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HEADER HYDROLASE 27-JAN-15 4XVC
TITLE CRYSTAL STRUCTURE OF AN ESTERASE FROM THE BACTERIAL HORMONE-SENSITIVE
TITLE 2 LIPASE (HSL) FAMILY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE E40;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 EC: 3.1.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENVIRONMENTAL SAMPLES;
SOURCE 3 ORGANISM_TAXID: 33858;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 866768
KEYWDS ESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.ZHANG,P.LI
REVDAT 1 25-MAR-15 4XVC 0
JRNL AUTH P.Y.LI,X.L.CHEN,P.JI,C.Y.LI,P.WANG,Y.ZHANG,B.B.XIE,Q.L.QIN,
JRNL AUTH 2 H.N.SU,B.C.ZHOU,Y.Z.ZHANG,X.Y.ZHANG
JRNL TITL INTER-DOMAIN HYDROPHOBIC INTERACTIONS MODULATE THE
JRNL TITL 2 THERMOSTABILITY OF MICROBIAL ESTERASES FROM THE
JRNL TITL 3 HORMONE-SENSITIVE LIPASE FAMILY
JRNL REF J.BIOL.CHEM. 2015
JRNL REFN ESSN 1083-351X
JRNL DOI 10.1074/JBC.M115.646182
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.4_486)
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.33
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.040
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.7
REMARK 3 NUMBER OF REFLECTIONS : 161567
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 8110
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 39.3382 - 6.2100 0.92 5086 261 0.2108 0.2219
REMARK 3 2 6.2100 - 4.9321 0.97 5376 258 0.2004 0.2132
REMARK 3 3 4.9321 - 4.3095 0.97 5376 265 0.1788 0.1928
REMARK 3 4 4.3095 - 3.9159 0.97 5297 299 0.1837 0.2386
REMARK 3 5 3.9159 - 3.6354 0.91 5040 225 0.1913 0.2058
REMARK 3 6 3.6354 - 3.4212 0.94 5160 307 0.1962 0.2370
REMARK 3 7 3.4212 - 3.2500 0.94 5166 283 0.2080 0.2311
REMARK 3 8 3.2500 - 3.1086 0.94 5156 292 0.2160 0.2206
REMARK 3 9 3.1086 - 2.9889 0.94 5205 270 0.2126 0.2286
REMARK 3 10 2.9889 - 2.8858 0.94 5202 269 0.2063 0.2270
REMARK 3 11 2.8858 - 2.7956 0.94 5130 286 0.2016 0.2579
REMARK 3 12 2.7956 - 2.7157 0.93 5162 276 0.1972 0.2391
REMARK 3 13 2.7157 - 2.6442 0.93 5139 281 0.2081 0.2358
REMARK 3 14 2.6442 - 2.5797 0.93 5186 262 0.2033 0.2491
REMARK 3 15 2.5797 - 2.5211 0.94 5134 295 0.2065 0.2514
REMARK 3 16 2.5211 - 2.4675 0.93 5136 280 0.1967 0.2217
REMARK 3 17 2.4675 - 2.4181 0.93 5117 275 0.2003 0.2551
REMARK 3 18 2.4181 - 2.3725 0.93 5175 266 0.1953 0.2403
REMARK 3 19 2.3725 - 2.3301 0.92 5045 266 0.1869 0.2342
REMARK 3 20 2.3301 - 2.2906 0.93 5208 265 0.1903 0.2478
REMARK 3 21 2.2906 - 2.2537 0.92 5038 267 0.1963 0.2499
REMARK 3 22 2.2537 - 2.2190 0.92 5110 289 0.1817 0.2178
REMARK 3 23 2.2190 - 2.1864 0.93 5082 270 0.1797 0.2259
REMARK 3 24 2.1864 - 2.1556 0.92 5094 274 0.1877 0.2304
REMARK 3 25 2.1556 - 2.1265 0.92 5028 267 0.1842 0.2139
REMARK 3 26 2.1265 - 2.0988 0.91 5063 257 0.1883 0.2656
REMARK 3 27 2.0988 - 2.0726 0.91 4983 261 0.1901 0.2306
REMARK 3 28 2.0726 - 2.0476 0.91 5146 229 0.1878 0.2515
REMARK 3 29 2.0476 - 2.0238 0.90 4934 257 0.1976 0.2710
REMARK 3 30 2.0238 - 2.0011 0.81 4483 258 0.1907 0.2391
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.95
REMARK 3 K_SOL : 0.34
REMARK 3 B_SOL : 40.10
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.120
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.65470
REMARK 3 B22 (A**2) : -2.43280
REMARK 3 B33 (A**2) : -0.22190
REMARK 3 B12 (A**2) : 7.10720
REMARK 3 B13 (A**2) : 2.09600
REMARK 3 B23 (A**2) : 1.36510
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 : 0.008 18566
REMARK 3 ANGLE : 1.088 25322
REMARK 3 CHIRALITY : 0.074 2829
REMARK 3 PLANARITY : 0.005 3338
REMARK 3 DIHEDRAL : 13.594 6858
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 2:297 )
REMARK 3 SELECTION : CHAIN B AND (RESSEQ 2:297 )
REMARK 3 ATOM PAIRS NUMBER : 2242
REMARK 3 RMSD : 0.033
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 2:297 )
REMARK 3 SELECTION : CHAIN C AND (RESSEQ 2:297 )
REMARK 3 ATOM PAIRS NUMBER : 2221
REMARK 3 RMSD : 0.043
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 2:297 )
REMARK 3 SELECTION : CHAIN D AND (RESSEQ 2:297 )
REMARK 3 ATOM PAIRS NUMBER : 2214
REMARK 3 RMSD : 0.045
REMARK 3 NCS OPERATOR : 4
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 2:297 )
REMARK 3 SELECTION : CHAIN E AND (RESSEQ 2:297 )
REMARK 3 ATOM PAIRS NUMBER : 2220
REMARK 3 RMSD : 0.039
REMARK 3 NCS OPERATOR : 5
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 2:297 )
REMARK 3 SELECTION : CHAIN F AND (RESSEQ 2:297 )
REMARK 3 ATOM PAIRS NUMBER : 2236
REMARK 3 RMSD : 0.031
REMARK 3 NCS OPERATOR : 6
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 2:297 )
REMARK 3 SELECTION : CHAIN G AND (RESSEQ 2:297 )
REMARK 3 ATOM PAIRS NUMBER : 2227
REMARK 3 RMSD : 0.046
REMARK 3 NCS OPERATOR : 7
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 2:297 )
REMARK 3 SELECTION : CHAIN H AND (RESSEQ 2:297 )
REMARK 3 ATOM PAIRS NUMBER : 2227
REMARK 3 RMSD : 0.045
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4XVC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-FEB-15.
REMARK 100 THE DEPOSITION ID IS D_1000206357.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-NOV-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.8
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
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 : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 161567
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.11800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 24.4170
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) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.24800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 3H18
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.15M AMMONIUM SULFATE, 0.1M MES,
REMARK 280 12%(W/V) PEG 4,000, PH 5.8, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
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, 4, 5, 6, 7, 8
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 7
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 8
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET C -19
REMARK 465 GLY C -18
REMARK 465 SER C -17
REMARK 465 SER C -16
REMARK 465 HIS C -15
REMARK 465 HIS C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 HIS C -10
REMARK 465 SER C -9
REMARK 465 SER C -8
REMARK 465 GLY C -7
REMARK 465 LEU C -6
REMARK 465 VAL C -5
REMARK 465 PRO C -4
REMARK 465 ARG C -3
REMARK 465 GLY C -2
REMARK 465 SER C -1
REMARK 465 HIS C 0
REMARK 465 MET D -19
REMARK 465 GLY D -18
REMARK 465 SER D -17
REMARK 465 SER D -16
REMARK 465 HIS D -15
REMARK 465 HIS D -14
REMARK 465 HIS D -13
REMARK 465 HIS D -12
REMARK 465 HIS D -11
REMARK 465 HIS D -10
REMARK 465 SER D -9
REMARK 465 SER D -8
REMARK 465 GLY D -7
REMARK 465 LEU D -6
REMARK 465 VAL D -5
REMARK 465 PRO D -4
REMARK 465 ARG D -3
REMARK 465 GLY D -2
REMARK 465 SER D -1
REMARK 465 HIS D 0
REMARK 465 MET E -19
REMARK 465 GLY E -18
REMARK 465 SER E -17
REMARK 465 SER E -16
REMARK 465 HIS E -15
REMARK 465 HIS E -14
REMARK 465 HIS E -13
REMARK 465 HIS E -12
REMARK 465 HIS E -11
REMARK 465 HIS E -10
REMARK 465 SER E -9
REMARK 465 SER E -8
REMARK 465 GLY E -7
REMARK 465 LEU E -6
REMARK 465 VAL E -5
REMARK 465 PRO E -4
REMARK 465 ARG E -3
REMARK 465 GLY E -2
REMARK 465 SER E -1
REMARK 465 HIS E 0
REMARK 465 MET F -19
REMARK 465 GLY F -18
REMARK 465 SER F -17
REMARK 465 SER F -16
REMARK 465 HIS F -15
REMARK 465 HIS F -14
REMARK 465 HIS F -13
REMARK 465 HIS F -12
REMARK 465 HIS F -11
REMARK 465 HIS F -10
REMARK 465 SER F -9
REMARK 465 SER F -8
REMARK 465 GLY F -7
REMARK 465 LEU F -6
REMARK 465 VAL F -5
REMARK 465 PRO F -4
REMARK 465 ARG F -3
REMARK 465 GLY F -2
REMARK 465 SER F -1
REMARK 465 HIS F 0
REMARK 465 MET G -19
REMARK 465 GLY G -18
REMARK 465 SER G -17
REMARK 465 SER G -16
REMARK 465 HIS G -15
REMARK 465 HIS G -14
REMARK 465 HIS G -13
REMARK 465 HIS G -12
REMARK 465 HIS G -11
REMARK 465 HIS G -10
REMARK 465 SER G -9
REMARK 465 SER G -8
REMARK 465 GLY G -7
REMARK 465 LEU G -6
REMARK 465 VAL G -5
REMARK 465 PRO G -4
REMARK 465 ARG G -3
REMARK 465 GLY G -2
REMARK 465 SER G -1
REMARK 465 HIS G 0
REMARK 465 MET H -19
REMARK 465 GLY H -18
REMARK 465 SER H -17
REMARK 465 SER H -16
REMARK 465 HIS H -15
REMARK 465 HIS H -14
REMARK 465 HIS H -13
REMARK 465 HIS H -12
REMARK 465 HIS H -11
REMARK 465 HIS H -10
REMARK 465 SER H -9
REMARK 465 SER H -8
REMARK 465 GLY H -7
REMARK 465 LEU H -6
REMARK 465 VAL H -5
REMARK 465 PRO H -4
REMARK 465 ARG H -3
REMARK 465 GLY H -2
REMARK 465 SER H -1
REMARK 465 HIS H 0
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OG SER C 145 S PMS C 301 1.05
REMARK 500 OG SER E 145 S PMS E 301 1.10
REMARK 500 OG SER H 145 S PMS H 301 1.14
REMARK 500 OG SER G 145 S PMS G 301 1.19
REMARK 500 OG SER F 145 O2S PMS F 301 1.23
REMARK 500 OG SER C 145 O2S PMS C 301 1.76
REMARK 500 OG SER E 145 O1S PMS E 301 1.97
REMARK 500 OG SER H 145 O2S PMS H 301 2.00
REMARK 500 O PRO D 220 O HOH D 490 2.03
REMARK 500 NH1 ARG F 66 O HOH F 401 2.06
REMARK 500 OG SER F 145 S PMS F 301 2.07
REMARK 500 CB SER E 145 S PMS E 301 2.09
REMARK 500 OG SER G 145 O2S PMS G 301 2.09
REMARK 500 NH2 ARG G 30 O HOH G 476 2.10
REMARK 500 CB SER C 145 S PMS C 301 2.11
REMARK 500 OG SER C 145 O1S PMS C 301 2.13
REMARK 500 OG SER H 145 O1S PMS H 301 2.13
REMARK 500 NH2 ARG B 30 O HOH B 2001 2.16
REMARK 500 CB SER D 145 S PMS D 301 2.17
REMARK 500 O HOH D 593 O HOH F 487 2.17
REMARK 500 OG SER D 145 O HOH D 624 2.18
REMARK 500 CG ARG D 66 NH1 ARG G 66 2.18
REMARK 500 OG SER B 145 O HOH B 2182 2.19
REMARK 500 CE MET A 39 O HOH A 532 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LYS E 3 N - CA - C ANGL. DEV. = -16.3 DEGREES
REMARK 500 ARG G 66 NE - CZ - NH1 ANGL. DEV. = -3.1 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 SER A 4 113.66 139.32
REMARK 500 LYS A 23 -55.28 -125.41
REMARK 500 SER A 83 -174.72 -176.40
REMARK 500 PRO A 116 31.67 -98.79
REMARK 500 SER A 145 -120.89 44.90
REMARK 500 ALA B 2 167.12 137.75
REMARK 500 SER B 4 113.88 139.41
REMARK 500 LYS B 23 -55.22 -126.24
REMARK 500 SER B 83 -174.96 -175.80
REMARK 500 SER B 145 -118.95 45.51
REMARK 500 ASP B 266 -1.66 71.53
REMARK 500 SER C 4 113.83 138.10
REMARK 500 LYS C 23 -54.42 -126.32
REMARK 500 SER C 83 -174.55 -177.21
REMARK 500 PRO C 116 31.83 -99.79
REMARK 500 SER C 145 -123.99 52.35
REMARK 500 PRO C 220 -9.28 -59.61
REMARK 500 ASP C 266 -1.27 72.64
REMARK 500 SER D 4 113.47 137.02
REMARK 500 LYS D 23 -54.20 -126.19
REMARK 500 SER D 83 -175.09 -177.24
REMARK 500 SER D 145 -117.42 47.46
REMARK 500 ASP D 266 -1.03 70.97
REMARK 500 SER E 4 114.15 140.58
REMARK 500 LYS E 23 -55.28 -126.53
REMARK 500 SER E 83 -172.70 -173.38
REMARK 500 SER E 145 -121.51 55.53
REMARK 500 ASP E 266 -1.46 71.54
REMARK 500 SER F 4 116.18 139.48
REMARK 500 LYS F 23 -54.99 -126.97
REMARK 500 SER F 83 -173.18 -173.57
REMARK 500 PRO F 116 32.59 -99.28
REMARK 500 SER F 145 -125.33 53.71
REMARK 500 ASP F 266 -3.22 72.43
REMARK 500 SER G 4 114.75 138.29
REMARK 500 LYS G 23 -53.34 -125.87
REMARK 500 SER G 83 -175.45 -174.70
REMARK 500 PRO G 116 33.85 -99.89
REMARK 500 SER G 145 -120.75 55.88
REMARK 500 ASP G 266 -1.17 73.58
REMARK 500 ALA H 2 169.29 141.20
REMARK 500 SER H 4 114.10 137.89
REMARK 500 LYS H 23 -54.32 -126.28
REMARK 500 SER H 83 -174.97 -175.27
REMARK 500 SER H 145 -120.06 53.62
REMARK 500 ASP H 266 -1.64 71.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ALA E 2 LYS E 3 -131.68
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 B2218 DISTANCE = 6.67 ANGSTROMS
REMARK 525 HOH F 641 DISTANCE = 5.99 ANGSTROMS
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 PMS C 301
REMARK 610 PMS D 301
REMARK 610 PMS E 301
REMARK 610 PMS F 301
REMARK 610 PMS G 301
REMARK 610 PMS H 301
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PMS A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PMS C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PMS D 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PMS E 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PMS F 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PMS G 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PMS H 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide PMS B 301 and SER B
REMARK 800 145
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4XVF RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE OF THIS PROTEIN WAS NOT AVAILABLE AT THE UNIPROT
REMARK 999 KNOWLEDGEBASE DATABASE (UNIPROTKB) AT THE TIME OF DEPOSITION AND
REMARK 999 THE SEQUENCE HAS BEEN SUBMITTED TO GENBANK UNDER THE ACCESSION
REMARK 999 NUMBER KP696774.
DBREF 4XVC A -19 297 PDB 4XVC 4XVC -19 297
DBREF 4XVC B -19 297 PDB 4XVC 4XVC -19 297
DBREF 4XVC C -19 297 PDB 4XVC 4XVC -19 297
DBREF 4XVC D -19 297 PDB 4XVC 4XVC -19 297
DBREF 4XVC E -19 297 PDB 4XVC 4XVC -19 297
DBREF 4XVC F -19 297 PDB 4XVC 4XVC -19 297
DBREF 4XVC G -19 297 PDB 4XVC 4XVC -19 297
DBREF 4XVC H -19 297 PDB 4XVC 4XVC -19 297
SEQRES 1 A 317 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 317 LEU VAL PRO ARG GLY SER HIS MET ALA LYS SER PRO GLU
SEQRES 3 A 317 LEU ASP ARG VAL ILE GLY MET ILE ARG GLU ARG ALA ALA
SEQRES 4 A 317 THR PRO ARG LYS THR THR ASP ASP ASP ARG ARG LEU TYR
SEQRES 5 A 317 GLU THR MET LEU GLY SER MET PRO LEU ASP ASP ASP ILE
SEQRES 6 A 317 GLN THR GLU ARG LEU GLY VAL ASN GLY VAL PRO ALA GLU
SEQRES 7 A 317 TRP ILE TYR ALA PRO GLY ALA ARG ASP ASP GLN VAL PHE
SEQRES 8 A 317 LEU TYR LEU HIS GLY GLY GLY TYR VAL ILE GLY SER MET
SEQRES 9 A 317 ARG THR HIS ARG VAL MET LEU SER HIS ILE ALA ARG ALA
SEQRES 10 A 317 ALA GLY CYS ARG VAL LEU GLY LEU ASP TYR ARG LEU ALA
SEQRES 11 A 317 PRO GLU THR PRO PHE PRO ALA PRO VAL GLU ASP THR VAL
SEQRES 12 A 317 ALA ALA TYR ARG TRP LEU LEU ALA HIS GLY TYR ASP PRO
SEQRES 13 A 317 SER ARG ILE ALA LEU GLY GLY ASP SER ALA GLY GLY GLY
SEQRES 14 A 317 LEU VAL VAL ALA ALA LEU VAL ALA LEU ARG TYR ILE GLY
SEQRES 15 A 317 GLU PRO LEU PRO ALA ALA GLY VAL CYS LEU SER PRO TRP
SEQRES 16 A 317 ILE ASP MET GLU ALA THR GLY GLU SER PHE THR THR ASN
SEQRES 17 A 317 ALA THR MET ASP PRO SER VAL ASN LYS GLU ARG VAL MET
SEQRES 18 A 317 SER ILE ALA ALA LEU TYR LEU GLY GLY LYS ASN PRO GLN
SEQRES 19 A 317 ALA PRO LEU ALA SER PRO LEU TYR ALA ASP LEU GLN GLY
SEQRES 20 A 317 LEU PRO PRO LEU LEU VAL GLN VAL GLY GLY ILE GLU THR
SEQRES 21 A 317 LEU LEU ASP ASP ALA ARG ALA LEU THR THR ARG ALA LYS
SEQRES 22 A 317 ALA ALA GLY VAL ASP ALA ASP LEU GLU VAL TRP ASP ASP
SEQRES 23 A 317 MET PRO HIS VAL TRP GLN HIS PHE ALA PRO ILE LEU PRO
SEQRES 24 A 317 GLU GLY LYS GLN ALA ILE ALA ARG ILE GLY GLU PHE LEU
SEQRES 25 A 317 ARG LYS GLN ILE GLY
SEQRES 1 B 317 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 317 LEU VAL PRO ARG GLY SER HIS MET ALA LYS SER PRO GLU
SEQRES 3 B 317 LEU ASP ARG VAL ILE GLY MET ILE ARG GLU ARG ALA ALA
SEQRES 4 B 317 THR PRO ARG LYS THR THR ASP ASP ASP ARG ARG LEU TYR
SEQRES 5 B 317 GLU THR MET LEU GLY SER MET PRO LEU ASP ASP ASP ILE
SEQRES 6 B 317 GLN THR GLU ARG LEU GLY VAL ASN GLY VAL PRO ALA GLU
SEQRES 7 B 317 TRP ILE TYR ALA PRO GLY ALA ARG ASP ASP GLN VAL PHE
SEQRES 8 B 317 LEU TYR LEU HIS GLY GLY GLY TYR VAL ILE GLY SER MET
SEQRES 9 B 317 ARG THR HIS ARG VAL MET LEU SER HIS ILE ALA ARG ALA
SEQRES 10 B 317 ALA GLY CYS ARG VAL LEU GLY LEU ASP TYR ARG LEU ALA
SEQRES 11 B 317 PRO GLU THR PRO PHE PRO ALA PRO VAL GLU ASP THR VAL
SEQRES 12 B 317 ALA ALA TYR ARG TRP LEU LEU ALA HIS GLY TYR ASP PRO
SEQRES 13 B 317 SER ARG ILE ALA LEU GLY GLY ASP SER ALA GLY GLY GLY
SEQRES 14 B 317 LEU VAL VAL ALA ALA LEU VAL ALA LEU ARG TYR ILE GLY
SEQRES 15 B 317 GLU PRO LEU PRO ALA ALA GLY VAL CYS LEU SER PRO TRP
SEQRES 16 B 317 ILE ASP MET GLU ALA THR GLY GLU SER PHE THR THR ASN
SEQRES 17 B 317 ALA THR MET ASP PRO SER VAL ASN LYS GLU ARG VAL MET
SEQRES 18 B 317 SER ILE ALA ALA LEU TYR LEU GLY GLY LYS ASN PRO GLN
SEQRES 19 B 317 ALA PRO LEU ALA SER PRO LEU TYR ALA ASP LEU GLN GLY
SEQRES 20 B 317 LEU PRO PRO LEU LEU VAL GLN VAL GLY GLY ILE GLU THR
SEQRES 21 B 317 LEU LEU ASP ASP ALA ARG ALA LEU THR THR ARG ALA LYS
SEQRES 22 B 317 ALA ALA GLY VAL ASP ALA ASP LEU GLU VAL TRP ASP ASP
SEQRES 23 B 317 MET PRO HIS VAL TRP GLN HIS PHE ALA PRO ILE LEU PRO
SEQRES 24 B 317 GLU GLY LYS GLN ALA ILE ALA ARG ILE GLY GLU PHE LEU
SEQRES 25 B 317 ARG LYS GLN ILE GLY
SEQRES 1 C 317 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 317 LEU VAL PRO ARG GLY SER HIS MET ALA LYS SER PRO GLU
SEQRES 3 C 317 LEU ASP ARG VAL ILE GLY MET ILE ARG GLU ARG ALA ALA
SEQRES 4 C 317 THR PRO ARG LYS THR THR ASP ASP ASP ARG ARG LEU TYR
SEQRES 5 C 317 GLU THR MET LEU GLY SER MET PRO LEU ASP ASP ASP ILE
SEQRES 6 C 317 GLN THR GLU ARG LEU GLY VAL ASN GLY VAL PRO ALA GLU
SEQRES 7 C 317 TRP ILE TYR ALA PRO GLY ALA ARG ASP ASP GLN VAL PHE
SEQRES 8 C 317 LEU TYR LEU HIS GLY GLY GLY TYR VAL ILE GLY SER MET
SEQRES 9 C 317 ARG THR HIS ARG VAL MET LEU SER HIS ILE ALA ARG ALA
SEQRES 10 C 317 ALA GLY CYS ARG VAL LEU GLY LEU ASP TYR ARG LEU ALA
SEQRES 11 C 317 PRO GLU THR PRO PHE PRO ALA PRO VAL GLU ASP THR VAL
SEQRES 12 C 317 ALA ALA TYR ARG TRP LEU LEU ALA HIS GLY TYR ASP PRO
SEQRES 13 C 317 SER ARG ILE ALA LEU GLY GLY ASP SER ALA GLY GLY GLY
SEQRES 14 C 317 LEU VAL VAL ALA ALA LEU VAL ALA LEU ARG TYR ILE GLY
SEQRES 15 C 317 GLU PRO LEU PRO ALA ALA GLY VAL CYS LEU SER PRO TRP
SEQRES 16 C 317 ILE ASP MET GLU ALA THR GLY GLU SER PHE THR THR ASN
SEQRES 17 C 317 ALA THR MET ASP PRO SER VAL ASN LYS GLU ARG VAL MET
SEQRES 18 C 317 SER ILE ALA ALA LEU TYR LEU GLY GLY LYS ASN PRO GLN
SEQRES 19 C 317 ALA PRO LEU ALA SER PRO LEU TYR ALA ASP LEU GLN GLY
SEQRES 20 C 317 LEU PRO PRO LEU LEU VAL GLN VAL GLY GLY ILE GLU THR
SEQRES 21 C 317 LEU LEU ASP ASP ALA ARG ALA LEU THR THR ARG ALA LYS
SEQRES 22 C 317 ALA ALA GLY VAL ASP ALA ASP LEU GLU VAL TRP ASP ASP
SEQRES 23 C 317 MET PRO HIS VAL TRP GLN HIS PHE ALA PRO ILE LEU PRO
SEQRES 24 C 317 GLU GLY LYS GLN ALA ILE ALA ARG ILE GLY GLU PHE LEU
SEQRES 25 C 317 ARG LYS GLN ILE GLY
SEQRES 1 D 317 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 317 LEU VAL PRO ARG GLY SER HIS MET ALA LYS SER PRO GLU
SEQRES 3 D 317 LEU ASP ARG VAL ILE GLY MET ILE ARG GLU ARG ALA ALA
SEQRES 4 D 317 THR PRO ARG LYS THR THR ASP ASP ASP ARG ARG LEU TYR
SEQRES 5 D 317 GLU THR MET LEU GLY SER MET PRO LEU ASP ASP ASP ILE
SEQRES 6 D 317 GLN THR GLU ARG LEU GLY VAL ASN GLY VAL PRO ALA GLU
SEQRES 7 D 317 TRP ILE TYR ALA PRO GLY ALA ARG ASP ASP GLN VAL PHE
SEQRES 8 D 317 LEU TYR LEU HIS GLY GLY GLY TYR VAL ILE GLY SER MET
SEQRES 9 D 317 ARG THR HIS ARG VAL MET LEU SER HIS ILE ALA ARG ALA
SEQRES 10 D 317 ALA GLY CYS ARG VAL LEU GLY LEU ASP TYR ARG LEU ALA
SEQRES 11 D 317 PRO GLU THR PRO PHE PRO ALA PRO VAL GLU ASP THR VAL
SEQRES 12 D 317 ALA ALA TYR ARG TRP LEU LEU ALA HIS GLY TYR ASP PRO
SEQRES 13 D 317 SER ARG ILE ALA LEU GLY GLY ASP SER ALA GLY GLY GLY
SEQRES 14 D 317 LEU VAL VAL ALA ALA LEU VAL ALA LEU ARG TYR ILE GLY
SEQRES 15 D 317 GLU PRO LEU PRO ALA ALA GLY VAL CYS LEU SER PRO TRP
SEQRES 16 D 317 ILE ASP MET GLU ALA THR GLY GLU SER PHE THR THR ASN
SEQRES 17 D 317 ALA THR MET ASP PRO SER VAL ASN LYS GLU ARG VAL MET
SEQRES 18 D 317 SER ILE ALA ALA LEU TYR LEU GLY GLY LYS ASN PRO GLN
SEQRES 19 D 317 ALA PRO LEU ALA SER PRO LEU TYR ALA ASP LEU GLN GLY
SEQRES 20 D 317 LEU PRO PRO LEU LEU VAL GLN VAL GLY GLY ILE GLU THR
SEQRES 21 D 317 LEU LEU ASP ASP ALA ARG ALA LEU THR THR ARG ALA LYS
SEQRES 22 D 317 ALA ALA GLY VAL ASP ALA ASP LEU GLU VAL TRP ASP ASP
SEQRES 23 D 317 MET PRO HIS VAL TRP GLN HIS PHE ALA PRO ILE LEU PRO
SEQRES 24 D 317 GLU GLY LYS GLN ALA ILE ALA ARG ILE GLY GLU PHE LEU
SEQRES 25 D 317 ARG LYS GLN ILE GLY
SEQRES 1 E 317 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 E 317 LEU VAL PRO ARG GLY SER HIS MET ALA LYS SER PRO GLU
SEQRES 3 E 317 LEU ASP ARG VAL ILE GLY MET ILE ARG GLU ARG ALA ALA
SEQRES 4 E 317 THR PRO ARG LYS THR THR ASP ASP ASP ARG ARG LEU TYR
SEQRES 5 E 317 GLU THR MET LEU GLY SER MET PRO LEU ASP ASP ASP ILE
SEQRES 6 E 317 GLN THR GLU ARG LEU GLY VAL ASN GLY VAL PRO ALA GLU
SEQRES 7 E 317 TRP ILE TYR ALA PRO GLY ALA ARG ASP ASP GLN VAL PHE
SEQRES 8 E 317 LEU TYR LEU HIS GLY GLY GLY TYR VAL ILE GLY SER MET
SEQRES 9 E 317 ARG THR HIS ARG VAL MET LEU SER HIS ILE ALA ARG ALA
SEQRES 10 E 317 ALA GLY CYS ARG VAL LEU GLY LEU ASP TYR ARG LEU ALA
SEQRES 11 E 317 PRO GLU THR PRO PHE PRO ALA PRO VAL GLU ASP THR VAL
SEQRES 12 E 317 ALA ALA TYR ARG TRP LEU LEU ALA HIS GLY TYR ASP PRO
SEQRES 13 E 317 SER ARG ILE ALA LEU GLY GLY ASP SER ALA GLY GLY GLY
SEQRES 14 E 317 LEU VAL VAL ALA ALA LEU VAL ALA LEU ARG TYR ILE GLY
SEQRES 15 E 317 GLU PRO LEU PRO ALA ALA GLY VAL CYS LEU SER PRO TRP
SEQRES 16 E 317 ILE ASP MET GLU ALA THR GLY GLU SER PHE THR THR ASN
SEQRES 17 E 317 ALA THR MET ASP PRO SER VAL ASN LYS GLU ARG VAL MET
SEQRES 18 E 317 SER ILE ALA ALA LEU TYR LEU GLY GLY LYS ASN PRO GLN
SEQRES 19 E 317 ALA PRO LEU ALA SER PRO LEU TYR ALA ASP LEU GLN GLY
SEQRES 20 E 317 LEU PRO PRO LEU LEU VAL GLN VAL GLY GLY ILE GLU THR
SEQRES 21 E 317 LEU LEU ASP ASP ALA ARG ALA LEU THR THR ARG ALA LYS
SEQRES 22 E 317 ALA ALA GLY VAL ASP ALA ASP LEU GLU VAL TRP ASP ASP
SEQRES 23 E 317 MET PRO HIS VAL TRP GLN HIS PHE ALA PRO ILE LEU PRO
SEQRES 24 E 317 GLU GLY LYS GLN ALA ILE ALA ARG ILE GLY GLU PHE LEU
SEQRES 25 E 317 ARG LYS GLN ILE GLY
SEQRES 1 F 317 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 F 317 LEU VAL PRO ARG GLY SER HIS MET ALA LYS SER PRO GLU
SEQRES 3 F 317 LEU ASP ARG VAL ILE GLY MET ILE ARG GLU ARG ALA ALA
SEQRES 4 F 317 THR PRO ARG LYS THR THR ASP ASP ASP ARG ARG LEU TYR
SEQRES 5 F 317 GLU THR MET LEU GLY SER MET PRO LEU ASP ASP ASP ILE
SEQRES 6 F 317 GLN THR GLU ARG LEU GLY VAL ASN GLY VAL PRO ALA GLU
SEQRES 7 F 317 TRP ILE TYR ALA PRO GLY ALA ARG ASP ASP GLN VAL PHE
SEQRES 8 F 317 LEU TYR LEU HIS GLY GLY GLY TYR VAL ILE GLY SER MET
SEQRES 9 F 317 ARG THR HIS ARG VAL MET LEU SER HIS ILE ALA ARG ALA
SEQRES 10 F 317 ALA GLY CYS ARG VAL LEU GLY LEU ASP TYR ARG LEU ALA
SEQRES 11 F 317 PRO GLU THR PRO PHE PRO ALA PRO VAL GLU ASP THR VAL
SEQRES 12 F 317 ALA ALA TYR ARG TRP LEU LEU ALA HIS GLY TYR ASP PRO
SEQRES 13 F 317 SER ARG ILE ALA LEU GLY GLY ASP SER ALA GLY GLY GLY
SEQRES 14 F 317 LEU VAL VAL ALA ALA LEU VAL ALA LEU ARG TYR ILE GLY
SEQRES 15 F 317 GLU PRO LEU PRO ALA ALA GLY VAL CYS LEU SER PRO TRP
SEQRES 16 F 317 ILE ASP MET GLU ALA THR GLY GLU SER PHE THR THR ASN
SEQRES 17 F 317 ALA THR MET ASP PRO SER VAL ASN LYS GLU ARG VAL MET
SEQRES 18 F 317 SER ILE ALA ALA LEU TYR LEU GLY GLY LYS ASN PRO GLN
SEQRES 19 F 317 ALA PRO LEU ALA SER PRO LEU TYR ALA ASP LEU GLN GLY
SEQRES 20 F 317 LEU PRO PRO LEU LEU VAL GLN VAL GLY GLY ILE GLU THR
SEQRES 21 F 317 LEU LEU ASP ASP ALA ARG ALA LEU THR THR ARG ALA LYS
SEQRES 22 F 317 ALA ALA GLY VAL ASP ALA ASP LEU GLU VAL TRP ASP ASP
SEQRES 23 F 317 MET PRO HIS VAL TRP GLN HIS PHE ALA PRO ILE LEU PRO
SEQRES 24 F 317 GLU GLY LYS GLN ALA ILE ALA ARG ILE GLY GLU PHE LEU
SEQRES 25 F 317 ARG LYS GLN ILE GLY
SEQRES 1 G 317 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 G 317 LEU VAL PRO ARG GLY SER HIS MET ALA LYS SER PRO GLU
SEQRES 3 G 317 LEU ASP ARG VAL ILE GLY MET ILE ARG GLU ARG ALA ALA
SEQRES 4 G 317 THR PRO ARG LYS THR THR ASP ASP ASP ARG ARG LEU TYR
SEQRES 5 G 317 GLU THR MET LEU GLY SER MET PRO LEU ASP ASP ASP ILE
SEQRES 6 G 317 GLN THR GLU ARG LEU GLY VAL ASN GLY VAL PRO ALA GLU
SEQRES 7 G 317 TRP ILE TYR ALA PRO GLY ALA ARG ASP ASP GLN VAL PHE
SEQRES 8 G 317 LEU TYR LEU HIS GLY GLY GLY TYR VAL ILE GLY SER MET
SEQRES 9 G 317 ARG THR HIS ARG VAL MET LEU SER HIS ILE ALA ARG ALA
SEQRES 10 G 317 ALA GLY CYS ARG VAL LEU GLY LEU ASP TYR ARG LEU ALA
SEQRES 11 G 317 PRO GLU THR PRO PHE PRO ALA PRO VAL GLU ASP THR VAL
SEQRES 12 G 317 ALA ALA TYR ARG TRP LEU LEU ALA HIS GLY TYR ASP PRO
SEQRES 13 G 317 SER ARG ILE ALA LEU GLY GLY ASP SER ALA GLY GLY GLY
SEQRES 14 G 317 LEU VAL VAL ALA ALA LEU VAL ALA LEU ARG TYR ILE GLY
SEQRES 15 G 317 GLU PRO LEU PRO ALA ALA GLY VAL CYS LEU SER PRO TRP
SEQRES 16 G 317 ILE ASP MET GLU ALA THR GLY GLU SER PHE THR THR ASN
SEQRES 17 G 317 ALA THR MET ASP PRO SER VAL ASN LYS GLU ARG VAL MET
SEQRES 18 G 317 SER ILE ALA ALA LEU TYR LEU GLY GLY LYS ASN PRO GLN
SEQRES 19 G 317 ALA PRO LEU ALA SER PRO LEU TYR ALA ASP LEU GLN GLY
SEQRES 20 G 317 LEU PRO PRO LEU LEU VAL GLN VAL GLY GLY ILE GLU THR
SEQRES 21 G 317 LEU LEU ASP ASP ALA ARG ALA LEU THR THR ARG ALA LYS
SEQRES 22 G 317 ALA ALA GLY VAL ASP ALA ASP LEU GLU VAL TRP ASP ASP
SEQRES 23 G 317 MET PRO HIS VAL TRP GLN HIS PHE ALA PRO ILE LEU PRO
SEQRES 24 G 317 GLU GLY LYS GLN ALA ILE ALA ARG ILE GLY GLU PHE LEU
SEQRES 25 G 317 ARG LYS GLN ILE GLY
SEQRES 1 H 317 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 H 317 LEU VAL PRO ARG GLY SER HIS MET ALA LYS SER PRO GLU
SEQRES 3 H 317 LEU ASP ARG VAL ILE GLY MET ILE ARG GLU ARG ALA ALA
SEQRES 4 H 317 THR PRO ARG LYS THR THR ASP ASP ASP ARG ARG LEU TYR
SEQRES 5 H 317 GLU THR MET LEU GLY SER MET PRO LEU ASP ASP ASP ILE
SEQRES 6 H 317 GLN THR GLU ARG LEU GLY VAL ASN GLY VAL PRO ALA GLU
SEQRES 7 H 317 TRP ILE TYR ALA PRO GLY ALA ARG ASP ASP GLN VAL PHE
SEQRES 8 H 317 LEU TYR LEU HIS GLY GLY GLY TYR VAL ILE GLY SER MET
SEQRES 9 H 317 ARG THR HIS ARG VAL MET LEU SER HIS ILE ALA ARG ALA
SEQRES 10 H 317 ALA GLY CYS ARG VAL LEU GLY LEU ASP TYR ARG LEU ALA
SEQRES 11 H 317 PRO GLU THR PRO PHE PRO ALA PRO VAL GLU ASP THR VAL
SEQRES 12 H 317 ALA ALA TYR ARG TRP LEU LEU ALA HIS GLY TYR ASP PRO
SEQRES 13 H 317 SER ARG ILE ALA LEU GLY GLY ASP SER ALA GLY GLY GLY
SEQRES 14 H 317 LEU VAL VAL ALA ALA LEU VAL ALA LEU ARG TYR ILE GLY
SEQRES 15 H 317 GLU PRO LEU PRO ALA ALA GLY VAL CYS LEU SER PRO TRP
SEQRES 16 H 317 ILE ASP MET GLU ALA THR GLY GLU SER PHE THR THR ASN
SEQRES 17 H 317 ALA THR MET ASP PRO SER VAL ASN LYS GLU ARG VAL MET
SEQRES 18 H 317 SER ILE ALA ALA LEU TYR LEU GLY GLY LYS ASN PRO GLN
SEQRES 19 H 317 ALA PRO LEU ALA SER PRO LEU TYR ALA ASP LEU GLN GLY
SEQRES 20 H 317 LEU PRO PRO LEU LEU VAL GLN VAL GLY GLY ILE GLU THR
SEQRES 21 H 317 LEU LEU ASP ASP ALA ARG ALA LEU THR THR ARG ALA LYS
SEQRES 22 H 317 ALA ALA GLY VAL ASP ALA ASP LEU GLU VAL TRP ASP ASP
SEQRES 23 H 317 MET PRO HIS VAL TRP GLN HIS PHE ALA PRO ILE LEU PRO
SEQRES 24 H 317 GLU GLY LYS GLN ALA ILE ALA ARG ILE GLY GLU PHE LEU
SEQRES 25 H 317 ARG LYS GLN ILE GLY
HET PMS A 301 10
HET PMS B 301 10
HET PMS C 301 10
HET PMS D 301 10
HET PMS E 301 10
HET PMS F 301 10
HET PMS G 301 10
HET PMS H 301 10
HETNAM PMS PHENYLMETHANESULFONIC ACID
FORMUL 9 PMS 8(C7 H8 O3 S)
FORMUL 17 HOH *1993(H2 O)
HELIX 1 AA1 SER A 4 THR A 20 1 17
HELIX 2 AA2 THR A 24 GLY A 37 1 14
HELIX 3 AA3 SER A 83 GLY A 99 1 17
HELIX 4 AA4 PRO A 116 HIS A 132 1 17
HELIX 5 AA5 ASP A 135 SER A 137 5 3
HELIX 6 AA6 SER A 145 ILE A 161 1 17
HELIX 7 AA7 GLU A 183 ASN A 188 1 6
HELIX 8 AA8 ASN A 196 GLY A 209 1 14
HELIX 9 AA9 SER A 219 ALA A 223 5 5
HELIX 10 AB1 LEU A 241 ALA A 255 1 15
HELIX 11 AB2 VAL A 270 ALA A 275 5 6
HELIX 12 AB3 LEU A 278 GLY A 297 1 20
HELIX 13 AB4 SER B 4 THR B 20 1 17
HELIX 14 AB5 THR B 24 GLY B 37 1 14
HELIX 15 AB6 SER B 83 GLY B 99 1 17
HELIX 16 AB7 PRO B 116 HIS B 132 1 17
HELIX 17 AB8 ASP B 135 SER B 137 5 3
HELIX 18 AB9 SER B 145 ILE B 161 1 17
HELIX 19 AC1 GLU B 183 ASN B 188 1 6
HELIX 20 AC2 ASN B 196 GLY B 209 1 14
HELIX 21 AC3 SER B 219 ALA B 223 5 5
HELIX 22 AC4 LEU B 241 ALA B 255 1 15
HELIX 23 AC5 VAL B 270 ALA B 275 5 6
HELIX 24 AC6 LEU B 278 GLY B 297 1 20
HELIX 25 AC7 SER C 4 THR C 20 1 17
HELIX 26 AC8 THR C 24 GLY C 37 1 14
HELIX 27 AC9 SER C 83 GLY C 99 1 17
HELIX 28 AD1 PRO C 116 HIS C 132 1 17
HELIX 29 AD2 ASP C 135 SER C 137 5 3
HELIX 30 AD3 SER C 145 ILE C 161 1 17
HELIX 31 AD4 GLU C 183 ASN C 188 1 6
HELIX 32 AD5 ASN C 196 GLY C 209 1 14
HELIX 33 AD6 SER C 219 ALA C 223 5 5
HELIX 34 AD7 LEU C 241 ALA C 255 1 15
HELIX 35 AD8 VAL C 270 ALA C 275 5 6
HELIX 36 AD9 LEU C 278 GLY C 297 1 20
HELIX 37 AE1 SER D 4 THR D 20 1 17
HELIX 38 AE2 THR D 24 GLY D 37 1 14
HELIX 39 AE3 SER D 83 GLY D 99 1 17
HELIX 40 AE4 PRO D 116 HIS D 132 1 17
HELIX 41 AE5 ASP D 135 SER D 137 5 3
HELIX 42 AE6 SER D 145 ILE D 161 1 17
HELIX 43 AE7 GLU D 183 ASN D 188 1 6
HELIX 44 AE8 ASN D 196 GLY D 209 1 14
HELIX 45 AE9 SER D 219 ALA D 223 5 5
HELIX 46 AF1 LEU D 241 ALA D 255 1 15
HELIX 47 AF2 VAL D 270 ALA D 275 5 6
HELIX 48 AF3 LEU D 278 ILE D 296 1 19
HELIX 49 AF4 SER E 4 THR E 20 1 17
HELIX 50 AF5 THR E 24 GLY E 37 1 14
HELIX 51 AF6 SER E 83 GLY E 99 1 17
HELIX 52 AF7 PRO E 116 HIS E 132 1 17
HELIX 53 AF8 ASP E 135 SER E 137 5 3
HELIX 54 AF9 SER E 145 ILE E 161 1 17
HELIX 55 AG1 GLU E 183 ASN E 188 1 6
HELIX 56 AG2 ASN E 196 GLY E 209 1 14
HELIX 57 AG3 SER E 219 ALA E 223 5 5
HELIX 58 AG4 LEU E 241 ALA E 255 1 15
HELIX 59 AG5 VAL E 270 ALA E 275 5 6
HELIX 60 AG6 LEU E 278 GLY E 297 1 20
HELIX 61 AG7 SER F 4 THR F 20 1 17
HELIX 62 AG8 THR F 24 GLY F 37 1 14
HELIX 63 AG9 SER F 83 GLY F 99 1 17
HELIX 64 AH1 PRO F 116 HIS F 132 1 17
HELIX 65 AH2 ASP F 135 SER F 137 5 3
HELIX 66 AH3 SER F 145 ILE F 161 1 17
HELIX 67 AH4 GLU F 183 ASN F 188 1 6
HELIX 68 AH5 ASN F 196 GLY F 209 1 14
HELIX 69 AH6 SER F 219 ALA F 223 5 5
HELIX 70 AH7 LEU F 241 ALA F 255 1 15
HELIX 71 AH8 VAL F 270 ALA F 275 5 6
HELIX 72 AH9 LEU F 278 GLY F 297 1 20
HELIX 73 AI1 SER G 4 THR G 20 1 17
HELIX 74 AI2 THR G 24 GLY G 37 1 14
HELIX 75 AI3 SER G 83 GLY G 99 1 17
HELIX 76 AI4 PRO G 116 HIS G 132 1 17
HELIX 77 AI5 ASP G 135 SER G 137 5 3
HELIX 78 AI6 SER G 145 ILE G 161 1 17
HELIX 79 AI7 GLU G 183 ASN G 188 1 6
HELIX 80 AI8 ASN G 196 GLY G 209 1 14
HELIX 81 AI9 SER G 219 ALA G 223 5 5
HELIX 82 AJ1 LEU G 241 ALA G 255 1 15
HELIX 83 AJ2 VAL G 270 ALA G 275 5 6
HELIX 84 AJ3 LEU G 278 GLY G 297 1 20
HELIX 85 AJ4 SER H 4 THR H 20 1 17
HELIX 86 AJ5 THR H 24 GLY H 37 1 14
HELIX 87 AJ6 SER H 83 GLY H 99 1 17
HELIX 88 AJ7 PRO H 116 HIS H 132 1 17
HELIX 89 AJ8 ASP H 135 SER H 137 5 3
HELIX 90 AJ9 SER H 145 ILE H 161 1 17
HELIX 91 AK1 GLU H 183 ASN H 188 1 6
HELIX 92 AK2 ASN H 196 GLY H 209 1 14
HELIX 93 AK3 SER H 219 ALA H 223 5 5
HELIX 94 AK4 LEU H 241 ALA H 255 1 15
HELIX 95 AK5 VAL H 270 ALA H 275 5 6
HELIX 96 AK6 LEU H 278 ILE H 296 1 19
SHEET 1 AA1 8 GLN A 46 VAL A 52 0
SHEET 2 AA1 8 VAL A 55 TYR A 61 -1 O TYR A 61 N GLN A 46
SHEET 3 AA1 8 CYS A 100 LEU A 105 -1 O VAL A 102 N ILE A 60
SHEET 4 AA1 8 ARG A 66 LEU A 74 1 N TYR A 73 O LEU A 103
SHEET 5 AA1 8 ILE A 139 ASP A 144 1 O ALA A 140 N LEU A 72
SHEET 6 AA1 8 ALA A 168 LEU A 172 1 O LEU A 172 N GLY A 143
SHEET 7 AA1 8 LEU A 231 GLY A 236 1 O LEU A 232 N CYS A 171
SHEET 8 AA1 8 ALA A 259 TRP A 264 1 O ASP A 260 N VAL A 233
SHEET 1 AA2 8 GLN B 46 VAL B 52 0
SHEET 2 AA2 8 VAL B 55 TYR B 61 -1 O TYR B 61 N GLN B 46
SHEET 3 AA2 8 CYS B 100 LEU B 105 -1 O VAL B 102 N ILE B 60
SHEET 4 AA2 8 ARG B 66 LEU B 74 1 N TYR B 73 O LEU B 103
SHEET 5 AA2 8 ILE B 139 ASP B 144 1 O GLY B 142 N LEU B 74
SHEET 6 AA2 8 ALA B 168 LEU B 172 1 O LEU B 172 N GLY B 143
SHEET 7 AA2 8 LEU B 231 GLY B 236 1 O LEU B 232 N CYS B 171
SHEET 8 AA2 8 ALA B 259 TRP B 264 1 O TRP B 264 N VAL B 235
SHEET 1 AA3 8 GLN C 46 VAL C 52 0
SHEET 2 AA3 8 VAL C 55 TYR C 61 -1 O TYR C 61 N GLN C 46
SHEET 3 AA3 8 CYS C 100 LEU C 105 -1 O VAL C 102 N ILE C 60
SHEET 4 AA3 8 ARG C 66 LEU C 74 1 N TYR C 73 O LEU C 103
SHEET 5 AA3 8 ILE C 139 ASP C 144 1 O ALA C 140 N LEU C 72
SHEET 6 AA3 8 ALA C 168 LEU C 172 1 O LEU C 172 N GLY C 143
SHEET 7 AA3 8 LEU C 231 GLY C 236 1 O LEU C 232 N CYS C 171
SHEET 8 AA3 8 ALA C 259 TRP C 264 1 O ASP C 260 N VAL C 233
SHEET 1 AA4 8 GLN D 46 VAL D 52 0
SHEET 2 AA4 8 VAL D 55 TYR D 61 -1 O TYR D 61 N GLN D 46
SHEET 3 AA4 8 CYS D 100 LEU D 105 -1 O VAL D 102 N ILE D 60
SHEET 4 AA4 8 ARG D 66 LEU D 74 1 N TYR D 73 O LEU D 103
SHEET 5 AA4 8 ILE D 139 ASP D 144 1 O GLY D 142 N LEU D 74
SHEET 6 AA4 8 ALA D 168 LEU D 172 1 O LEU D 172 N GLY D 143
SHEET 7 AA4 8 LEU D 231 GLY D 236 1 O LEU D 232 N CYS D 171
SHEET 8 AA4 8 ALA D 259 TRP D 264 1 O TRP D 264 N VAL D 235
SHEET 1 AA5 8 GLN E 46 VAL E 52 0
SHEET 2 AA5 8 VAL E 55 TYR E 61 -1 O TYR E 61 N GLN E 46
SHEET 3 AA5 8 CYS E 100 LEU E 105 -1 O VAL E 102 N ILE E 60
SHEET 4 AA5 8 ARG E 66 LEU E 74 1 N TYR E 73 O LEU E 103
SHEET 5 AA5 8 ILE E 139 ASP E 144 1 O GLY E 142 N LEU E 74
SHEET 6 AA5 8 ALA E 168 LEU E 172 1 O LEU E 172 N GLY E 143
SHEET 7 AA5 8 LEU E 231 GLY E 236 1 O LEU E 232 N CYS E 171
SHEET 8 AA5 8 ALA E 259 TRP E 264 1 O ASP E 260 N VAL E 233
SHEET 1 AA6 8 GLN F 46 VAL F 52 0
SHEET 2 AA6 8 VAL F 55 TYR F 61 -1 O TYR F 61 N GLN F 46
SHEET 3 AA6 8 CYS F 100 LEU F 105 -1 O VAL F 102 N ILE F 60
SHEET 4 AA6 8 ARG F 66 LEU F 74 1 N PHE F 71 O LEU F 103
SHEET 5 AA6 8 ILE F 139 ASP F 144 1 O ALA F 140 N LEU F 72
SHEET 6 AA6 8 ALA F 168 LEU F 172 1 O LEU F 172 N GLY F 143
SHEET 7 AA6 8 LEU F 231 GLY F 236 1 O LEU F 232 N CYS F 171
SHEET 8 AA6 8 ALA F 259 TRP F 264 1 O ASP F 260 N VAL F 233
SHEET 1 AA7 8 GLN G 46 VAL G 52 0
SHEET 2 AA7 8 VAL G 55 TYR G 61 -1 O TYR G 61 N GLN G 46
SHEET 3 AA7 8 CYS G 100 LEU G 105 -1 O VAL G 102 N ILE G 60
SHEET 4 AA7 8 ARG G 66 LEU G 74 1 N PHE G 71 O LEU G 103
SHEET 5 AA7 8 ILE G 139 ASP G 144 1 O ALA G 140 N LEU G 72
SHEET 6 AA7 8 ALA G 168 LEU G 172 1 O LEU G 172 N GLY G 143
SHEET 7 AA7 8 LEU G 231 GLY G 236 1 O LEU G 232 N CYS G 171
SHEET 8 AA7 8 ALA G 259 TRP G 264 1 O ASP G 260 N VAL G 233
SHEET 1 AA8 8 GLN H 46 VAL H 52 0
SHEET 2 AA8 8 VAL H 55 TYR H 61 -1 O TYR H 61 N GLN H 46
SHEET 3 AA8 8 CYS H 100 LEU H 105 -1 O VAL H 102 N ILE H 60
SHEET 4 AA8 8 ARG H 66 LEU H 74 1 N TYR H 73 O LEU H 103
SHEET 5 AA8 8 ILE H 139 ASP H 144 1 O GLY H 142 N LEU H 74
SHEET 6 AA8 8 ALA H 168 LEU H 172 1 O LEU H 172 N GLY H 143
SHEET 7 AA8 8 LEU H 231 GLY H 236 1 O LEU H 232 N CYS H 171
SHEET 8 AA8 8 ALA H 259 TRP H 264 1 O ASP H 260 N VAL H 233
LINK CB SER A 145 S PMS A 301 1555 1555 1.96
LINK CB SER B 145 S PMS B 301 1555 1555 1.98
CISPEP 1 ALA A 110 PRO A 111 0 4.50
CISPEP 2 PHE A 115 PRO A 116 0 0.30
CISPEP 3 ALA B 110 PRO B 111 0 3.82
CISPEP 4 PHE B 115 PRO B 116 0 1.30
CISPEP 5 ALA C 110 PRO C 111 0 3.74
CISPEP 6 PHE C 115 PRO C 116 0 2.07
CISPEP 7 MET D 1 ALA D 2 0 -7.45
CISPEP 8 ALA D 110 PRO D 111 0 4.06
CISPEP 9 PHE D 115 PRO D 116 0 2.81
CISPEP 10 ALA E 110 PRO E 111 0 4.86
CISPEP 11 PHE E 115 PRO E 116 0 2.78
CISPEP 12 ALA F 110 PRO F 111 0 4.26
CISPEP 13 PHE F 115 PRO F 116 0 0.65
CISPEP 14 ALA G 110 PRO G 111 0 4.55
CISPEP 15 PHE G 115 PRO G 116 0 1.95
CISPEP 16 ALA H 110 PRO H 111 0 3.40
CISPEP 17 PHE H 115 PRO H 116 0 2.71
SITE 1 AC1 8 GLY A 77 GLY A 78 SER A 145 ALA A 146
SITE 2 AC1 8 TRP A 175 ILE A 203 HIS A 269 HOH A 547
SITE 1 AC2 6 GLY C 77 GLY C 78 SER C 145 ALA C 146
SITE 2 AC2 6 HIS C 269 HOH C 503
SITE 1 AC3 7 GLY D 77 GLY D 78 SER D 145 ALA D 146
SITE 2 AC3 7 TRP D 175 HIS D 269 HOH D 597
SITE 1 AC4 8 ARG E 17 GLY E 77 GLY E 78 SER E 145
SITE 2 AC4 8 ALA E 146 HIS E 269 HOH E 603 HOH E 635
SITE 1 AC5 8 GLY F 76 GLY F 77 GLY F 78 SER F 145
SITE 2 AC5 8 ALA F 146 VAL F 200 HIS F 269 HOH F 536
SITE 1 AC6 7 GLY G 77 GLY G 78 SER G 145 ALA G 146
SITE 2 AC6 7 TRP G 175 ILE G 203 HIS G 269
SITE 1 AC7 7 GLY H 77 GLY H 78 SER H 145 ALA H 146
SITE 2 AC7 7 TRP H 175 ILE H 203 HIS H 269
SITE 1 AC8 16 GLY B 76 GLY B 77 GLY B 78 ASP B 144
SITE 2 AC8 16 ALA B 146 GLY B 147 GLY B 148 GLY B 149
SITE 3 AC8 16 LEU B 172 SER B 173 PRO B 174 TRP B 175
SITE 4 AC8 16 ILE B 203 HIS B 269 HOH B2182 HOH B2209
CRYST1 74.630 76.172 130.186 74.04 75.15 72.60 P 1
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 0.013399 -0.004199 -0.002713 0.00000
SCALE2 0.000000 0.013758 -0.003030 0.00000
SCALE3 0.000000 0.000000 0.008137 0.00000
TER 2278 GLY A 297
TER 4562 GLY B 297
TER 6825 GLY C 297
TER 9095 GLY D 297
TER 11359 GLY E 297
TER 13631 GLY F 297
TER 15888 GLY G 297
TER 18145 GLY H 297
MASTER 654 0 8 96 64 0 18 620121 8 82 200
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