| content |
HEADER BIOSYNTHETIC PROTEIN 12-FEB-22 7WWF
TITLE CRYSTAL STRUCTURE OF BIOH3 FROM MYCOLICIBACTERIUM SMEGMATIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOLICIBACTERIUM SMEGMATIS MC2 155;
SOURCE 3 ORGANISM_TAXID: 246196;
SOURCE 4 GENE: NCTC7017_02293;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS MYCOLICIBACTERIUM SMEGMATIS, BIOH3, CRYSTAL, BIOSYNTHETIC PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.YANG,Y.C.XU,J.H.GAN,Y.J.FENG
REVDAT 1 06-JUL-22 7WWF 0
JRNL AUTH J.YANG,Y.C.XU,Y.J.FENG,J.H.GAN
JRNL TITL CRYSTAL STRUCTURE OF BIOH3 FROM MYCOLICIBACTERIUM SMEGMATIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.27 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.19.1_4122
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.27
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.63
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 93298
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.810
REMARK 3 FREE R VALUE TEST SET COUNT : 4490
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 45.6300 - 7.0500 0.96 3053 154 0.1410 0.1795
REMARK 3 2 7.0400 - 5.6000 0.98 3013 153 0.1628 0.1806
REMARK 3 3 5.6000 - 4.8900 0.99 3014 154 0.1473 0.1630
REMARK 3 4 4.8900 - 4.4400 0.98 2976 165 0.1382 0.1505
REMARK 3 5 4.4400 - 4.1200 0.99 2993 152 0.1328 0.1437
REMARK 3 6 4.1200 - 3.8800 0.99 2978 148 0.1535 0.1741
REMARK 3 7 3.8800 - 3.6900 0.99 3016 140 0.1670 0.2071
REMARK 3 8 3.6900 - 3.5300 0.99 2998 146 0.1899 0.2330
REMARK 3 9 3.5300 - 3.3900 0.99 3008 144 0.1930 0.2502
REMARK 3 10 3.3900 - 3.2700 0.99 2969 160 0.2097 0.2551
REMARK 3 11 3.2700 - 3.1700 0.99 3032 133 0.2200 0.2575
REMARK 3 12 3.1700 - 3.0800 1.00 2983 156 0.2302 0.2832
REMARK 3 13 3.0800 - 3.0000 1.00 3010 148 0.2240 0.2597
REMARK 3 14 3.0000 - 2.9300 1.00 3016 139 0.2310 0.2423
REMARK 3 15 2.9300 - 2.8600 1.00 2961 147 0.2225 0.2626
REMARK 3 16 2.8600 - 2.8000 1.00 2999 157 0.2188 0.2411
REMARK 3 17 2.8000 - 2.7400 1.00 2963 162 0.2234 0.2806
REMARK 3 18 2.7400 - 2.6900 1.00 3026 151 0.2326 0.2830
REMARK 3 19 2.6900 - 2.6400 0.68 1993 110 0.2460 0.2929
REMARK 3 20 2.6400 - 2.6000 1.00 3050 139 0.2497 0.3095
REMARK 3 21 2.6000 - 2.5600 1.00 2980 136 0.2407 0.2784
REMARK 3 22 2.5600 - 2.5200 1.00 2982 160 0.2448 0.2811
REMARK 3 23 2.5200 - 2.4800 1.00 2982 154 0.2346 0.2871
REMARK 3 24 2.4800 - 2.4500 1.00 2973 152 0.2374 0.3048
REMARK 3 25 2.4500 - 2.4100 1.00 2958 169 0.2428 0.2923
REMARK 3 26 2.4100 - 2.3800 1.00 3008 161 0.2536 0.2949
REMARK 3 27 2.3800 - 2.3500 1.00 2928 143 0.2499 0.2765
REMARK 3 28 2.3500 - 2.3200 1.00 3033 151 0.2646 0.3414
REMARK 3 29 2.3200 - 2.3000 1.00 2953 148 0.2710 0.2690
REMARK 3 30 2.3000 - 2.2700 1.00 2960 158 0.2746 0.3240
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.270
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.400
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 38.42
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.77
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 75.0405 -13.4704 135.5625
REMARK 3 T TENSOR
REMARK 3 T11: 0.2772 T22: 0.2497
REMARK 3 T33: 0.2256 T12: -0.0453
REMARK 3 T13: 0.0178 T23: 0.0288
REMARK 3 L TENSOR
REMARK 3 L11: 0.1165 L22: 0.1381
REMARK 3 L33: 0.1981 L12: -0.0180
REMARK 3 L13: 0.0003 L23: 0.0136
REMARK 3 S TENSOR
REMARK 3 S11: -0.0364 S12: 0.0085 S13: -0.0331
REMARK 3 S21: 0.0107 S22: -0.0083 S23: 0.0100
REMARK 3 S31: 0.0291 S32: 0.0160 S33: 0.0441
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 7WWF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-FEB-22.
REMARK 100 THE DEPOSITION ID IS D_1300027641.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-SEP-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.7-8.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.4
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 93409
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.270
REMARK 200 RESOLUTION RANGE LOW (A) : 90.830
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.08500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.27
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.39
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.57300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: AUTOSOL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: THE ENTRY CONTAINS FRIEDEL PAIRS IN I/F_PLUS/MINUS
REMARK 200 COLUMNS.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, CITRIC ACID, PH 8.8, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 32.91500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 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: 4230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 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: 4470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19270 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 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: 4110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 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 MSE A 1
REMARK 465 ASN A 2
REMARK 465 ASP A 3
REMARK 465 SER A 4
REMARK 465 ARG A 5
REMARK 465 MSE B 1
REMARK 465 ASN B 2
REMARK 465 ASP B 3
REMARK 465 SER B 4
REMARK 465 ARG B 5
REMARK 465 ASN B 6
REMARK 465 SER B 7
REMARK 465 MSE C 1
REMARK 465 ASN C 2
REMARK 465 ASP C 3
REMARK 465 SER C 4
REMARK 465 ARG C 5
REMARK 465 MSE D 1
REMARK 465 ASN D 2
REMARK 465 ASP D 3
REMARK 465 SER D 4
REMARK 465 ARG D 5
REMARK 465 ASN D 6
REMARK 465 SER D 7
REMARK 465 MSE E 1
REMARK 465 ASN E 2
REMARK 465 ASP E 3
REMARK 465 SER E 4
REMARK 465 ARG E 5
REMARK 465 ASN E 6
REMARK 465 SER E 7
REMARK 465 MSE F 1
REMARK 465 ASN F 2
REMARK 465 ASP F 3
REMARK 465 SER F 4
REMARK 465 ARG F 5
REMARK 465 ASN F 6
REMARK 465 SER F 7
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 ASN A 6 CG OD1 ND2
REMARK 470 PRO B 189 CG CD
REMARK 470 ASP B 190 CG OD1 OD2
REMARK 470 ASP B 277 CG OD1 OD2
REMARK 470 SER C 7 OG
REMARK 470 ASP C 157 CG OD1 OD2
REMARK 470 ASP C 190 CG OD1 OD2
REMARK 470 ASP D 49 CG OD1 OD2
REMARK 470 ASP D 277 CG OD1 OD2
REMARK 470 ASP E 148 CG OD1 OD2
REMARK 470 ASP E 190 CG OD1 OD2
REMARK 470 ASP E 277 CG OD1 OD2
REMARK 470 GLU F 193 CG CD OE1 OE2
REMARK 470 ASP F 277 CG OD1 OD2
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 TRP A 18 -1.52 66.91
REMARK 500 HIS A 19 -169.70 -100.84
REMARK 500 SER A 103 -125.77 55.44
REMARK 500 ASP A 157 66.72 60.82
REMARK 500 ARG A 218 -76.96 -113.79
REMARK 500 SER B 103 -127.55 58.59
REMARK 500 ARG B 218 -82.72 -114.21
REMARK 500 TRP C 18 -0.55 66.39
REMARK 500 SER C 103 -126.58 55.67
REMARK 500 ARG C 218 -76.39 -112.93
REMARK 500 SER D 103 -129.05 58.18
REMARK 500 ASP D 157 62.35 60.30
REMARK 500 ARG D 218 -79.40 -112.67
REMARK 500 ASP D 264 -168.54 -80.00
REMARK 500 SER E 103 -126.45 56.86
REMARK 500 ASP E 157 71.19 53.70
REMARK 500 ASP E 190 66.93 -104.27
REMARK 500 ARG E 218 -76.20 -119.25
REMARK 500 ASP E 264 -165.94 -78.85
REMARK 500 HIS F 19 -169.38 -108.15
REMARK 500 SER F 103 -127.13 54.83
REMARK 500 ASP F 157 70.27 62.70
REMARK 500 ARG F 218 -77.61 -116.09
REMARK 500 ASP F 264 -168.79 -79.40
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 PEG B 301
REMARK 610 PEG C 301
REMARK 610 PEG D 301
REMARK 610 PEG E 301
REMARK 610 PEG F 301
DBREF1 7WWF A 1 282 UNP A0A8B4QLS5_MYCSM
DBREF2 7WWF A A0A8B4QLS5 1 282
DBREF1 7WWF B 1 282 UNP A0A8B4QLS5_MYCSM
DBREF2 7WWF B A0A8B4QLS5 1 282
DBREF1 7WWF C 1 282 UNP A0A8B4QLS5_MYCSM
DBREF2 7WWF C A0A8B4QLS5 1 282
DBREF1 7WWF D 1 282 UNP A0A8B4QLS5_MYCSM
DBREF2 7WWF D A0A8B4QLS5 1 282
DBREF1 7WWF E 1 282 UNP A0A8B4QLS5_MYCSM
DBREF2 7WWF E A0A8B4QLS5 1 282
DBREF1 7WWF F 1 282 UNP A0A8B4QLS5_MYCSM
DBREF2 7WWF F A0A8B4QLS5 1 282
SEQRES 1 A 282 MSE ASN ASP SER ARG ASN SER GLY THR LEU ALA VAL LEU
SEQRES 2 A 282 VAL HIS GLY ALA TRP HIS SER SER LEU HIS TRP ALA ALA
SEQRES 3 A 282 ALA GLN ARG GLY LEU ALA ARG ARG GLY VAL ALA SER ILE
SEQRES 4 A 282 ALA VAL ASP LEU PRO GLY HIS GLY LEU ASP ALA PRO VAL
SEQRES 5 A 282 PRO SER GLY TYR LEU THR ALA GLY GLN PRO GLY LEU GLU
SEQRES 6 A 282 THR GLU LYS SER ALA LEU ALA ASP ILE THR MSE ASP ASP
SEQRES 7 A 282 LEU ALA ASP ALA VAL VAL ASP ALA LEU ALA GLU VAL ARG
SEQRES 8 A 282 SER ARG PHE ALA ARG VAL LEU LEU VAL ALA HIS SER ALA
SEQRES 9 A 282 GLY GLY GLY PRO ALA SER LEU ALA ALA GLU LYS ALA PRO
SEQRES 10 A 282 GLU LEU VAL ASP HIS LEU VAL TYR LEU ALA ALA PHE VAL
SEQRES 11 A 282 PRO ALA ALA ARG PRO ARG PHE THR ASP TYR ILE ASN ALA
SEQRES 12 A 282 PRO GLU ASN ALA ASP VAL VAL ALA LEU PRO ILE PHE SER
SEQRES 13 A 282 ASP PRO ALA ASN LEU GLY ALA HIS ARG LEU ASN PRO LEU
SEQRES 14 A 282 SER SER ASP ALA ILE GLU VAL ASP ALA ILE ARG ARG ALA
SEQRES 15 A 282 PHE LEU THR ASP MSE PRO PRO ASP ALA PRO GLU GLY TRP
SEQRES 16 A 282 ARG HIS LEU LEU HIS PRO ASP GLU PRO TYR ALA SER LEU
SEQRES 17 A 282 SER ALA PRO VAL PRO VAL THR PRO ARG ARG TRP GLY ARG
SEQRES 18 A 282 ILE PRO ARG THR TYR ILE ARG LEU ASP GLY ASP ARG ALA
SEQRES 19 A 282 LEU ALA PRO THR THR GLN ASN LEU MSE ILE ALA GLU ALA
SEQRES 20 A 282 ASP ARG LEU THR PRO ASP ASN PRO PHE GLY VAL ARG SER
SEQRES 21 A 282 LEU PRO GLY ASP HIS SER PRO MSE VAL HIS ARG PRO GLY
SEQRES 22 A 282 GLU LEU ALA ASP LEU LEU ALA GLY ILE
SEQRES 1 B 282 MSE ASN ASP SER ARG ASN SER GLY THR LEU ALA VAL LEU
SEQRES 2 B 282 VAL HIS GLY ALA TRP HIS SER SER LEU HIS TRP ALA ALA
SEQRES 3 B 282 ALA GLN ARG GLY LEU ALA ARG ARG GLY VAL ALA SER ILE
SEQRES 4 B 282 ALA VAL ASP LEU PRO GLY HIS GLY LEU ASP ALA PRO VAL
SEQRES 5 B 282 PRO SER GLY TYR LEU THR ALA GLY GLN PRO GLY LEU GLU
SEQRES 6 B 282 THR GLU LYS SER ALA LEU ALA ASP ILE THR MSE ASP ASP
SEQRES 7 B 282 LEU ALA ASP ALA VAL VAL ASP ALA LEU ALA GLU VAL ARG
SEQRES 8 B 282 SER ARG PHE ALA ARG VAL LEU LEU VAL ALA HIS SER ALA
SEQRES 9 B 282 GLY GLY GLY PRO ALA SER LEU ALA ALA GLU LYS ALA PRO
SEQRES 10 B 282 GLU LEU VAL ASP HIS LEU VAL TYR LEU ALA ALA PHE VAL
SEQRES 11 B 282 PRO ALA ALA ARG PRO ARG PHE THR ASP TYR ILE ASN ALA
SEQRES 12 B 282 PRO GLU ASN ALA ASP VAL VAL ALA LEU PRO ILE PHE SER
SEQRES 13 B 282 ASP PRO ALA ASN LEU GLY ALA HIS ARG LEU ASN PRO LEU
SEQRES 14 B 282 SER SER ASP ALA ILE GLU VAL ASP ALA ILE ARG ARG ALA
SEQRES 15 B 282 PHE LEU THR ASP MSE PRO PRO ASP ALA PRO GLU GLY TRP
SEQRES 16 B 282 ARG HIS LEU LEU HIS PRO ASP GLU PRO TYR ALA SER LEU
SEQRES 17 B 282 SER ALA PRO VAL PRO VAL THR PRO ARG ARG TRP GLY ARG
SEQRES 18 B 282 ILE PRO ARG THR TYR ILE ARG LEU ASP GLY ASP ARG ALA
SEQRES 19 B 282 LEU ALA PRO THR THR GLN ASN LEU MSE ILE ALA GLU ALA
SEQRES 20 B 282 ASP ARG LEU THR PRO ASP ASN PRO PHE GLY VAL ARG SER
SEQRES 21 B 282 LEU PRO GLY ASP HIS SER PRO MSE VAL HIS ARG PRO GLY
SEQRES 22 B 282 GLU LEU ALA ASP LEU LEU ALA GLY ILE
SEQRES 1 C 282 MSE ASN ASP SER ARG ASN SER GLY THR LEU ALA VAL LEU
SEQRES 2 C 282 VAL HIS GLY ALA TRP HIS SER SER LEU HIS TRP ALA ALA
SEQRES 3 C 282 ALA GLN ARG GLY LEU ALA ARG ARG GLY VAL ALA SER ILE
SEQRES 4 C 282 ALA VAL ASP LEU PRO GLY HIS GLY LEU ASP ALA PRO VAL
SEQRES 5 C 282 PRO SER GLY TYR LEU THR ALA GLY GLN PRO GLY LEU GLU
SEQRES 6 C 282 THR GLU LYS SER ALA LEU ALA ASP ILE THR MSE ASP ASP
SEQRES 7 C 282 LEU ALA ASP ALA VAL VAL ASP ALA LEU ALA GLU VAL ARG
SEQRES 8 C 282 SER ARG PHE ALA ARG VAL LEU LEU VAL ALA HIS SER ALA
SEQRES 9 C 282 GLY GLY GLY PRO ALA SER LEU ALA ALA GLU LYS ALA PRO
SEQRES 10 C 282 GLU LEU VAL ASP HIS LEU VAL TYR LEU ALA ALA PHE VAL
SEQRES 11 C 282 PRO ALA ALA ARG PRO ARG PHE THR ASP TYR ILE ASN ALA
SEQRES 12 C 282 PRO GLU ASN ALA ASP VAL VAL ALA LEU PRO ILE PHE SER
SEQRES 13 C 282 ASP PRO ALA ASN LEU GLY ALA HIS ARG LEU ASN PRO LEU
SEQRES 14 C 282 SER SER ASP ALA ILE GLU VAL ASP ALA ILE ARG ARG ALA
SEQRES 15 C 282 PHE LEU THR ASP MSE PRO PRO ASP ALA PRO GLU GLY TRP
SEQRES 16 C 282 ARG HIS LEU LEU HIS PRO ASP GLU PRO TYR ALA SER LEU
SEQRES 17 C 282 SER ALA PRO VAL PRO VAL THR PRO ARG ARG TRP GLY ARG
SEQRES 18 C 282 ILE PRO ARG THR TYR ILE ARG LEU ASP GLY ASP ARG ALA
SEQRES 19 C 282 LEU ALA PRO THR THR GLN ASN LEU MSE ILE ALA GLU ALA
SEQRES 20 C 282 ASP ARG LEU THR PRO ASP ASN PRO PHE GLY VAL ARG SER
SEQRES 21 C 282 LEU PRO GLY ASP HIS SER PRO MSE VAL HIS ARG PRO GLY
SEQRES 22 C 282 GLU LEU ALA ASP LEU LEU ALA GLY ILE
SEQRES 1 D 282 MSE ASN ASP SER ARG ASN SER GLY THR LEU ALA VAL LEU
SEQRES 2 D 282 VAL HIS GLY ALA TRP HIS SER SER LEU HIS TRP ALA ALA
SEQRES 3 D 282 ALA GLN ARG GLY LEU ALA ARG ARG GLY VAL ALA SER ILE
SEQRES 4 D 282 ALA VAL ASP LEU PRO GLY HIS GLY LEU ASP ALA PRO VAL
SEQRES 5 D 282 PRO SER GLY TYR LEU THR ALA GLY GLN PRO GLY LEU GLU
SEQRES 6 D 282 THR GLU LYS SER ALA LEU ALA ASP ILE THR MSE ASP ASP
SEQRES 7 D 282 LEU ALA ASP ALA VAL VAL ASP ALA LEU ALA GLU VAL ARG
SEQRES 8 D 282 SER ARG PHE ALA ARG VAL LEU LEU VAL ALA HIS SER ALA
SEQRES 9 D 282 GLY GLY GLY PRO ALA SER LEU ALA ALA GLU LYS ALA PRO
SEQRES 10 D 282 GLU LEU VAL ASP HIS LEU VAL TYR LEU ALA ALA PHE VAL
SEQRES 11 D 282 PRO ALA ALA ARG PRO ARG PHE THR ASP TYR ILE ASN ALA
SEQRES 12 D 282 PRO GLU ASN ALA ASP VAL VAL ALA LEU PRO ILE PHE SER
SEQRES 13 D 282 ASP PRO ALA ASN LEU GLY ALA HIS ARG LEU ASN PRO LEU
SEQRES 14 D 282 SER SER ASP ALA ILE GLU VAL ASP ALA ILE ARG ARG ALA
SEQRES 15 D 282 PHE LEU THR ASP MSE PRO PRO ASP ALA PRO GLU GLY TRP
SEQRES 16 D 282 ARG HIS LEU LEU HIS PRO ASP GLU PRO TYR ALA SER LEU
SEQRES 17 D 282 SER ALA PRO VAL PRO VAL THR PRO ARG ARG TRP GLY ARG
SEQRES 18 D 282 ILE PRO ARG THR TYR ILE ARG LEU ASP GLY ASP ARG ALA
SEQRES 19 D 282 LEU ALA PRO THR THR GLN ASN LEU MSE ILE ALA GLU ALA
SEQRES 20 D 282 ASP ARG LEU THR PRO ASP ASN PRO PHE GLY VAL ARG SER
SEQRES 21 D 282 LEU PRO GLY ASP HIS SER PRO MSE VAL HIS ARG PRO GLY
SEQRES 22 D 282 GLU LEU ALA ASP LEU LEU ALA GLY ILE
SEQRES 1 E 282 MSE ASN ASP SER ARG ASN SER GLY THR LEU ALA VAL LEU
SEQRES 2 E 282 VAL HIS GLY ALA TRP HIS SER SER LEU HIS TRP ALA ALA
SEQRES 3 E 282 ALA GLN ARG GLY LEU ALA ARG ARG GLY VAL ALA SER ILE
SEQRES 4 E 282 ALA VAL ASP LEU PRO GLY HIS GLY LEU ASP ALA PRO VAL
SEQRES 5 E 282 PRO SER GLY TYR LEU THR ALA GLY GLN PRO GLY LEU GLU
SEQRES 6 E 282 THR GLU LYS SER ALA LEU ALA ASP ILE THR MSE ASP ASP
SEQRES 7 E 282 LEU ALA ASP ALA VAL VAL ASP ALA LEU ALA GLU VAL ARG
SEQRES 8 E 282 SER ARG PHE ALA ARG VAL LEU LEU VAL ALA HIS SER ALA
SEQRES 9 E 282 GLY GLY GLY PRO ALA SER LEU ALA ALA GLU LYS ALA PRO
SEQRES 10 E 282 GLU LEU VAL ASP HIS LEU VAL TYR LEU ALA ALA PHE VAL
SEQRES 11 E 282 PRO ALA ALA ARG PRO ARG PHE THR ASP TYR ILE ASN ALA
SEQRES 12 E 282 PRO GLU ASN ALA ASP VAL VAL ALA LEU PRO ILE PHE SER
SEQRES 13 E 282 ASP PRO ALA ASN LEU GLY ALA HIS ARG LEU ASN PRO LEU
SEQRES 14 E 282 SER SER ASP ALA ILE GLU VAL ASP ALA ILE ARG ARG ALA
SEQRES 15 E 282 PHE LEU THR ASP MSE PRO PRO ASP ALA PRO GLU GLY TRP
SEQRES 16 E 282 ARG HIS LEU LEU HIS PRO ASP GLU PRO TYR ALA SER LEU
SEQRES 17 E 282 SER ALA PRO VAL PRO VAL THR PRO ARG ARG TRP GLY ARG
SEQRES 18 E 282 ILE PRO ARG THR TYR ILE ARG LEU ASP GLY ASP ARG ALA
SEQRES 19 E 282 LEU ALA PRO THR THR GLN ASN LEU MSE ILE ALA GLU ALA
SEQRES 20 E 282 ASP ARG LEU THR PRO ASP ASN PRO PHE GLY VAL ARG SER
SEQRES 21 E 282 LEU PRO GLY ASP HIS SER PRO MSE VAL HIS ARG PRO GLY
SEQRES 22 E 282 GLU LEU ALA ASP LEU LEU ALA GLY ILE
SEQRES 1 F 282 MSE ASN ASP SER ARG ASN SER GLY THR LEU ALA VAL LEU
SEQRES 2 F 282 VAL HIS GLY ALA TRP HIS SER SER LEU HIS TRP ALA ALA
SEQRES 3 F 282 ALA GLN ARG GLY LEU ALA ARG ARG GLY VAL ALA SER ILE
SEQRES 4 F 282 ALA VAL ASP LEU PRO GLY HIS GLY LEU ASP ALA PRO VAL
SEQRES 5 F 282 PRO SER GLY TYR LEU THR ALA GLY GLN PRO GLY LEU GLU
SEQRES 6 F 282 THR GLU LYS SER ALA LEU ALA ASP ILE THR MSE ASP ASP
SEQRES 7 F 282 LEU ALA ASP ALA VAL VAL ASP ALA LEU ALA GLU VAL ARG
SEQRES 8 F 282 SER ARG PHE ALA ARG VAL LEU LEU VAL ALA HIS SER ALA
SEQRES 9 F 282 GLY GLY GLY PRO ALA SER LEU ALA ALA GLU LYS ALA PRO
SEQRES 10 F 282 GLU LEU VAL ASP HIS LEU VAL TYR LEU ALA ALA PHE VAL
SEQRES 11 F 282 PRO ALA ALA ARG PRO ARG PHE THR ASP TYR ILE ASN ALA
SEQRES 12 F 282 PRO GLU ASN ALA ASP VAL VAL ALA LEU PRO ILE PHE SER
SEQRES 13 F 282 ASP PRO ALA ASN LEU GLY ALA HIS ARG LEU ASN PRO LEU
SEQRES 14 F 282 SER SER ASP ALA ILE GLU VAL ASP ALA ILE ARG ARG ALA
SEQRES 15 F 282 PHE LEU THR ASP MSE PRO PRO ASP ALA PRO GLU GLY TRP
SEQRES 16 F 282 ARG HIS LEU LEU HIS PRO ASP GLU PRO TYR ALA SER LEU
SEQRES 17 F 282 SER ALA PRO VAL PRO VAL THR PRO ARG ARG TRP GLY ARG
SEQRES 18 F 282 ILE PRO ARG THR TYR ILE ARG LEU ASP GLY ASP ARG ALA
SEQRES 19 F 282 LEU ALA PRO THR THR GLN ASN LEU MSE ILE ALA GLU ALA
SEQRES 20 F 282 ASP ARG LEU THR PRO ASP ASN PRO PHE GLY VAL ARG SER
SEQRES 21 F 282 LEU PRO GLY ASP HIS SER PRO MSE VAL HIS ARG PRO GLY
SEQRES 22 F 282 GLU LEU ALA ASP LEU LEU ALA GLY ILE
MODRES 7WWF MSE A 76 MET MODIFIED RESIDUE
MODRES 7WWF MSE A 187 MET MODIFIED RESIDUE
MODRES 7WWF MSE A 243 MET MODIFIED RESIDUE
MODRES 7WWF MSE A 268 MET MODIFIED RESIDUE
MODRES 7WWF MSE B 76 MET MODIFIED RESIDUE
MODRES 7WWF MSE B 187 MET MODIFIED RESIDUE
MODRES 7WWF MSE B 243 MET MODIFIED RESIDUE
MODRES 7WWF MSE B 268 MET MODIFIED RESIDUE
MODRES 7WWF MSE C 76 MET MODIFIED RESIDUE
MODRES 7WWF MSE C 187 MET MODIFIED RESIDUE
MODRES 7WWF MSE C 243 MET MODIFIED RESIDUE
MODRES 7WWF MSE C 268 MET MODIFIED RESIDUE
MODRES 7WWF MSE D 76 MET MODIFIED RESIDUE
MODRES 7WWF MSE D 187 MET MODIFIED RESIDUE
MODRES 7WWF MSE D 243 MET MODIFIED RESIDUE
MODRES 7WWF MSE D 268 MET MODIFIED RESIDUE
MODRES 7WWF MSE E 76 MET MODIFIED RESIDUE
MODRES 7WWF MSE E 187 MET MODIFIED RESIDUE
MODRES 7WWF MSE E 243 MET MODIFIED RESIDUE
MODRES 7WWF MSE E 268 MET MODIFIED RESIDUE
MODRES 7WWF MSE F 76 MET MODIFIED RESIDUE
MODRES 7WWF MSE F 187 MET MODIFIED RESIDUE
MODRES 7WWF MSE F 243 MET MODIFIED RESIDUE
MODRES 7WWF MSE F 268 MET MODIFIED RESIDUE
HET MSE A 76 8
HET MSE A 187 8
HET MSE A 243 8
HET MSE A 268 8
HET MSE B 76 8
HET MSE B 187 8
HET MSE B 243 8
HET MSE B 268 8
HET MSE C 76 8
HET MSE C 187 8
HET MSE C 243 8
HET MSE C 268 8
HET MSE D 76 8
HET MSE D 187 8
HET MSE D 243 8
HET MSE D 268 8
HET MSE E 76 8
HET MSE E 187 8
HET MSE E 243 8
HET MSE E 268 8
HET MSE F 76 8
HET MSE F 187 8
HET MSE F 243 8
HET MSE F 268 8
HET PEG A 301 7
HET PEG B 301 4
HET TRS B 302 8
HET PEG C 301 5
HET PEG D 301 4
HET TRS D 302 8
HET PEG E 301 4
HET TRS E 302 8
HET PEG F 301 4
HETNAM MSE SELENOMETHIONINE
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETSYN TRS TRIS BUFFER
FORMUL 1 MSE 24(C5 H11 N O2 SE)
FORMUL 7 PEG 6(C4 H10 O3)
FORMUL 9 TRS 3(C4 H12 N O3 1+)
FORMUL 16 HOH *241(H2 O)
HELIX 1 AA1 SER A 20 HIS A 23 5 4
HELIX 2 AA2 TRP A 24 ARG A 34 1 11
HELIX 3 AA3 HIS A 46 ALA A 50 5 5
HELIX 4 AA4 THR A 75 ARG A 91 1 17
HELIX 5 AA5 SER A 92 PHE A 94 5 3
HELIX 6 AA6 GLY A 105 ALA A 116 1 12
HELIX 7 AA7 PRO A 117 VAL A 120 5 4
HELIX 8 AA8 PHE A 137 ASN A 142 1 6
HELIX 9 AA9 ALA A 143 ALA A 147 5 5
HELIX 10 AB1 ASP A 157 GLY A 162 1 6
HELIX 11 AB2 ASP A 172 LEU A 184 1 13
HELIX 12 AB3 GLY A 194 LEU A 199 1 6
HELIX 13 AB4 TYR A 205 ALA A 210 1 6
HELIX 14 AB5 ARG A 218 ILE A 222 5 5
HELIX 15 AB6 ALA A 236 THR A 251 1 16
HELIX 16 AB7 SER A 266 ARG A 271 1 6
HELIX 17 AB8 ARG A 271 GLY A 281 1 11
HELIX 18 AB9 SER B 20 HIS B 23 5 4
HELIX 19 AC1 TRP B 24 ARG B 34 1 11
HELIX 20 AC2 HIS B 46 ALA B 50 5 5
HELIX 21 AC3 THR B 75 ARG B 91 1 17
HELIX 22 AC4 SER B 92 PHE B 94 5 3
HELIX 23 AC5 GLY B 105 ALA B 116 1 12
HELIX 24 AC6 PRO B 117 VAL B 120 5 4
HELIX 25 AC7 PHE B 137 ASN B 142 1 6
HELIX 26 AC8 ALA B 143 ALA B 147 5 5
HELIX 27 AC9 ASP B 157 GLY B 162 1 6
HELIX 28 AD1 ASP B 172 LEU B 184 1 13
HELIX 29 AD2 GLU B 193 LEU B 198 1 6
HELIX 30 AD3 TYR B 205 ALA B 210 1 6
HELIX 31 AD4 ARG B 218 ILE B 222 5 5
HELIX 32 AD5 ALA B 236 LEU B 250 1 15
HELIX 33 AD6 SER B 266 ARG B 271 1 6
HELIX 34 AD7 ARG B 271 GLY B 281 1 11
HELIX 35 AD8 SER C 20 HIS C 23 5 4
HELIX 36 AD9 TRP C 24 ARG C 34 1 11
HELIX 37 AE1 HIS C 46 ALA C 50 5 5
HELIX 38 AE2 THR C 75 ARG C 91 1 17
HELIX 39 AE3 GLY C 105 ALA C 116 1 12
HELIX 40 AE4 PRO C 117 VAL C 120 5 4
HELIX 41 AE5 PHE C 137 ASN C 142 1 6
HELIX 42 AE6 ALA C 143 ALA C 147 5 5
HELIX 43 AE7 ASP C 157 GLY C 162 1 6
HELIX 44 AE8 ASP C 172 LEU C 184 1 13
HELIX 45 AE9 GLU C 193 HIS C 197 5 5
HELIX 46 AF1 TYR C 205 ALA C 210 1 6
HELIX 47 AF2 ARG C 218 ILE C 222 5 5
HELIX 48 AF3 ALA C 236 THR C 251 1 16
HELIX 49 AF4 SER C 266 ARG C 271 1 6
HELIX 50 AF5 ARG C 271 GLY C 281 1 11
HELIX 51 AF6 SER D 20 HIS D 23 5 4
HELIX 52 AF7 TRP D 24 ARG D 34 1 11
HELIX 53 AF8 HIS D 46 ALA D 50 5 5
HELIX 54 AF9 THR D 75 ARG D 91 1 17
HELIX 55 AG1 SER D 92 PHE D 94 5 3
HELIX 56 AG2 GLY D 105 ALA D 116 1 12
HELIX 57 AG3 PRO D 117 VAL D 120 5 4
HELIX 58 AG4 PHE D 137 ASN D 142 1 6
HELIX 59 AG5 ALA D 143 ALA D 147 5 5
HELIX 60 AG6 ASP D 157 GLY D 162 1 6
HELIX 61 AG7 ASP D 172 LEU D 184 1 13
HELIX 62 AG8 GLU D 193 LEU D 199 5 7
HELIX 63 AG9 TYR D 205 ALA D 210 1 6
HELIX 64 AH1 ARG D 218 ILE D 222 5 5
HELIX 65 AH2 ALA D 236 LEU D 250 1 15
HELIX 66 AH3 SER D 266 ARG D 271 1 6
HELIX 67 AH4 ARG D 271 GLY D 281 1 11
HELIX 68 AH5 SER E 20 HIS E 23 5 4
HELIX 69 AH6 TRP E 24 ARG E 34 1 11
HELIX 70 AH7 HIS E 46 ALA E 50 5 5
HELIX 71 AH8 THR E 75 ARG E 91 1 17
HELIX 72 AH9 SER E 92 PHE E 94 5 3
HELIX 73 AI1 GLY E 105 ALA E 116 1 12
HELIX 74 AI2 PRO E 117 VAL E 120 5 4
HELIX 75 AI3 PHE E 137 ASN E 142 1 6
HELIX 76 AI4 ALA E 143 ALA E 147 5 5
HELIX 77 AI5 ASP E 157 GLY E 162 1 6
HELIX 78 AI6 ASP E 172 LEU E 184 1 13
HELIX 79 AI7 GLU E 193 HIS E 197 5 5
HELIX 80 AI8 TYR E 205 ALA E 210 1 6
HELIX 81 AI9 ARG E 218 ILE E 222 5 5
HELIX 82 AJ1 ALA E 236 THR E 251 1 16
HELIX 83 AJ2 SER E 266 ARG E 271 1 6
HELIX 84 AJ3 ARG E 271 ILE E 282 1 12
HELIX 85 AJ4 SER F 20 HIS F 23 5 4
HELIX 86 AJ5 TRP F 24 ARG F 34 1 11
HELIX 87 AJ6 HIS F 46 ALA F 50 5 5
HELIX 88 AJ7 THR F 75 ARG F 91 1 17
HELIX 89 AJ8 GLY F 105 ALA F 116 1 12
HELIX 90 AJ9 PRO F 117 VAL F 120 5 4
HELIX 91 AK1 ARG F 136 ASN F 142 1 7
HELIX 92 AK2 ALA F 143 ALA F 147 5 5
HELIX 93 AK3 ASP F 157 GLY F 162 1 6
HELIX 94 AK4 ASP F 172 LEU F 184 1 13
HELIX 95 AK5 GLU F 193 LEU F 198 5 6
HELIX 96 AK6 TYR F 205 ALA F 210 1 6
HELIX 97 AK7 ARG F 218 ILE F 222 5 5
HELIX 98 AK8 ALA F 236 THR F 251 1 16
HELIX 99 AK9 SER F 266 ARG F 271 1 6
HELIX 100 AL1 ARG F 271 ILE F 282 1 12
SHEET 1 AA1 6 ALA A 37 VAL A 41 0
SHEET 2 AA1 6 THR A 9 VAL A 14 1 N LEU A 13 O ILE A 39
SHEET 3 AA1 6 ARG A 96 HIS A 102 1 O LEU A 98 N VAL A 12
SHEET 4 AA1 6 HIS A 122 LEU A 126 1 O VAL A 124 N LEU A 99
SHEET 5 AA1 6 ARG A 224 LEU A 229 1 O ILE A 227 N TYR A 125
SHEET 6 AA1 6 GLY A 257 LEU A 261 1 O GLY A 257 N TYR A 226
SHEET 1 AA2 2 ALA A 163 ARG A 165 0
SHEET 2 AA2 2 ASP A 202 PRO A 204 -1 O GLU A 203 N HIS A 164
SHEET 1 AA3 6 ALA B 37 VAL B 41 0
SHEET 2 AA3 6 THR B 9 VAL B 14 1 N LEU B 13 O VAL B 41
SHEET 3 AA3 6 ARG B 96 HIS B 102 1 O LEU B 98 N VAL B 12
SHEET 4 AA3 6 HIS B 122 LEU B 126 1 O LEU B 126 N ALA B 101
SHEET 5 AA3 6 ARG B 224 LEU B 229 1 O ILE B 227 N TYR B 125
SHEET 6 AA3 6 GLY B 257 LEU B 261 1 O GLY B 257 N TYR B 226
SHEET 1 AA4 2 ALA B 163 ARG B 165 0
SHEET 2 AA4 2 ASP B 202 PRO B 204 -1 O GLU B 203 N HIS B 164
SHEET 1 AA5 6 ALA C 37 VAL C 41 0
SHEET 2 AA5 6 THR C 9 VAL C 14 1 N LEU C 13 O ILE C 39
SHEET 3 AA5 6 ARG C 96 HIS C 102 1 O LEU C 98 N VAL C 12
SHEET 4 AA5 6 HIS C 122 LEU C 126 1 O VAL C 124 N LEU C 99
SHEET 5 AA5 6 ARG C 224 LEU C 229 1 O ILE C 227 N TYR C 125
SHEET 6 AA5 6 GLY C 257 LEU C 261 1 O GLY C 257 N TYR C 226
SHEET 1 AA6 2 ALA C 163 ARG C 165 0
SHEET 2 AA6 2 ASP C 202 PRO C 204 -1 O GLU C 203 N HIS C 164
SHEET 1 AA7 6 ALA D 37 VAL D 41 0
SHEET 2 AA7 6 THR D 9 VAL D 14 1 N LEU D 13 O ILE D 39
SHEET 3 AA7 6 ARG D 96 HIS D 102 1 O LEU D 98 N VAL D 12
SHEET 4 AA7 6 HIS D 122 LEU D 126 1 O LEU D 126 N ALA D 101
SHEET 5 AA7 6 ARG D 224 LEU D 229 1 O ILE D 227 N TYR D 125
SHEET 6 AA7 6 GLY D 257 LEU D 261 1 O GLY D 257 N TYR D 226
SHEET 1 AA8 2 ALA D 163 ARG D 165 0
SHEET 2 AA8 2 ASP D 202 PRO D 204 -1 O GLU D 203 N HIS D 164
SHEET 1 AA9 6 ALA E 37 VAL E 41 0
SHEET 2 AA9 6 THR E 9 VAL E 14 1 N LEU E 13 O ILE E 39
SHEET 3 AA9 6 ARG E 96 HIS E 102 1 O LEU E 98 N VAL E 12
SHEET 4 AA9 6 HIS E 122 LEU E 126 1 O LEU E 126 N ALA E 101
SHEET 5 AA9 6 ARG E 224 LEU E 229 1 O ILE E 227 N TYR E 125
SHEET 6 AA9 6 GLY E 257 LEU E 261 1 O GLY E 257 N TYR E 226
SHEET 1 AB1 2 ALA E 163 ARG E 165 0
SHEET 2 AB1 2 ASP E 202 PRO E 204 -1 O GLU E 203 N HIS E 164
SHEET 1 AB2 6 ALA F 37 VAL F 41 0
SHEET 2 AB2 6 THR F 9 VAL F 14 1 N LEU F 13 O ILE F 39
SHEET 3 AB2 6 ARG F 96 HIS F 102 1 O LEU F 98 N VAL F 12
SHEET 4 AB2 6 HIS F 122 LEU F 126 1 O LEU F 126 N ALA F 101
SHEET 5 AB2 6 ARG F 224 LEU F 229 1 O ILE F 227 N TYR F 125
SHEET 6 AB2 6 GLY F 257 LEU F 261 1 O GLY F 257 N TYR F 226
SHEET 1 AB3 2 ALA F 163 ARG F 165 0
SHEET 2 AB3 2 ASP F 202 PRO F 204 -1 O GLU F 203 N HIS F 164
LINK C THR A 75 N MSE A 76 1555 1555 1.33
LINK C MSE A 76 N ASP A 77 1555 1555 1.34
LINK C ASP A 186 N MSE A 187 1555 1555 1.33
LINK C MSE A 187 N PRO A 188 1555 1555 1.33
LINK C LEU A 242 N MSE A 243 1555 1555 1.33
LINK C MSE A 243 N ILE A 244 1555 1555 1.33
LINK C PRO A 267 N MSE A 268 1555 1555 1.33
LINK C MSE A 268 N VAL A 269 1555 1555 1.33
LINK C THR B 75 N MSE B 76 1555 1555 1.33
LINK C MSE B 76 N ASP B 77 1555 1555 1.34
LINK C ASP B 186 N MSE B 187 1555 1555 1.33
LINK C MSE B 187 N PRO B 188 1555 1555 1.33
LINK C LEU B 242 N MSE B 243 1555 1555 1.33
LINK C MSE B 243 N ILE B 244 1555 1555 1.33
LINK C PRO B 267 N MSE B 268 1555 1555 1.33
LINK C MSE B 268 N VAL B 269 1555 1555 1.33
LINK C THR C 75 N MSE C 76 1555 1555 1.33
LINK C MSE C 76 N ASP C 77 1555 1555 1.34
LINK C ASP C 186 N MSE C 187 1555 1555 1.33
LINK C MSE C 187 N PRO C 188 1555 1555 1.33
LINK C LEU C 242 N MSE C 243 1555 1555 1.33
LINK C MSE C 243 N ILE C 244 1555 1555 1.34
LINK C PRO C 267 N MSE C 268 1555 1555 1.33
LINK C MSE C 268 N VAL C 269 1555 1555 1.33
LINK C THR D 75 N MSE D 76 1555 1555 1.33
LINK C MSE D 76 N ASP D 77 1555 1555 1.34
LINK C ASP D 186 N MSE D 187 1555 1555 1.33
LINK C MSE D 187 N PRO D 188 1555 1555 1.33
LINK C LEU D 242 N MSE D 243 1555 1555 1.33
LINK C MSE D 243 N ILE D 244 1555 1555 1.33
LINK C PRO D 267 N MSE D 268 1555 1555 1.33
LINK C MSE D 268 N VAL D 269 1555 1555 1.33
LINK C THR E 75 N MSE E 76 1555 1555 1.33
LINK C MSE E 76 N ASP E 77 1555 1555 1.34
LINK C ASP E 186 N MSE E 187 1555 1555 1.33
LINK C MSE E 187 N PRO E 188 1555 1555 1.33
LINK C LEU E 242 N MSE E 243 1555 1555 1.33
LINK C MSE E 243 N ILE E 244 1555 1555 1.33
LINK C PRO E 267 N MSE E 268 1555 1555 1.33
LINK C MSE E 268 N VAL E 269 1555 1555 1.33
LINK C THR F 75 N MSE F 76 1555 1555 1.33
LINK C MSE F 76 N ASP F 77 1555 1555 1.34
LINK C ASP F 186 N MSE F 187 1555 1555 1.33
LINK C MSE F 187 N PRO F 188 1555 1555 1.34
LINK C LEU F 242 N MSE F 243 1555 1555 1.33
LINK C MSE F 243 N ILE F 244 1555 1555 1.34
LINK C PRO F 267 N MSE F 268 1555 1555 1.33
LINK C MSE F 268 N VAL F 269 1555 1555 1.33
CRYST1 91.668 65.830 172.809 90.00 97.76 90.00 P 1 21 1 12
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 0.010909 0.000000 0.001487 0.00000
SCALE2 0.000000 0.015191 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005840 0.00000
TER 2076 ILE A 282
TER 4133 ILE B 282
TER 6205 ILE C 282
TER 8264 ILE D 282
TER 10320 ILE E 282
TER 12378 ILE F 282
MASTER 370 0 33 100 48 0 0 612665 6 292 132
END |