THR D 133 ASP D 140 5 8
HELIX 59 AG5 ALA D 159 ILE D 172 1 14
HELIX 60 AG6 PRO D 176 GLY D 186 1 11
HELIX 61 AG7 ALA D 187 VAL D 189 5 3
HELIX 62 AG8 ASN D 190 ALA D 199 1 10
HELIX 63 AG9 ASN D 203 TYR D 206 5 4
HELIX 64 AH1 LYS D 207 ILE D 217 1 11
HELIX 65 AH2 ASP D 223 GLU D 239 1 17
HELIX 66 AH3 GLY D 256 THR D 265 1 10
HELIX 67 AH4 PHE D 282 TYR D 286 5 5
HELIX 68 AH5 GLY D 287 PHE D 298 1 12
HELIX 69 AH6 PRO E 9 SER E 14 5 6
HELIX 70 AH7 TRP E 60 ARG E 65 5 6
HELIX 71 AH8 MET E 67 ALA E 74 1 8
HELIX 72 AH9 GLU E 94 TYR E 98 5 5
HELIX 73 AI1 ASN E 99 LEU E 114 1 16
HELIX 74 AI2 ASP E 125 LEU E 132 1 8
HELIX 75 AI3 THR E 133 ASP E 140 5 8
HELIX 76 AI4 ALA E 159 ILE E 172 1 14
HELIX 77 AI5 PRO E 176 GLY E 186 1 11
HELIX 78 AI6 ALA E 187 VAL E 189 5 3
HELIX 79 AI7 ASN E 190 ALA E 199 1 10
HELIX 80 AI8 ASN E 203 TYR E 206 5 4
HELIX 81 AI9 LYS E 207 ILE E 217 1 11
HELIX 82 AJ1 ASP E 223 GLU E 239 1 17
HELIX 83 AJ2 GLY E 256 THR E 265 1 10
HELIX 84 AJ3 PHE E 282 GLU E 285 5 4
HELIX 85 AJ4 TYR E 286 PHE E 298 1 13
HELIX 86 AJ5 PRO F 9 SER F 14 5 6
HELIX 87 AJ6 TRP F 60 ARG F 65 5 6
HELIX 88 AJ7 MET F 67 ALA F 74 1 8
HELIX 89 AJ8 GLU F 94 TYR F 98 5 5
HELIX 90 AJ9 ASN F 99 ASP F 115 1 17
HELIX 91 AK1 ASP F 125 LEU F 132 1 8
HELIX 92 AK2 THR F 133 ASP F 140 5 8
HELIX 93 AK3 ALA F 159 ILE F 172 1 14
HELIX 94 AK4 PRO F 176 GLY F 186 1 11
HELIX 95 AK5 ALA F 187 VAL F 189 5 3
HELIX 96 AK6 ASN F 190 ALA F 199 1 10
HELIX 97 AK7 ASN F 203 TYR F 206 5 4
HELIX 98 AK8 LYS F 207 ILE F 217 1 11
HELIX 99 AK9 ASP F 223 GLU F 239 1 17
HELIX 100 AL1 GLY F 256 THR F 265 1 10
HELIX 101 AL2 PHE F 282 TYR F 286 5 5
HELIX 102 AL3 GLY F 287 PHE F 298 1 12
HELIX 103 AL4 PRO G 9 SER G 14 5 6
HELIX 104 AL5 TRP G 60 ARG G 65 5 6
HELIX 105 AL6 MET G 67 ALA G 74 1 8
HELIX 106 AL7 GLU G 94 TYR G 98 5 5
HELIX 107 AL8 ASN G 99 ASP G 115 1 17
HELIX 108 AL9 ASP G 125 LEU G 132 1 8
HELIX 109 AM1 THR G 133 MET G 138 5 6
HELIX 110 AM2 ALA G 159 ILE G 172 1 14
HELIX 111 AM3 PRO G 176 GLY G 186 1 11
HELIX 112 AM4 ALA G 187 VAL G 189 5 3
HELIX 113 AM5 ASN G 190 ALA G 199 1 10
HELIX 114 AM6 ASN G 203 TYR G 206 5 4
HELIX 115 AM7 LYS G 207 MET G 216 1 10
HELIX 116 AM8 ASP G 223 GLU G 239 1 17
HELIX 117 AM9 GLY G 256 THR G 265 1 10
HELIX 118 AN1 PHE G 282 TYR G 286 5 5
HELIX 119 AN2 GLY G 287 PHE G 298 1 12
HELIX 120 AN3 PRO H 9 SER H 14 5 6
HELIX 121 AN4 TRP H 60 ARG H 65 5 6
HELIX 122 AN5 MET H 67 ALA H 74 1 8
HELIX 123 AN6 GLU H 94 TYR H 98 5 5
HELIX 124 AN7 ASN H 99 LEU H 114 1 16
HELIX 125 AN8 ASP H 125 LEU H 132 1 8
HELIX 126 AN9 THR H 133 ASP H 140 5 8
HELIX 127 AO1 ALA H 159 ILE H 172 1 14
HELIX 128 AO2 PRO H 176 GLY H 186 1 11
HELIX 129 AO3 ALA H 187 VAL H 189 5 3
HELIX 130 AO4 ASN H 190 ALA H 199 1 10
HELIX 131 AO5 ASN H 203 TYR H 206 5 4
HELIX 132 AO6 LYS H 207 ILE H 217 1 11
HELIX 133 AO7 ASP H 223 GLU H 239 1 17
HELIX 134 AO8 GLY H 256 THR H 265 1 10
HELIX 135 AO9 PHE H 282 GLU H 285 5 4
HELIX 136 AP1 TYR H 286 PHE H 298 1 13
SHEET 1 AA1 2 ALA A 5 LEU A 6 0
SHEET 2 AA1 2 LYS A 91 PRO A 92 -1 O LYS A 91 N LEU A 6
SHEET 1 AA2 8 ASN A 24 VAL A 26 0
SHEET 2 AA2 8 MET A 37 GLU A 42 -1 O TYR A 39 N ASN A 24
SHEET 3 AA2 8 ARG A 77 PRO A 81 -1 O VAL A 78 N GLU A 42
SHEET 4 AA2 8 THR A 50 LEU A 54 1 N PHE A 51 O ARG A 77
SHEET 5 AA2 8 ILE A 119 CYS A 123 1 O VAL A 122 N LEU A 52
SHEET 6 AA2 8 PHE A 142 VAL A 147 1 O ILE A 146 N LEU A 121
SHEET 7 AA2 8 GLU A 243 LYS A 251 1 O PHE A 245 N VAL A 147
SHEET 8 AA2 8 MET A 274 GLY A 280 1 O ILE A 276 N ILE A 248
SHEET 1 AA3 2 ALA B 5 LEU B 6 0
SHEET 2 AA3 2 LYS B 91 PRO B 92 -1 O LYS B 91 N LEU B 6
SHEET 1 AA4 8 ASN B 24 VAL B 26 0
SHEET 2 AA4 8 MET B 37 GLU B 42 -1 O TYR B 39 N ASN B 24
SHEET 3 AA4 8 ARG B 77 PRO B 81 -1 O ALA B 80 N ILE B 40
SHEET 4 AA4 8 THR B 50 LEU B 54 1 N PHE B 51 O ARG B 77
SHEET 5 AA4 8 ILE B 119 CYS B 123 1 O VAL B 122 N LEU B 52
SHEET 6 AA4 8 PHE B 142 MET B 148 1 O ILE B 146 N LEU B 121
SHEET 7 AA4 8 GLU B 243 LYS B 251 1 O ALA B 247 N VAL B 147
SHEET 8 AA4 8 MET B 274 GLY B 280 1 O ILE B 276 N ILE B 248
SHEET 1 AA5 2 ALA C 5 LEU C 6 0
SHEET 2 AA5 2 LYS C 91 PRO C 92 -1 O LYS C 91 N LEU C 6
SHEET 1 AA6 8 ASN C 24 VAL C 26 0
SHEET 2 AA6 8 MET C 37 GLU C 42 -1 O TYR C 39 N ASN C 24
SHEET 3 AA6 8 ARG C 77 PRO C 81 -1 O VAL C 78 N GLU C 42
SHEET 4 AA6 8 THR C 50 LEU C 54 1 N PHE C 51 O ARG C 77
SHEET 5 AA6 8 ILE C 119 CYS C 123 1 O VAL C 122 N LEU C 52
SHEET 6 AA6 8 PHE C 142 VAL C 147 1 O ILE C 146 N LEU C 121
SHEET 7 AA6 8 GLU C 243 LYS C 251 1 O ALA C 247 N VAL C 147
SHEET 8 AA6 8 MET C 274 GLY C 280 1 O ILE C 276 N ILE C 248
SHEET 1 AA7 2 ALA D 5 LEU D 6 0
SHEET 2 AA7 2 LYS D 91 PRO D 92 -1 O LYS D 91 N LEU D 6
SHEET 1 AA8 8 ASN D 24 VAL D 26 0
SHEET 2 AA8 8 MET D 37 GLU D 42 -1 O TYR D 39 N ASN D 24
SHEET 3 AA8 8 ARG D 77 PRO D 81 -1 O VAL D 78 N GLU D 42
SHEET 4 AA8 8 THR D 50 LEU D 54 1 N PHE D 51 O ARG D 77
SHEET 5 AA8 8 ILE D 119 CYS D 123 1 O VAL D 122 N LEU D 52
SHEET 6 AA8 8 PHE D 142 MET D 148 1 O ILE D 146 N LEU D 121
SHEET 7 AA8 8 GLU D 243 LYS D 251 1 O PHE D 245 N VAL D 147
SHEET 8 AA8 8 MET D 274 GLY D 280 1 O ILE D 276 N ILE D 248
SHEET 1 AA9 2 ALA E 5 LEU E 6 0
SHEET 2 AA9 2 LYS E 91 PRO E 92 -1 O LYS E 91 N LEU E 6
SHEET 1 AB1 8 ASN E 24 VAL E 26 0
SHEET 2 AB1 8 MET E 37 GLU E 42 -1 O TYR E 39 N ASN E 24
SHEET 3 AB1 8 ARG E 77 PRO E 81 -1 O VAL E 78 N GLU E 42
SHEET 4 AB1 8 THR E 50 LEU E 54 1 N PHE E 51 O ARG E 77
SHEET 5 AB1 8 ILE E 119 CYS E 123 1 O VAL E 122 N LEU E 52
SHEET 6 AB1 8 PHE E 142 MET E 148 1 O ILE E 146 N LEU E 121
SHEET 7 AB1 8 GLU E 243 LYS E 251 1 O PHE E 245 N VAL E 147
SHEET 8 AB1 8 MET E 274 GLY E 280 1 O ILE E 276 N ILE E 248
SHEET 1 AB2 2 ALA F 5 LEU F 6 0
SHEET 2 AB2 2 LYS F 91 PRO F 92 -1 O LYS F 91 N LEU F 6
SHEET 1 AB3 8 ASN F 24 VAL F 26 0
SHEET 2 AB3 8 MET F 37 GLU F 42 -1 O TYR F 39 N ASN F 24
SHEET 3 AB3 8 ARG F 77 PRO F 81 -1 O VAL F 78 N GLU F 42
SHEET 4 AB3 8 THR F 50 LEU F 54 1 N PHE F 51 O ARG F 77
SHEET 5 AB3 8 ILE F 119 CYS F 123 1 O VAL F 122 N LEU F 52
SHEET 6 AB3 8 PHE F 142 MET F 148 1 O ILE F 146 N LEU F 121
SHEET 7 AB3 8 GLU F 243 LYS F 251 1 O PHE F 245 N VAL F 147
SHEET 8 AB3 8 MET F 274 GLY F 280 1 O ILE F 276 N ILE F 248
SHEET 1 AB4 2 ALA G 5 LEU G 6 0
SHEET 2 AB4 2 LYS G 91 PRO G 92 -1 O LYS G 91 N LEU G 6
SHEET 1 AB5 8 ASN G 24 VAL G 26 0
SHEET 2 AB5 8 MET G 37 GLU G 42 -1 O TYR G 39 N ASN G 24
SHEET 3 AB5 8 ARG G 77 PRO G 81 -1 O VAL G 78 N GLU G 42
SHEET 4 AB5 8 THR G 50 LEU G 54 1 N PHE G 51 O ARG G 77
SHEET 5 AB5 8 ILE G 119 CYS G 123 1 O VAL G 122 N LEU G 52
SHEET 6 AB5 8 PHE G 142 MET G 148 1 O ILE G 146 N LEU G 121
SHEET 7 AB5 8 GLU G 243 LYS G 251 1 O ALA G 247 N VAL G 147
SHEET 8 AB5 8 MET G 274 GLY G 280 1 O ILE G 276 N ILE G 248
SHEET 1 AB6 2 ALA H 5 LEU H 6 0
SHEET 2 AB6 2 LYS H 91 PRO H 92 -1 O LYS H 91 N LEU H 6
SHEET 1 AB7 8 ASN H 24 VAL H 26 0
SHEET 2 AB7 8 MET H 37 GLU H 42 -1 O TYR H 39 N ASN H 24
SHEET 3 AB7 8 ARG H 77 PRO H 81 -1 O VAL H 78 N GLU H 42
SHEET 4 AB7 8 THR H 50 LEU H 54 1 N PHE H 51 O ARG H 77
SHEET 5 AB7 8 ILE H 119 CYS H 123 1 O VAL H 122 N LEU H 52
SHEET 6 AB7 8 PHE H 142 MET H 148 1 O ILE H 146 N LEU H 121
SHEET 7 AB7 8 GLU H 243 LYS H 251 1 O PHE H 245 N VAL H 147
SHEET 8 AB7 8 MET H 274 GLY H 280 1 O ILE H 276 N ILE H 248
CISPEP 1 GLU A 57 PRO A 58 0 -22.48
CISPEP 2 GLU B 57 PRO B 58 0 -20.84
CISPEP 3 GLU C 57 PRO C 58 0 -21.29
CISPEP 4 GLU D 57 PRO D 58 0 -22.44
CISPEP 5 GLU E 57 PRO E 58 0 -21.85
CISPEP 6 GLU F 57 PRO F 58 0 -22.01
CISPEP 7 GLU G 57 PRO G 58 0 -18.86
CISPEP 8 GLU H 57 PRO H 58 0 -21.16
SITE 1 AC1 6 GLU A 57 TRP A 126 TRP A 165 PHE A 213
SITE 2 AC1 6 PRO A 214 HOH A 596
SITE 1 AC2 5 GLU B 57 TRP B 126 TRP B 165 PHE B 213
SITE 2 AC2 5 PRO B 214
SITE 1 AC3 5 GLU C 57 TRP C 126 TRP C 165 PRO C 214
SITE 2 AC3 5 HOH C 643
SITE 1 AC4 2 LEU C 6 ARG C 7
SITE 1 AC5 6 ARG C 7 THR C 8 ARG C 88 SER C 89
SITE 2 AC5 6 LYS C 91 HOH C 650
SITE 1 AC6 4 TRP D 126 TRP D 165 PHE D 213 PRO D 214
SITE 1 AC7 4 GLU E 57 TRP E 126 TRP E 165 PRO E 214
SITE 1 AC8 4 SER E 47 GLU E 48 GLY E 75 HOH E 534
SITE 1 AC9 5 HOH E 536 MET F 136 ASP F 137 MET F 138
SITE 2 AC9 5 GLN F 139
SITE 1 AD1 6 GLU F 57 TRP F 126 TRP F 165 PHE F 213
SITE 2 AD1 6 PRO F 214 HOH F 629
SITE 1 AD2 6 SER F 153 ASN F 154 GLY F 155 PRO F 218
SITE 2 AD2 6 HOH F 541 HOH F 581
SITE 1 AD3 2 PRO F 157 LEU F 158
SITE 1 AD4 3 GLY F 186 ALA F 187 TYR F 286
SITE 1 AD5 2 GLU F 272 HOH H 637
SITE 1 AD6 3 TRP G 126 TRP G 165 PRO G 214
SITE 1 AD7 3 LEU G 6 ARG G 7 HOH G 564
SITE 1 AD8 6 ARG G 7 THR G 8 ARG G 88 SER G 89
SITE 2 AD8 6 LYS G 91 HOH G 604
SITE 1 AD9 6 GLU H 57 TRP H 126 TRP H 165 PHE H 213
SITE 2 AD9 6 PRO H 214 HOH H 567
CRYST1 117.385 155.506 155.611 90.00 90.00 90.00 P 21 21 2 32
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 0.008519 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006431 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006426 0.00000
TER 2356 ILE A 301
TER 4698 MET B 300
TER 7053 MET C 300
TER 9387 THR D 299
TER 11746 MET E 300
TER 14095 THR F 299
TER 16450 MET G 300
TER 18803 ILE H 301
MASTER 695 0 18 136 80 0 27 620771 8 0 192
END |