HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 10-MAY-05 1ZMB
TITLE CRYSTAL STRUCTURE OF THE PUTATIVE ACETYLXYLAN ESTERASE FROM
TITLE 2 CLOSTRIDIUM ACETOBUTYLICUM, NORTHEAST STRUCTURAL GENOMICS TARGET CAR6
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLXYLAN ESTERASE RELATED ENZYME;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM ACETOBUTYLICUM;
SOURCE 3 ORGANISM_TAXID: 272562;
SOURCE 4 STRAIN: ATCC 824;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)+MAGIC;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET21(BL21)
KEYWDS ALPHA-BETA PROTEIN, STRUCTURAL GENOMICS, PSI, PROTEIN STRUCTURE
KEYWDS 2 INITIATIVE, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, NESG, UNKNOWN
KEYWDS 3 FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR F.FOROUHAR,S.M.VOROBIEV,M.ABASHIDZE,M.CIAO,T.B.ACTON,G.T.MONTELIONE,
AUTHOR 2 J.F.HUNT,L.TONG,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG)
REVDAT 3 13-JUL-11 1ZMB 1 VERSN
REVDAT 2 24-FEB-09 1ZMB 1 VERSN
REVDAT 1 17-MAY-05 1ZMB 0
JRNL AUTH F.FOROUHAR,S.M.VOROBIEV,M.ABASHIDZE,M.CIAO,T.B.ACTON,
JRNL AUTH 2 G.T.MONTELIONE,J.F.HUNT,L.TONG
JRNL TITL CRYSTAL STRUCTURE OF THE PUTATIVE ACETYLXYLAN ESTERASE FROM
JRNL TITL 2 CLOSTRIDIUM ACETOBUTYLICUM, NORTHEAST STRUCTURAL GENOMICS
JRNL TITL 3 TARGET CAR6
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.61 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XTALVIEW, CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.61
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.31
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 243470.200
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 82.9
REMARK 3 NUMBER OF REFLECTIONS : 104393
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 SET) : 0.243
REMARK 3 FREE R VALUE : 0.269
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.700
REMARK 3 FREE R VALUE TEST SET COUNT : 10170
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.76
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 55.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 10598
REMARK 3 BIN R VALUE (WORKING SET) : 0.3040
REMARK 3 BIN FREE R VALUE : 0.3150
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 1090
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.010
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 13668
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 123
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.50000
REMARK 3 B22 (A**2) : -1.07000
REMARK 3 B33 (A**2) : 0.57000
REMARK 3 B12 (A**2) : 3.94000
REMARK 3 B13 (A**2) : 1.70000
REMARK 3 B23 (A**2) : 6.87000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.36
REMARK 3 ESD FROM SIGMAA (A) : 0.41
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.40
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.47
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.20
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.72
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : OVERALL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.32
REMARK 3 BSOL : 13.29
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ZMB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-MAY-05.
REMARK 100 THE RCSB ID CODE IS RCSB032887.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-FEB-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97914
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 118658
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.08800
REMARK 200 R SYM (I) : 0.07600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.0400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.37500
REMARK 200 R SYM FOR SHELL (I) : 0.34100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXS, SOLVE/RESOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES, 10% PEG 20K, AND 5 MM DTT,
REMARK 280 PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3570 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
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 HIS A 285
REMARK 465 HIS A 286
REMARK 465 HIS A 287
REMARK 465 HIS A 288
REMARK 465 HIS A 289
REMARK 465 HIS A 290
REMARK 465 HIS B 285
REMARK 465 HIS B 286
REMARK 465 HIS B 287
REMARK 465 HIS B 288
REMARK 465 HIS B 289
REMARK 465 HIS B 290
REMARK 465 HIS C 285
REMARK 465 HIS C 286
REMARK 465 HIS C 287
REMARK 465 HIS C 288
REMARK 465 HIS C 289
REMARK 465 HIS C 290
REMARK 465 HIS D 285
REMARK 465 HIS D 286
REMARK 465 HIS D 287
REMARK 465 HIS D 288
REMARK 465 HIS D 289
REMARK 465 HIS D 290
REMARK 465 HIS E 285
REMARK 465 HIS E 286
REMARK 465 HIS E 287
REMARK 465 HIS E 288
REMARK 465 HIS E 289
REMARK 465 HIS E 290
REMARK 465 HIS F 285
REMARK 465 HIS F 286
REMARK 465 HIS F 287
REMARK 465 HIS F 288
REMARK 465 HIS F 289
REMARK 465 HIS F 290
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 ASN A 35 63.08 36.18
REMARK 500 ASN A 46 77.70 -102.55
REMARK 500 SER A 108 17.38 -159.00
REMARK 500 SER A 123 36.26 -92.16
REMARK 500 ASN A 125 62.64 24.21
REMARK 500 ASN A 127 10.77 47.60
REMARK 500 LYS A 164 -47.40 -143.03
REMARK 500 ARG A 166 -113.73 16.58
REMARK 500 LEU A 283 -81.47 -77.21
REMARK 500 ASN B 35 62.89 36.67
REMARK 500 ASN B 46 78.79 -103.55
REMARK 500 SER B 108 16.02 -159.52
REMARK 500 SER B 123 37.22 -90.02
REMARK 500 ASN B 125 63.37 25.25
REMARK 500 ASN B 127 10.97 47.73
REMARK 500 LYS B 164 -48.62 -142.79
REMARK 500 ARG B 166 -113.81 16.53
REMARK 500 LEU B 283 -91.08 -75.80
REMARK 500 ASN C 35 64.32 38.00
REMARK 500 ASN C 46 78.94 -101.67
REMARK 500 SER C 108 17.89 -159.82
REMARK 500 SER C 123 35.31 -89.70
REMARK 500 ASN C 125 63.03 22.52
REMARK 500 ASN C 127 10.38 47.83
REMARK 500 LYS C 164 -48.08 -141.66
REMARK 500 ARG C 166 -114.25 15.91
REMARK 500 ASP C 204 -6.90 -59.99
REMARK 500 ARG C 247 135.37 -39.78
REMARK 500 LEU C 283 -96.95 -73.91
REMARK 500 ASN D 35 64.56 37.69
REMARK 500 ASN D 46 78.61 -101.60
REMARK 500 CYS D 78 28.46 -141.39
REMARK 500 SER D 108 17.80 -157.75
REMARK 500 SER D 123 35.93 -89.81
REMARK 500 ASN D 125 62.50 24.41
REMARK 500 ASN D 127 10.82 48.05
REMARK 500 LYS D 164 -48.30 -143.12
REMARK 500 ARG D 166 -114.35 16.15
REMARK 500 LEU D 283 -91.82 -75.52
REMARK 500 ASN E 35 62.52 37.88
REMARK 500 ASN E 46 79.71 -102.35
REMARK 500 SER E 108 16.95 -158.19
REMARK 500 SER E 123 36.12 -90.83
REMARK 500 ASN E 125 63.73 24.25
REMARK 500 ASN E 127 11.06 47.15
REMARK 500 LYS E 164 -47.00 -142.72
REMARK 500 ARG E 166 -112.88 16.41
REMARK 500 LEU E 283 -93.08 -76.77
REMARK 500 ASN F 35 63.51 37.80
REMARK 500 ASN F 46 79.04 -103.50
REMARK 500
REMARK 500 THIS ENTRY HAS 58 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 315 DISTANCE = 5.03 ANGSTROMS
REMARK 525 HOH F 307 DISTANCE = 5.74 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: CAR6 RELATED DB: TARGETDB
DBREF 1ZMB A 1 282 UNP Q97LM8 Q97LM8_CLOAB 1 282
DBREF 1ZMB B 1 282 UNP Q97LM8 Q97LM8_CLOAB 1 282
DBREF 1ZMB C 1 282 UNP Q97LM8 Q97LM8_CLOAB 1 282
DBREF 1ZMB D 1 282 UNP Q97LM8 Q97LM8_CLOAB 1 282
DBREF 1ZMB E 1 282 UNP Q97LM8 Q97LM8_CLOAB 1 282
DBREF 1ZMB F 1 282 UNP Q97LM8 Q97LM8_CLOAB 1 282
SEQADV 1ZMB MSE A 1 UNP Q97LM8 MET 1 MODIFIED RESIDUE
SEQADV 1ZMB MSE A 7 UNP Q97LM8 MET 7 MODIFIED RESIDUE
SEQADV 1ZMB MSE A 13 UNP Q97LM8 MET 13 MODIFIED RESIDUE
SEQADV 1ZMB MSE A 24 UNP Q97LM8 MET 24 MODIFIED RESIDUE
SEQADV 1ZMB MSE A 32 UNP Q97LM8 MET 32 MODIFIED RESIDUE
SEQADV 1ZMB MSE A 40 UNP Q97LM8 MET 40 MODIFIED RESIDUE
SEQADV 1ZMB MSE A 41 UNP Q97LM8 MET 41 MODIFIED RESIDUE
SEQADV 1ZMB MSE A 106 UNP Q97LM8 MET 106 MODIFIED RESIDUE
SEQADV 1ZMB MSE A 260 UNP Q97LM8 MET 260 MODIFIED RESIDUE
SEQADV 1ZMB MSE A 277 UNP Q97LM8 MET 277 MODIFIED RESIDUE
SEQADV 1ZMB LEU A 283 UNP Q97LM8 CLONING ARTIFACT
SEQADV 1ZMB GLU A 284 UNP Q97LM8 CLONING ARTIFACT
SEQADV 1ZMB HIS A 285 UNP Q97LM8 CLONING ARTIFACT
SEQADV 1ZMB HIS A 286 UNP Q97LM8 CLONING ARTIFACT
SEQADV 1ZMB HIS A 287 UNP Q97LM8 CLONING ARTIFACT
SEQADV 1ZMB HIS A 288 UNP Q97LM8 CLONING ARTIFACT
SEQADV 1ZMB HIS A 289 UNP Q97LM8 CLONING ARTIFACT
SEQADV 1ZMB HIS A 290 UNP Q97LM8 CLONING ARTIFACT
SEQADV 1ZMB MSE B 1 UNP Q97LM8 MET 1 MODIFIED RESIDUE
SEQADV 1ZMB MSE B 7 UNP Q97LM8 MET 7 MODIFIED RESIDUE
SEQADV 1ZMB MSE B 13 UNP Q97LM8 MET 13 MODIFIED RESIDUE
SEQADV 1ZMB MSE B 24 UNP Q97LM8 MET 24 MODIFIED RESIDUE
SEQADV 1ZMB MSE B 32 UNP Q97LM8 MET 32 MODIFIED RESIDUE
SEQADV 1ZMB MSE B 40 UNP Q97LM8 MET 40 MODIFIED RESIDUE
SEQADV 1ZMB MSE B 41 UNP Q97LM8 MET 41 MODIFIED RESIDUE
SEQADV 1ZMB MSE B 106 UNP Q97LM8 MET 106 MODIFIED RESIDUE
SEQADV 1ZMB MSE B 260 UNP Q97LM8 MET 260 MODIFIED RESIDUE
SEQADV 1ZMB MSE B 277 UNP Q97LM8 MET 277 MODIFIED RESIDUE
SEQADV 1ZMB LEU B 283 UNP Q97LM8 CLONING ARTIFACT
SEQADV 1ZMB GLU B 284 UNP Q97LM8 CLONING ARTIFACT
SEQADV 1ZMB HIS B 285 UNP Q97LM8 CLONING ARTIFACT
SEQADV 1ZMB HIS B 286 UNP Q97LM8 CLONING ARTIFACT
SEQADV 1ZMB HIS B 287 UNP Q97LM8 CLONING ARTIFACT
SEQADV 1ZMB HIS B 288 UNP Q97LM8 CLONING ARTIFACT
SEQADV 1ZMB HIS B 289 UNP Q97LM8 CLONING ARTIFACT
SEQADV 1ZMB HIS B 290 UNP Q97LM8 CLONING ARTIFACT
SEQADV 1ZMB MSE C 1 UNP Q97LM8 MET 1 MODIFIED RESIDUE
SEQADV 1ZMB MSE C 7 UNP Q97LM8 MET 7 MODIFIED RESIDUE
SEQADV 1ZMB MSE C 13 UNP Q97LM8 MET 13 MODIFIED RESIDUE
SEQADV 1ZMB MSE C 24 UNP Q97LM8 MET 24 MODIFIED RESIDUE
SEQADV 1ZMB MSE C 32 UNP Q97LM8 MET 32 MODIFIED RESIDUE
SEQADV 1ZMB MSE C 40 UNP Q97LM8 MET 40 MODIFIED RESIDUE
SEQADV 1ZMB MSE C 41 UNP Q97LM8 MET 41 MODIFIED RESIDUE
SEQADV 1ZMB MSE C 106 UNP Q97LM8 MET 106 MODIFIED RESIDUE
SEQADV 1ZMB MSE C 260 UNP Q97LM8 MET 260 MODIFIED RESIDUE
SEQADV 1ZMB MSE C 277 UNP Q97LM8 MET 277 MODIFIED RESIDUE
SEQADV 1ZMB LEU C 283 UNP Q97LM8 CLONING ARTIFACT
SEQADV 1ZMB GLU C 284 UNP Q97LM8 CLONING ARTIFACT
SEQADV 1ZMB HIS C 285 UNP Q97LM8 CLONING ARTIFACT
SEQADV 1ZMB HIS C 286 UNP Q97LM8 CLONING ARTIFACT
SEQADV 1ZMB HIS C 287 UNP Q97LM8 CLONING ARTIFACT
SEQADV 1ZMB HIS C 288 UNP Q97LM8 CLONING ARTIFACT
SEQADV 1ZMB HIS C 289 UNP Q97LM8 CLONING ARTIFACT
SEQADV 1ZMB HIS C 290 UNP Q97LM8 CLONING ARTIFACT
SEQADV 1ZMB MSE D 1 UNP Q97LM8 MET 1 MODIFIED RESIDUE
SEQADV 1ZMB MSE D 7 UNP Q97LM8 MET 7 MODIFIED RESIDUE
SEQADV 1ZMB MSE D 13 UNP Q97LM8 MET 13 MODIFIED RESIDUE
SEQADV 1ZMB MSE D 24 UNP Q97LM8 MET 24 MODIFIED RESIDUE
SEQADV 1ZMB MSE D 32 UNP Q97LM8 MET 32 MODIFIED RESIDUE
SEQADV 1ZMB MSE D 40 UNP Q97LM8 MET 40 MODIFIED RESIDUE
SEQADV 1ZMB MSE D 41 UNP Q97LM8 MET 41 MODIFIED RESIDUE
SEQADV 1ZMB MSE D 106 UNP Q97LM8 MET 106 MODIFIED RESIDUE
SEQADV 1ZMB MSE D 260 UNP Q97LM8 MET 260 MODIFIED RESIDUE
SEQADV 1ZMB MSE D 277 UNP Q97LM8 MET 277 MODIFIED RESIDUE
SEQADV 1ZMB LEU D 283 UNP Q97LM8 CLONING ARTIFACT
SEQADV 1ZMB GLU D 284 UNP Q97LM8 CLONING ARTIFACT
SEQADV 1ZMB HIS D 285 UNP Q97LM8 CLONING ARTIFACT
SEQADV 1ZMB HIS D 286 UNP Q97LM8 CLONING ARTIFACT
SEQADV 1ZMB HIS D 287 UNP Q97LM8 CLONING ARTIFACT
SEQADV 1ZMB HIS D 288 UNP Q97LM8 CLONING ARTIFACT
SEQADV 1ZMB HIS D 289 UNP Q97LM8 CLONING ARTIFACT
SEQADV 1ZMB HIS D 290 UNP Q97LM8 CLONING ARTIFACT
SEQADV 1ZMB MSE E 1 UNP Q97LM8 MET 1 MODIFIED RESIDUE
SEQADV 1ZMB MSE E 7 UNP Q97LM8 MET 7 MODIFIED RESIDUE
SEQADV 1ZMB MSE E 13 UNP Q97LM8 MET 13 MODIFIED RESIDUE
SEQADV 1ZMB MSE E 24 UNP Q97LM8 MET 24 MODIFIED RESIDUE
SEQADV 1ZMB MSE E 32 UNP Q97LM8 MET 32 MODIFIED RESIDUE
SEQADV 1ZMB MSE E 40 UNP Q97LM8 MET 40 MODIFIED RESIDUE
SEQADV 1ZMB MSE E 41 UNP Q97LM8 MET 41 MODIFIED RESIDUE
SEQADV 1ZMB MSE E 106 UNP Q97LM8 MET 106 MODIFIED RESIDUE
SEQADV 1ZMB MSE E 260 UNP Q97LM8 MET 260 MODIFIED RESIDUE
SEQADV 1ZMB MSE E 277 UNP Q97LM8 MET 277 MODIFIED RESIDUE
SEQADV 1ZMB LEU E 283 UNP Q97LM8 CLONING ARTIFACT
SEQADV 1ZMB GLU E 284 UNP Q97LM8 CLONING ARTIFACT
SEQADV 1ZMB HIS E 285 UNP Q97LM8 CLONING ARTIFACT
SEQADV 1ZMB HIS E 286 UNP Q97LM8 CLONING ARTIFACT
SEQADV 1ZMB HIS E 287 UNP Q97LM8 CLONING ARTIFACT
SEQADV 1ZMB HIS E 288 UNP Q97LM8 CLONING ARTIFACT
SEQADV 1ZMB HIS E 289 UNP Q97LM8 CLONING ARTIFACT
SEQADV 1ZMB HIS E 290 UNP Q97LM8 CLONING ARTIFACT
SEQADV 1ZMB MSE F 1 UNP Q97LM8 MET 1 MODIFIED RESIDUE
SEQADV 1ZMB MSE F 7 UNP Q97LM8 MET 7 MODIFIED RESIDUE
SEQADV 1ZMB MSE F 13 UNP Q97LM8 MET 13 MODIFIED RESIDUE
SEQADV 1ZMB MSE F 24 UNP Q97LM8 MET 24 MODIFIED RESIDUE
SEQADV 1ZMB MSE F 32 UNP Q97LM8 MET 32 MODIFIED RESIDUE
SEQADV 1ZMB MSE F 40 UNP Q97LM8 MET 40 MODIFIED RESIDUE
SEQADV 1ZMB MSE F 41 UNP Q97LM8 MET 41 MODIFIED RESIDUE
SEQADV 1ZMB MSE F 106 UNP Q97LM8 MET 106 MODIFIED RESIDUE
SEQADV 1ZMB MSE F 260 UNP Q97LM8 MET 260 MODIFIED RESIDUE
SEQADV 1ZMB MSE F 277 UNP Q97LM8 MET 277 MODIFIED RESIDUE
SEQADV 1ZMB LEU F 283 UNP Q97LM8 CLONING ARTIFACT
SEQADV 1ZMB GLU F 284 UNP Q97LM8 CLONING ARTIFACT
SEQADV 1ZMB HIS F 285 UNP Q97LM8 CLONING ARTIFACT
SEQADV 1ZMB HIS F 286 UNP Q97LM8 CLONING ARTIFACT
SEQADV 1ZMB HIS F 287 UNP Q97LM8 CLONING ARTIFACT
SEQADV 1ZMB HIS F 288 UNP Q97LM8 CLONING ARTIFACT
SEQADV 1ZMB HIS F 289 UNP Q97LM8 CLONING ARTIFACT
SEQADV 1ZMB HIS F 290 UNP Q97LM8 CLONING ARTIFACT
SEQRES 1 A 290 MSE VAL LYS SER PHE LEU MSE LEU GLY GLN SER ASN MSE
SEQRES 2 A 290 ALA GLY ARG GLY PHE ILE ASN GLU VAL PRO MSE ILE TYR
SEQRES 3 A 290 ASN GLU ARG ILE GLN MSE LEU ARG ASN GLY ARG TRP GLN
SEQRES 4 A 290 MSE MSE THR GLU PRO ILE ASN TYR ASP ARG PRO VAL SER
SEQRES 5 A 290 GLY ILE SER LEU ALA GLY SER PHE ALA ASP ALA TRP SER
SEQRES 6 A 290 GLN LYS ASN GLN GLU ASP ILE ILE GLY LEU ILE PRO CYS
SEQRES 7 A 290 ALA GLU GLY GLY SER SER ILE ASP GLU TRP ALA LEU ASP
SEQRES 8 A 290 GLY VAL LEU PHE ARG HIS ALA LEU THR GLU ALA LYS PHE
SEQRES 9 A 290 ALA MSE GLU SER SER GLU LEU THR GLY ILE LEU TRP HIS
SEQRES 10 A 290 GLN GLY GLU SER ASP SER LEU ASN GLY ASN TYR LYS VAL
SEQRES 11 A 290 TYR TYR LYS LYS LEU LEU LEU ILE ILE GLU ALA LEU ARG
SEQRES 12 A 290 LYS GLU LEU ASN VAL PRO ASP ILE PRO ILE ILE ILE GLY
SEQRES 13 A 290 GLY LEU GLY ASP PHE LEU GLY LYS GLU ARG PHE GLY LYS
SEQRES 14 A 290 GLY CYS THR GLU TYR ASN PHE ILE ASN LYS GLU LEU GLN
SEQRES 15 A 290 LYS PHE ALA PHE GLU GLN ASP ASN CYS TYR PHE VAL THR
SEQRES 16 A 290 ALA SER GLY LEU THR CYS ASN PRO ASP GLY ILE HIS ILE
SEQRES 17 A 290 ASP ALA ILE SER GLN ARG LYS PHE GLY LEU ARG TYR PHE
SEQRES 18 A 290 GLU ALA PHE PHE ASN ARG LYS HIS VAL LEU GLU PRO LEU
SEQRES 19 A 290 ILE ASN GLU ASN GLU LEU LEU ASN LEU ASN TYR ALA ARG
SEQRES 20 A 290 THR HIS THR LYS ALA GLU LYS ILE TYR ILE LYS SER MSE
SEQRES 21 A 290 ASP PHE ALA LEU GLY LYS ILE SER TYR ASP GLU PHE THR
SEQRES 22 A 290 SER GLU LEU MSE LYS ILE ASN ASN ASP LEU GLU HIS HIS
SEQRES 23 A 290 HIS HIS HIS HIS
SEQRES 1 B 290 MSE VAL LYS SER PHE LEU MSE LEU GLY GLN SER ASN MSE
SEQRES 2 B 290 ALA GLY ARG GLY PHE ILE ASN GLU VAL PRO MSE ILE TYR
SEQRES 3 B 290 ASN GLU ARG ILE GLN MSE LEU ARG ASN GLY ARG TRP GLN
SEQRES 4 B 290 MSE MSE THR GLU PRO ILE ASN TYR ASP ARG PRO VAL SER
SEQRES 5 B 290 GLY ILE SER LEU ALA GLY SER PHE ALA ASP ALA TRP SER
SEQRES 6 B 290 GLN LYS ASN GLN GLU ASP ILE ILE GLY LEU ILE PRO CYS
SEQRES 7 B 290 ALA GLU GLY GLY SER SER ILE ASP GLU TRP ALA LEU ASP
SEQRES 8 B 290 GLY VAL LEU PHE ARG HIS ALA LEU THR GLU ALA LYS PHE
SEQRES 9 B 290 ALA MSE GLU SER SER GLU LEU THR GLY ILE LEU TRP HIS
SEQRES 10 B 290 GLN GLY GLU SER ASP SER LEU ASN GLY ASN TYR LYS VAL
SEQRES 11 B 290 TYR TYR LYS LYS LEU LEU LEU ILE ILE GLU ALA LEU ARG
SEQRES 12 B 290 LYS GLU LEU ASN VAL PRO ASP ILE PRO ILE ILE ILE GLY
SEQRES 13 B 290 GLY LEU GLY ASP PHE LEU GLY LYS GLU ARG PHE GLY LYS
SEQRES 14 B 290 GLY CYS THR GLU TYR ASN PHE ILE ASN LYS GLU LEU GLN
SEQRES 15 B 290 LYS PHE ALA PHE GLU GLN ASP ASN CYS TYR PHE VAL THR
SEQRES 16 B 290 ALA SER GLY LEU THR CYS ASN PRO ASP GLY ILE HIS ILE
SEQRES 17 B 290 ASP ALA ILE SER GLN ARG LYS PHE GLY LEU ARG TYR PHE
SEQRES 18 B 290 GLU ALA PHE PHE ASN ARG LYS HIS VAL LEU GLU PRO LEU
SEQRES 19 B 290 ILE ASN GLU ASN GLU LEU LEU ASN LEU ASN TYR ALA ARG
SEQRES 20 B 290 THR HIS THR LYS ALA GLU LYS ILE TYR ILE LYS SER MSE
SEQRES 21 B 290 ASP PHE ALA LEU GLY LYS ILE SER TYR ASP GLU PHE THR
SEQRES 22 B 290 SER GLU LEU MSE LYS ILE ASN ASN ASP LEU GLU HIS HIS
SEQRES 23 B 290 HIS HIS HIS HIS
SEQRES 1 C 290 MSE VAL LYS SER PHE LEU MSE LEU GLY GLN SER ASN MSE
SEQRES 2 C 290 ALA GLY ARG GLY PHE ILE ASN GLU VAL PRO MSE ILE TYR
SEQRES 3 C 290 ASN GLU ARG ILE GLN MSE LEU ARG ASN GLY ARG TRP GLN
SEQRES 4 C 290 MSE MSE THR GLU PRO ILE ASN TYR ASP ARG PRO VAL SER
SEQRES 5 C 290 GLY ILE SER LEU ALA GLY SER PHE ALA ASP ALA TRP SER
SEQRES 6 C 290 GLN LYS ASN GLN GLU ASP ILE ILE GLY LEU ILE PRO CYS
SEQRES 7 C 290 ALA GLU GLY GLY SER SER ILE ASP GLU TRP ALA LEU ASP
SEQRES 8 C 290 GLY VAL LEU PHE ARG HIS ALA LEU THR GLU ALA LYS PHE
SEQRES 9 C 290 ALA MSE GLU SER SER GLU LEU THR GLY ILE LEU TRP HIS
SEQRES 10 C 290 GLN GLY GLU SER ASP SER LEU ASN GLY ASN TYR LYS VAL
SEQRES 11 C 290 TYR TYR LYS LYS LEU LEU LEU ILE ILE GLU ALA LEU ARG
SEQRES 12 C 290 LYS GLU LEU ASN VAL PRO ASP ILE PRO ILE ILE ILE GLY
SEQRES 13 C 290 GLY LEU GLY ASP PHE LEU GLY LYS GLU ARG PHE GLY LYS
SEQRES 14 C 290 GLY CYS THR GLU TYR ASN PHE ILE ASN LYS GLU LEU GLN
SEQRES 15 C 290 LYS PHE ALA PHE GLU GLN ASP ASN CYS TYR PHE VAL THR
SEQRES 16 C 290 ALA SER GLY LEU THR CYS ASN PRO ASP GLY ILE HIS ILE
SEQRES 17 C 290 ASP ALA ILE SER GLN ARG LYS PHE GLY LEU ARG TYR PHE
SEQRES 18 C 290 GLU ALA PHE PHE ASN ARG LYS HIS VAL LEU GLU PRO LEU
SEQRES 19 C 290 ILE ASN GLU ASN GLU LEU LEU ASN LEU ASN TYR ALA ARG
SEQRES 20 C 290 THR HIS THR LYS ALA GLU LYS ILE TYR ILE LYS SER MSE
SEQRES 21 C 290 ASP PHE ALA LEU GLY LYS ILE SER TYR ASP GLU PHE THR
SEQRES 22 C 290 SER GLU LEU MSE LYS ILE ASN ASN ASP LEU GLU HIS HIS
SEQRES 23 C 290 HIS HIS HIS HIS
SEQRES 1 D 290 MSE VAL LYS SER PHE LEU MSE LEU GLY GLN SER ASN MSE
SEQRES 2 D 290 ALA GLY ARG GLY PHE ILE ASN GLU VAL PRO MSE ILE TYR
SEQRES 3 D 290 ASN GLU ARG ILE GLN MSE LEU ARG ASN GLY ARG TRP GLN
SEQRES 4 D 290 MSE MSE THR GLU PRO ILE ASN TYR ASP ARG PRO VAL SER
SEQRES 5 D 290 GLY ILE SER LEU ALA GLY SER PHE ALA ASP ALA TRP SER
SEQRES 6 D 290 GLN LYS ASN GLN GLU ASP ILE ILE GLY LEU ILE PRO CYS
SEQRES 7 D 290 ALA GLU GLY GLY SER SER ILE ASP GLU TRP ALA LEU ASP
SEQRES 8 D 290 GLY VAL LEU PHE ARG HIS ALA LEU THR GLU ALA LYS PHE
SEQRES 9 D 290 ALA MSE GLU SER SER GLU LEU THR GLY ILE LEU TRP HIS
SEQRES 10 D 290 GLN GLY GLU SER ASP SER LEU ASN GLY ASN TYR LYS VAL
SEQRES 11 D 290 TYR TYR LYS LYS LEU LEU LEU ILE ILE GLU ALA LEU ARG
SEQRES 12 D 290 LYS GLU LEU ASN VAL PRO ASP ILE PRO ILE ILE ILE GLY
SEQRES 13 D 290 GLY LEU GLY ASP PHE LEU GLY LYS GLU ARG PHE GLY LYS
SEQRES 14 D 290 GLY CYS THR GLU TYR ASN PHE ILE ASN LYS GLU LEU GLN
SEQRES 15 D 290 LYS PHE ALA PHE GLU GLN ASP ASN CYS TYR PHE VAL THR
SEQRES 16 D 290 ALA SER GLY LEU THR CYS ASN PRO ASP GLY ILE HIS ILE
SEQRES 17 D 290 ASP ALA ILE SER GLN ARG LYS PHE GLY LEU ARG TYR PHE
SEQRES 18 D 290 GLU ALA PHE PHE ASN ARG LYS HIS VAL LEU GLU PRO LEU
SEQRES 19 D 290 ILE ASN GLU ASN GLU LEU LEU ASN LEU ASN TYR ALA ARG
SEQRES 20 D 290 THR HIS THR LYS ALA GLU LYS ILE TYR ILE LYS SER MSE
SEQRES 21 D 290 ASP PHE ALA LEU GLY LYS ILE SER TYR ASP GLU PHE THR
SEQRES 22 D 290 SER GLU LEU MSE LYS ILE ASN ASN ASP LEU GLU HIS HIS
SEQRES 23 D 290 HIS HIS HIS HIS
SEQRES 1 E 290 MSE VAL LYS SER PHE LEU MSE LEU GLY GLN SER ASN MSE
SEQRES 2 E 290 ALA GLY ARG GLY PHE ILE ASN GLU VAL PRO MSE ILE TYR
SEQRES 3 E 290 ASN GLU ARG ILE GLN MSE LEU ARG ASN GLY ARG TRP GLN
SEQRES 4 E 290 MSE MSE THR GLU PRO ILE ASN TYR ASP ARG PRO VAL SER
SEQRES 5 E 290 GLY ILE SER LEU ALA GLY SER PHE ALA ASP ALA TRP SER
SEQRES 6 E 290 GLN LYS ASN GLN GLU ASP ILE ILE GLY LEU ILE PRO CYS
SEQRES 7 E 290 ALA GLU GLY GLY SER SER ILE ASP GLU TRP ALA LEU ASP
SEQRES 8 E 290 GLY VAL LEU PHE ARG HIS ALA LEU THR GLU ALA LYS PHE
SEQRES 9 E 290 ALA MSE GLU SER SER GLU LEU THR GLY ILE LEU TRP HIS
SEQRES 10 E 290 GLN GLY GLU SER ASP SER LEU ASN GLY ASN TYR LYS VAL
SEQRES 11 E 290 TYR TYR LYS LYS LEU LEU LEU ILE ILE GLU ALA LEU ARG
SEQRES 12 E 290 LYS GLU LEU ASN VAL PRO ASP ILE PRO ILE ILE ILE GLY
SEQRES 13 E 290 GLY LEU GLY ASP PHE LEU GLY LYS GLU ARG PHE GLY LYS
SEQRES 14 E 290 GLY CYS THR GLU TYR ASN PHE ILE ASN LYS GLU LEU GLN
SEQRES 15 E 290 LYS PHE ALA PHE GLU GLN ASP ASN CYS TYR PHE VAL THR
SEQRES 16 E 290 ALA SER GLY LEU THR CYS ASN PRO ASP GLY ILE HIS ILE
SEQRES 17 E 290 ASP ALA ILE SER GLN ARG LYS PHE GLY LEU ARG TYR PHE
SEQRES 18 E 290 GLU ALA PHE PHE ASN ARG LYS HIS VAL LEU GLU PRO LEU
SEQRES 19 E 290 ILE ASN GLU ASN GLU LEU LEU ASN LEU ASN TYR ALA ARG
SEQRES 20 E 290 THR HIS THR LYS ALA GLU LYS ILE TYR ILE LYS SER MSE
SEQRES 21 E 290 ASP PHE ALA LEU GLY LYS ILE SER TYR ASP GLU PHE THR
SEQRES 22 E 290 SER GLU LEU MSE LYS ILE ASN ASN ASP LEU GLU HIS HIS
SEQRES 23 E 290 HIS HIS HIS HIS
SEQRES 1 F 290 MSE VAL LYS SER PHE LEU MSE LEU GLY GLN SER ASN MSE
SEQRES 2 F 290 ALA GLY ARG GLY PHE ILE ASN GLU VAL PRO MSE ILE TYR
SEQRES 3 F 290 ASN GLU ARG ILE GLN MSE LEU ARG ASN GLY ARG TRP GLN
SEQRES 4 F 290 MSE MSE THR GLU PRO ILE ASN TYR ASP ARG PRO VAL SER
SEQRES 5 F 290 GLY ILE SER LEU ALA GLY SER PHE ALA ASP ALA TRP SER
SEQRES 6 F 290 GLN LYS ASN GLN GLU ASP ILE ILE GLY LEU ILE PRO CYS
SEQRES 7 F 290 ALA GLU GLY GLY SER SER ILE ASP GLU TRP ALA LEU ASP
SEQRES 8 F 290 GLY VAL LEU PHE ARG HIS ALA LEU THR GLU ALA LYS PHE
SEQRES 9 F 290 ALA MSE GLU SER SER GLU LEU THR GLY ILE LEU TRP HIS
SEQRES 10 F 290 GLN GLY GLU SER ASP SER LEU ASN GLY ASN TYR LYS VAL
SEQRES 11 F 290 TYR TYR LYS LYS LEU LEU LEU ILE ILE GLU ALA LEU ARG
SEQRES 12 F 290 LYS GLU LEU ASN VAL PRO ASP ILE PRO ILE ILE ILE GLY
SEQRES 13 F 290 GLY LEU GLY ASP PHE LEU GLY LYS GLU ARG PHE GLY LYS
SEQRES 14 F 290 GLY CYS THR GLU TYR ASN PHE ILE ASN LYS GLU LEU GLN
SEQRES 15 F 290 LYS PHE ALA PHE GLU GLN ASP ASN CYS TYR PHE VAL THR
SEQRES 16 F 290 ALA SER GLY LEU THR CYS ASN PRO ASP GLY ILE HIS ILE
SEQRES 17 F 290 ASP ALA ILE SER GLN ARG LYS PHE GLY LEU ARG TYR PHE
SEQRES 18 F 290 GLU ALA PHE PHE ASN ARG LYS HIS VAL LEU GLU PRO LEU
SEQRES 19 F 290 ILE ASN GLU ASN GLU LEU LEU ASN LEU ASN TYR ALA ARG
SEQRES 20 F 290 THR HIS THR LYS ALA GLU LYS ILE TYR ILE LYS SER MSE
SEQRES 21 F 290 ASP PHE ALA LEU GLY LYS ILE SER TYR ASP GLU PHE THR
SEQRES 22 F 290 SER GLU LEU MSE LYS ILE ASN ASN ASP LEU GLU HIS HIS
SEQRES 23 F 290 HIS HIS HIS HIS
MODRES 1ZMB MSE A 1 MET SELENOMETHIONINE
MODRES 1ZMB MSE A 7 MET SELENOMETHIONINE
MODRES 1ZMB MSE A 13 MET SELENOMETHIONINE
MODRES 1ZMB MSE A 24 MET SELENOMETHIONINE
MODRES 1ZMB MSE A 32 MET SELENOMETHIONINE
MODRES 1ZMB MSE A 40 MET SELENOMETHIONINE
MODRES 1ZMB MSE A 41 MET SELENOMETHIONINE
MODRES 1ZMB MSE A 106 MET SELENOMETHIONINE
MODRES 1ZMB MSE A 260 MET SELENOMETHIONINE
MODRES 1ZMB MSE A 277 MET SELENOMETHIONINE
MODRES 1ZMB MSE B 1 MET SELENOMETHIONINE
MODRES 1ZMB MSE B 7 MET SELENOMETHIONINE
MODRES 1ZMB MSE B 13 MET SELENOMETHIONINE
MODRES 1ZMB MSE B 24 MET SELENOMETHIONINE
MODRES 1ZMB MSE B 32 MET SELENOMETHIONINE
MODRES 1ZMB MSE B 40 MET SELENOMETHIONINE
MODRES 1ZMB MSE B 41 MET SELENOMETHIONINE
MODRES 1ZMB MSE B 106 MET SELENOMETHIONINE
MODRES 1ZMB MSE B 260 MET SELENOMETHIONINE
MODRES 1ZMB MSE B 277 MET SELENOMETHIONINE
MODRES 1ZMB MSE C 1 MET SELENOMETHIONINE
MODRES 1ZMB MSE C 7 MET SELENOMETHIONINE
MODRES 1ZMB MSE C 13 MET SELENOMETHIONINE
MODRES 1ZMB MSE C 24 MET SELENOMETHIONINE
MODRES 1ZMB MSE C 32 MET SELENOMETHIONINE
MODRES 1ZMB MSE C 40 MET SELENOMETHIONINE
MODRES 1ZMB MSE C 41 MET SELENOMETHIONINE
MODRES 1ZMB MSE C 106 MET SELENOMETHIONINE
MODRES 1ZMB MSE C 260 MET SELENOMETHIONINE
MODRES 1ZMB MSE C 277 MET SELENOMETHIONINE
MODRES 1ZMB MSE D 1 MET SELENOMETHIONINE
MODRES 1ZMB MSE D 7 MET SELENOMETHIONINE
MODRES 1ZMB MSE D 13 MET SELENOMETHIONINE
MODRES 1ZMB MSE D 24 MET SELENOMETHIONINE
MODRES 1ZMB MSE D 32 MET SELENOMETHIONINE
MODRES 1ZMB MSE D 40 MET SELENOMETHIONINE
MODRES 1ZMB MSE D 41 MET SELENOMETHIONINE
MODRES 1ZMB MSE D 106 MET SELENOMETHIONINE
MODRES 1ZMB MSE D 260 MET SELENOMETHIONINE
MODRES 1ZMB MSE D 277 MET SELENOMETHIONINE
MODRES 1ZMB MSE E 1 MET SELENOMETHIONINE
MODRES 1ZMB MSE E 7 MET SELENOMETHIONINE
MODRES 1ZMB MSE E 13 MET SELENOMETHIONINE
MODRES 1ZMB MSE E 24 MET SELENOMETHIONINE
MODRES 1ZMB MSE E 32 MET SELENOMETHIONINE
MODRES 1ZMB MSE E 40 MET SELENOMETHIONINE
MODRES 1ZMB MSE E 41 MET SELENOMETHIONINE
MODRES 1ZMB MSE E 106 MET SELENOMETHIONINE
MODRES 1ZMB MSE E 260 MET SELENOMETHIONINE
MODRES 1ZMB MSE E 277 MET SELENOMETHIONINE
MODRES 1ZMB MSE F 1 MET SELENOMETHIONINE
MODRES 1ZMB MSE F 7 MET SELENOMETHIONINE
MODRES 1ZMB MSE F 13 MET SELENOMETHIONINE
MODRES 1ZMB MSE F 24 MET SELENOMETHIONINE
MODRES 1ZMB MSE F 32 MET SELENOMETHIONINE
MODRES 1ZMB MSE F 40 MET SELENOMETHIONINE
MODRES 1ZMB MSE F 41 MET SELENOMETHIONINE
MODRES 1ZMB MSE F 106 MET SELENOMETHIONINE
MODRES 1ZMB MSE F 260 MET SELENOMETHIONINE
MODRES 1ZMB MSE F 277 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 7 8
HET MSE A 13 8
HET MSE A 24 8
HET MSE A 32 8
HET MSE A 40 8
HET MSE A 41 8
HET MSE A 106 8
HET MSE A 260 8
HET MSE A 277 8
HET MSE B 1 8
HET MSE B 7 8
HET MSE B 13 8
HET MSE B 24 8
HET MSE B 32 8
HET MSE B 40 8
HET MSE B 41 8
HET MSE B 106 8
HET MSE B 260 8
HET MSE B 277 8
HET MSE C 1 8
HET MSE C 7 8
HET MSE C 13 8
HET MSE C 24 8
HET MSE C 32 8
HET MSE C 40 8
HET MSE C 41 8
HET MSE C 106 8
HET MSE C 260 8
HET MSE C 277 8
HET MSE D 1 8
HET MSE D 7 8
HET MSE D 13 8
HET MSE D 24 8
HET MSE D 32 8
HET MSE D 40 8
HET MSE D 41 8
HET MSE D 106 8
HET MSE D 260 8
HET MSE D 277 8
HET MSE E 1 8
HET MSE E 7 8
HET MSE E 13 8
HET MSE E 24 8
HET MSE E 32 8
HET MSE E 40 8
HET MSE E 41 8
HET MSE E 106 8
HET MSE E 260 8
HET MSE E 277 8
HET MSE F 1 8
HET MSE F 7 8
HET MSE F 13 8
HET MSE F 24 8
HET MSE F 32 8
HET MSE F 40 8
HET MSE F 41 8
HET MSE F 106 8
HET MSE F 260 8
HET MSE F 277 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 60(C5 H11 N O2 SE)
FORMUL 7 HOH *123(H2 O)
HELIX 1 1 GLN A 10 GLY A 15 1 6
HELIX 2 2 LEU A 56 LYS A 67 1 12
HELIX 3 3 SER A 84 ALA A 89 5 6
HELIX 4 4 GLY A 92 GLU A 107 1 16
HELIX 5 5 GLY A 119 SER A 123 5 5
HELIX 6 6 VAL A 130 LEU A 146 1 17
HELIX 7 7 GLU A 165 LYS A 169 5 5
HELIX 8 8 GLU A 173 GLN A 188 1 16
HELIX 9 9 ASP A 209 ARG A 227 1 19
HELIX 10 10 ASN A 236 ARG A 247 1 12
HELIX 11 11 THR A 250 LEU A 264 1 15
HELIX 12 12 SER A 268 ASP A 282 1 15
HELIX 13 13 GLN B 10 GLY B 15 1 6
HELIX 14 14 LEU B 56 LYS B 67 1 12
HELIX 15 15 SER B 84 ALA B 89 5 6
HELIX 16 16 GLY B 92 GLU B 107 1 16
HELIX 17 17 GLY B 119 SER B 123 5 5
HELIX 18 18 VAL B 130 LEU B 146 1 17
HELIX 19 19 GLU B 165 LYS B 169 5 5
HELIX 20 20 GLU B 173 GLN B 188 1 16
HELIX 21 21 ASP B 209 ARG B 227 1 19
HELIX 22 22 ASN B 236 ARG B 247 1 12
HELIX 23 23 THR B 250 LEU B 264 1 15
HELIX 24 24 SER B 268 ASP B 282 1 15
HELIX 25 25 GLN C 10 GLY C 15 1 6
HELIX 26 26 PHE C 18 VAL C 22 5 5
HELIX 27 27 LEU C 56 LYS C 67 1 12
HELIX 28 28 SER C 84 ALA C 89 5 6
HELIX 29 29 GLY C 92 GLU C 107 1 16
HELIX 30 30 GLY C 119 SER C 123 5 5
HELIX 31 31 VAL C 130 LEU C 146 1 17
HELIX 32 32 GLU C 165 LYS C 169 5 5
HELIX 33 33 GLU C 173 GLN C 188 1 16
HELIX 34 34 ASP C 209 ARG C 227 1 19
HELIX 35 35 ASN C 236 ARG C 247 1 12
HELIX 36 36 THR C 250 LEU C 264 1 15
HELIX 37 37 SER C 268 ASP C 282 1 15
HELIX 38 38 GLN D 10 GLY D 15 1 6
HELIX 39 39 LEU D 56 LYS D 67 1 12
HELIX 40 40 SER D 84 ALA D 89 5 6
HELIX 41 41 GLY D 92 GLU D 107 1 16
HELIX 42 42 GLY D 119 SER D 123 5 5
HELIX 43 43 VAL D 130 LEU D 146 1 17
HELIX 44 44 GLU D 165 LYS D 169 5 5
HELIX 45 45 GLU D 173 GLN D 188 1 16
HELIX 46 46 ASP D 209 ARG D 227 1 19
HELIX 47 47 ASN D 236 ARG D 247 1 12
HELIX 48 48 THR D 250 LEU D 264 1 15
HELIX 49 49 SER D 268 ASP D 282 1 15
HELIX 50 50 GLN E 10 GLY E 15 1 6
HELIX 51 51 LEU E 56 LYS E 67 1 12
HELIX 52 52 SER E 84 ALA E 89 5 6
HELIX 53 53 GLY E 92 GLU E 107 1 16
HELIX 54 54 GLY E 119 SER E 123 5 5
HELIX 55 55 VAL E 130 LEU E 146 1 17
HELIX 56 56 GLU E 165 LYS E 169 5 5
HELIX 57 57 GLU E 173 GLN E 188 1 16
HELIX 58 58 ASP E 209 ARG E 227 1 19
HELIX 59 59 ASN E 236 ARG E 247 1 12
HELIX 60 60 THR E 250 LEU E 264 1 15
HELIX 61 61 SER E 268 ASP E 282 1 15
HELIX 62 62 GLN F 10 GLY F 15 1 6
HELIX 63 63 PHE F 18 VAL F 22 5 5
HELIX 64 64 LEU F 56 LYS F 67 1 12
HELIX 65 65 SER F 84 ALA F 89 5 6
HELIX 66 66 GLY F 92 GLU F 107 1 16
HELIX 67 67 GLY F 119 SER F 123 5 5
HELIX 68 68 VAL F 130 LEU F 146 1 17
HELIX 69 69 GLU F 165 LYS F 169 5 5
HELIX 70 70 GLU F 173 GLN F 188 1 16
HELIX 71 71 ASP F 209 ARG F 227 1 19
HELIX 72 72 ASN F 236 ARG F 247 1 12
HELIX 73 73 THR F 250 LEU F 264 1 15
HELIX 74 74 SER F 268 ASP F 282 1 15
SHEET 1 A 7 ARG A 37 MSE A 40 0
SHEET 2 A 7 ILE A 30 ARG A 34 -1 N MSE A 32 O GLN A 39
SHEET 3 A 7 ILE A 72 PRO A 77 1 O ILE A 73 N GLN A 31
SHEET 4 A 7 VAL A 2 GLY A 9 1 N MSE A 7 O ILE A 76
SHEET 5 A 7 GLU A 110 HIS A 117 1 O LEU A 115 N LEU A 8
SHEET 6 A 7 ILE A 153 GLY A 156 1 O ILE A 154 N TRP A 116
SHEET 7 A 7 CYS A 191 VAL A 194 1 O TYR A 192 N ILE A 155
SHEET 1 B 7 ARG B 37 MSE B 40 0
SHEET 2 B 7 ILE B 30 ARG B 34 -1 N ARG B 34 O ARG B 37
SHEET 3 B 7 ILE B 72 PRO B 77 1 O LEU B 75 N GLN B 31
SHEET 4 B 7 VAL B 2 GLY B 9 1 N LYS B 3 O GLY B 74
SHEET 5 B 7 GLU B 110 HIS B 117 1 O LEU B 115 N LEU B 8
SHEET 6 B 7 ILE B 153 GLY B 156 1 O ILE B 154 N TRP B 116
SHEET 7 B 7 CYS B 191 VAL B 194 1 O TYR B 192 N ILE B 155
SHEET 1 C 7 ARG C 37 MSE C 40 0
SHEET 2 C 7 ILE C 30 ARG C 34 -1 N ARG C 34 O ARG C 37
SHEET 3 C 7 ILE C 72 PRO C 77 1 O LEU C 75 N GLN C 31
SHEET 4 C 7 VAL C 2 GLY C 9 1 N LYS C 3 O GLY C 74
SHEET 5 C 7 GLU C 110 HIS C 117 1 O LEU C 115 N LEU C 8
SHEET 6 C 7 ILE C 153 GLY C 156 1 O ILE C 154 N TRP C 116
SHEET 7 C 7 CYS C 191 VAL C 194 1 O TYR C 192 N ILE C 155
SHEET 1 D 7 ARG D 37 MSE D 40 0
SHEET 2 D 7 ILE D 30 ARG D 34 -1 N ARG D 34 O ARG D 37
SHEET 3 D 7 ILE D 72 PRO D 77 1 O LEU D 75 N GLN D 31
SHEET 4 D 7 VAL D 2 GLY D 9 1 N MSE D 7 O ILE D 76
SHEET 5 D 7 GLU D 110 HIS D 117 1 O LEU D 115 N LEU D 8
SHEET 6 D 7 ILE D 153 GLY D 156 1 O ILE D 154 N TRP D 116
SHEET 7 D 7 CYS D 191 VAL D 194 1 O TYR D 192 N ILE D 155
SHEET 1 E 7 ARG E 37 MSE E 40 0
SHEET 2 E 7 ILE E 30 ARG E 34 -1 N ARG E 34 O ARG E 37
SHEET 3 E 7 ILE E 72 PRO E 77 1 O LEU E 75 N GLN E 31
SHEET 4 E 7 VAL E 2 GLY E 9 1 N MSE E 7 O ILE E 76
SHEET 5 E 7 GLU E 110 HIS E 117 1 O LEU E 115 N LEU E 8
SHEET 6 E 7 ILE E 153 GLY E 156 1 O ILE E 154 N TRP E 116
SHEET 7 E 7 CYS E 191 VAL E 194 1 O TYR E 192 N ILE E 155
SHEET 1 F 7 ARG F 37 MSE F 40 0
SHEET 2 F 7 ILE F 30 ARG F 34 -1 N ARG F 34 O ARG F 37
SHEET 3 F 7 ILE F 72 PRO F 77 1 O LEU F 75 N GLN F 31
SHEET 4 F 7 VAL F 2 GLY F 9 1 N LYS F 3 O GLY F 74
SHEET 5 F 7 GLU F 110 HIS F 117 1 O LEU F 115 N LEU F 8
SHEET 6 F 7 ILE F 153 GLY F 156 1 O ILE F 154 N TRP F 116
SHEET 7 F 7 CYS F 191 VAL F 194 1 O TYR F 192 N ILE F 155
LINK C MSE A 1 N VAL A 2 1555 1555 1.33
LINK C LEU A 6 N MSE A 7 1555 1555 1.33
LINK C MSE A 7 N LEU A 8 1555 1555 1.33
LINK C ASN A 12 N MSE A 13 1555 1555 1.33
LINK C MSE A 13 N ALA A 14 1555 1555 1.33
LINK C PRO A 23 N MSE A 24 1555 1555 1.33
LINK C MSE A 24 N ILE A 25 1555 1555 1.33
LINK C GLN A 31 N MSE A 32 1555 1555 1.33
LINK C MSE A 32 N LEU A 33 1555 1555 1.33
LINK C GLN A 39 N MSE A 40 1555 1555 1.33
LINK C MSE A 40 N MSE A 41 1555 1555 1.33
LINK C MSE A 41 N THR A 42 1555 1555 1.33
LINK C ALA A 105 N MSE A 106 1555 1555 1.33
LINK C MSE A 106 N GLU A 107 1555 1555 1.32
LINK C SER A 259 N MSE A 260 1555 1555 1.32
LINK C MSE A 260 N ASP A 261 1555 1555 1.33
LINK C LEU A 276 N MSE A 277 1555 1555 1.33
LINK C MSE A 277 N LYS A 278 1555 1555 1.34
LINK C MSE B 1 N VAL B 2 1555 1555 1.33
LINK C LEU B 6 N MSE B 7 1555 1555 1.33
LINK C MSE B 7 N LEU B 8 1555 1555 1.33
LINK C ASN B 12 N MSE B 13 1555 1555 1.33
LINK C MSE B 13 N ALA B 14 1555 1555 1.34
LINK C PRO B 23 N MSE B 24 1555 1555 1.33
LINK C MSE B 24 N ILE B 25 1555 1555 1.33
LINK C GLN B 31 N MSE B 32 1555 1555 1.33
LINK C MSE B 32 N LEU B 33 1555 1555 1.32
LINK C GLN B 39 N MSE B 40 1555 1555 1.32
LINK C MSE B 40 N MSE B 41 1555 1555 1.33
LINK C MSE B 41 N THR B 42 1555 1555 1.33
LINK C ALA B 105 N MSE B 106 1555 1555 1.33
LINK C MSE B 106 N GLU B 107 1555 1555 1.32
LINK C SER B 259 N MSE B 260 1555 1555 1.32
LINK C MSE B 260 N ASP B 261 1555 1555 1.33
LINK C LEU B 276 N MSE B 277 1555 1555 1.33
LINK C MSE B 277 N LYS B 278 1555 1555 1.33
LINK C MSE C 1 N VAL C 2 1555 1555 1.33
LINK C LEU C 6 N MSE C 7 1555 1555 1.33
LINK C MSE C 7 N LEU C 8 1555 1555 1.33
LINK C ASN C 12 N MSE C 13 1555 1555 1.33
LINK C MSE C 13 N ALA C 14 1555 1555 1.33
LINK C PRO C 23 N MSE C 24 1555 1555 1.33
LINK C MSE C 24 N ILE C 25 1555 1555 1.33
LINK C GLN C 31 N MSE C 32 1555 1555 1.33
LINK C MSE C 32 N LEU C 33 1555 1555 1.33
LINK C GLN C 39 N MSE C 40 1555 1555 1.32
LINK C MSE C 40 N MSE C 41 1555 1555 1.33
LINK C MSE C 41 N THR C 42 1555 1555 1.33
LINK C ALA C 105 N MSE C 106 1555 1555 1.33
LINK C MSE C 106 N GLU C 107 1555 1555 1.32
LINK C SER C 259 N MSE C 260 1555 1555 1.32
LINK C MSE C 260 N ASP C 261 1555 1555 1.33
LINK C LEU C 276 N MSE C 277 1555 1555 1.33
LINK C MSE C 277 N LYS C 278 1555 1555 1.33
LINK C MSE D 1 N VAL D 2 1555 1555 1.33
LINK C LEU D 6 N MSE D 7 1555 1555 1.34
LINK C MSE D 7 N LEU D 8 1555 1555 1.33
LINK C ASN D 12 N MSE D 13 1555 1555 1.33
LINK C MSE D 13 N ALA D 14 1555 1555 1.33
LINK C PRO D 23 N MSE D 24 1555 1555 1.33
LINK C MSE D 24 N ILE D 25 1555 1555 1.33
LINK C GLN D 31 N MSE D 32 1555 1555 1.33
LINK C MSE D 32 N LEU D 33 1555 1555 1.32
LINK C GLN D 39 N MSE D 40 1555 1555 1.33
LINK C MSE D 40 N MSE D 41 1555 1555 1.33
LINK C MSE D 41 N THR D 42 1555 1555 1.33
LINK C ALA D 105 N MSE D 106 1555 1555 1.33
LINK C MSE D 106 N GLU D 107 1555 1555 1.32
LINK C SER D 259 N MSE D 260 1555 1555 1.32
LINK C MSE D 260 N ASP D 261 1555 1555 1.33
LINK C LEU D 276 N MSE D 277 1555 1555 1.33
LINK C MSE D 277 N LYS D 278 1555 1555 1.33
LINK C MSE E 1 N VAL E 2 1555 1555 1.33
LINK C LEU E 6 N MSE E 7 1555 1555 1.34
LINK C MSE E 7 N LEU E 8 1555 1555 1.33
LINK C ASN E 12 N MSE E 13 1555 1555 1.33
LINK C MSE E 13 N ALA E 14 1555 1555 1.33
LINK C PRO E 23 N MSE E 24 1555 1555 1.33
LINK C MSE E 24 N ILE E 25 1555 1555 1.33
LINK C GLN E 31 N MSE E 32 1555 1555 1.33
LINK C MSE E 32 N LEU E 33 1555 1555 1.33
LINK C GLN E 39 N MSE E 40 1555 1555 1.33
LINK C MSE E 40 N MSE E 41 1555 1555 1.33
LINK C MSE E 41 N THR E 42 1555 1555 1.33
LINK C ALA E 105 N MSE E 106 1555 1555 1.33
LINK C MSE E 106 N GLU E 107 1555 1555 1.32
LINK C SER E 259 N MSE E 260 1555 1555 1.32
LINK C MSE E 260 N ASP E 261 1555 1555 1.33
LINK C LEU E 276 N MSE E 277 1555 1555 1.33
LINK C MSE E 277 N LYS E 278 1555 1555 1.34
LINK C MSE F 1 N VAL F 2 1555 1555 1.33
LINK C LEU F 6 N MSE F 7 1555 1555 1.33
LINK C MSE F 7 N LEU F 8 1555 1555 1.33
LINK C ASN F 12 N MSE F 13 1555 1555 1.33
LINK C MSE F 13 N ALA F 14 1555 1555 1.34
LINK C PRO F 23 N MSE F 24 1555 1555 1.33
LINK C MSE F 24 N ILE F 25 1555 1555 1.33
LINK C GLN F 31 N MSE F 32 1555 1555 1.33
LINK C MSE F 32 N LEU F 33 1555 1555 1.33
LINK C GLN F 39 N MSE F 40 1555 1555 1.33
LINK C MSE F 40 N MSE F 41 1555 1555 1.33
LINK C MSE F 41 N THR F 42 1555 1555 1.33
LINK C ALA F 105 N MSE F 106 1555 1555 1.33
LINK C MSE F 106 N GLU F 107 1555 1555 1.33
LINK C SER F 259 N MSE F 260 1555 1555 1.32
LINK C MSE F 260 N ASP F 261 1555 1555 1.33
LINK C LEU F 276 N MSE F 277 1555 1555 1.33
LINK C MSE F 277 N LYS F 278 1555 1555 1.34
CISPEP 1 GLU A 43 PRO A 44 0 -0.22
CISPEP 2 GLU B 43 PRO B 44 0 -0.83
CISPEP 3 GLU C 43 PRO C 44 0 -1.82
CISPEP 4 GLU D 43 PRO D 44 0 -0.61
CISPEP 5 GLU E 43 PRO E 44 0 -1.84
CISPEP 6 GLU F 43 PRO F 44 0 0.38
CRYST1 70.999 87.936 103.510 106.50 100.22 113.80 P 1 6
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 0.014085 0.006213 0.005438 0.00000
SCALE2 0.000000 0.012429 0.005346 0.00000
SCALE3 0.000000 0.000000 0.010686 0.00000
HETATM 1 N MSE A 1 36.358 -26.713 43.446 1.00 60.87 N
HETATM 2 CA MSE A 1 36.788 -26.209 44.782 1.00 60.52 C
HETATM 3 C MSE A 1 35.746 -25.243 45.347 1.00 55.61 C
HETATM 4 O MSE A 1 34.603 -25.185 44.874 1.00 55.50 O
HETATM 5 CB MSE A 1 38.156 -25.500 44.688 1.00 68.32 C
HETATM 6 CG MSE A 1 38.161 -24.177 43.889 1.00 78.54 C
HETATM 7 SE MSE A 1 39.811 -23.059 43.986 1.00 94.81 SE
HETATM 8 CE MSE A 1 40.708 -23.593 42.310 1.00 89.76 C
(ATOM LINES ARE NOT SHOWN.)
END