HEADER OXIDOREDUCTASE 26-NOV-13 4NQZ
TITLE CRYSTAL STRUCTURE OF THE PSEUDOMONAS AERUGINOSA ENOYL-ACYL CARRIER
TITLE 2 PROTEIN REDUCTASE (FABI) IN APO FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE [NADH] FABI;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P;
COMPND 4 SYNONYM: ENR, NADH-DEPENDENT ENOYL-ACP REDUCTASE;
COMPND 5 EC: 1.3.1.9;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 208964;
SOURCE 4 STRAIN: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;
SOURCE 5 GENE: FABI, PA1806;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS ROSSMANN FOLD MOTIF, REDUCTASE, CYTOSOL, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.M.CHI,J.H.LEE,A.K.PARK
REVDAT 3 08-NOV-23 4NQZ 1 SEQADV
REVDAT 2 06-MAY-15 4NQZ 1 JRNL
REVDAT 1 26-NOV-14 4NQZ 0
JRNL AUTH J.H.LEE,A.K.PARK,Y.M.CHI,S.W.JEONG
JRNL TITL CRYSTAL STRUCTURES OF PSEUDOMONAS AERUGINOSA ENOYL-ACP
JRNL TITL 2 REDUCTASE (FABI) IN THE PRESENCE AND ABSENCE OF NAD+ AND
JRNL TITL 3 TRICLOSAN
JRNL REF BULL.KOREAN CHEM.SOC. V. 36 322 2015
JRNL REFN ISSN 0253-2964
JRNL DOI 10.1002/BKCS.10084
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.4_1496
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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.39
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.480
REMARK 3 COMPLETENESS FOR RANGE (%) : 84.7
REMARK 3 NUMBER OF REFLECTIONS : 112296
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.286
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 5660
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 44.4009 - 8.0770 0.96 4131 226 0.1521 0.1971
REMARK 3 2 8.0770 - 6.4172 0.97 4157 201 0.1480 0.2387
REMARK 3 3 6.4172 - 5.6078 0.96 4044 224 0.1666 0.2644
REMARK 3 4 5.6078 - 5.0959 0.97 4099 200 0.1520 0.2391
REMARK 3 5 5.0959 - 4.7311 0.97 4102 203 0.1569 0.2317
REMARK 3 6 4.7311 - 4.4524 0.97 4038 220 0.1420 0.2182
REMARK 3 7 4.4524 - 4.2296 0.97 4073 232 0.1473 0.2372
REMARK 3 8 4.2296 - 4.0456 0.95 3952 220 0.1703 0.2689
REMARK 3 9 4.0456 - 3.8900 0.93 3892 213 0.1776 0.2754
REMARK 3 10 3.8900 - 3.7558 0.94 3970 206 0.1824 0.2792
REMARK 3 11 3.7558 - 3.6384 0.89 3745 187 0.2001 0.3051
REMARK 3 12 3.6384 - 3.5345 0.83 3465 202 0.2172 0.3309
REMARK 3 13 3.5345 - 3.4415 0.91 3810 201 0.2178 0.2945
REMARK 3 14 3.4415 - 3.3575 0.89 3747 190 0.2205 0.3175
REMARK 3 15 3.3575 - 3.2812 0.89 3706 213 0.2200 0.3125
REMARK 3 16 3.2812 - 3.2114 0.87 3637 191 0.2360 0.3551
REMARK 3 17 3.2114 - 3.1472 0.86 3588 207 0.2425 0.3315
REMARK 3 18 3.1472 - 3.0878 0.84 3472 191 0.2478 0.3375
REMARK 3 19 3.0878 - 3.0327 0.82 3472 185 0.2529 0.3297
REMARK 3 20 3.0327 - 2.9813 0.81 3394 178 0.2504 0.3498
REMARK 3 21 2.9813 - 2.9332 0.79 3297 181 0.2503 0.3379
REMARK 3 22 2.9332 - 2.8881 0.78 3256 180 0.2667 0.4101
REMARK 3 23 2.8881 - 2.8456 0.75 3111 174 0.2695 0.3571
REMARK 3 24 2.8456 - 2.8055 0.73 3080 165 0.2909 0.4144
REMARK 3 25 2.8055 - 2.7676 0.72 3026 163 0.3064 0.3848
REMARK 3 26 2.7676 - 2.7317 0.71 2936 157 0.3143 0.4152
REMARK 3 27 2.7317 - 2.6976 0.70 2922 155 0.3065 0.3913
REMARK 3 28 2.6976 - 2.6651 0.70 2956 131 0.2981 0.4208
REMARK 3 29 2.6651 - 2.6341 0.69 2913 141 0.3153 0.3664
REMARK 3 30 2.6341 - 2.6045 0.63 2645 123 0.3171 0.3767
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) : 0.560
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.710
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 37.74
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.21
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 : 0.009 29571
REMARK 3 ANGLE : 1.237 39897
REMARK 3 CHIRALITY : 0.045 4438
REMARK 3 PLANARITY : 0.005 5264
REMARK 3 DIHEDRAL : 14.100 10560
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 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4NQZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-DEC-13.
REMARK 100 THE DEPOSITION ID IS D_1000083546.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-DEC-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : SI (111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 112296
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 84.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
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) : 2.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 67.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> 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: PHENIX
REMARK 200 STARTING MODEL: 1C14
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 6% TACSIMATE, 8% PEG 3350, PH 5.0,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
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 77.92200
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, 4
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13740 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -80.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13820 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32030 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -81.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -69.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J, K, L
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32920 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, N, O, P
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 LEU A 198
REMARK 465 ALA A 199
REMARK 465 ALA A 200
REMARK 465 SER A 201
REMARK 465 GLY A 202
REMARK 465 ILE A 203
REMARK 465 LYS A 204
REMARK 465 SER A 205
REMARK 465 PHE A 206
REMARK 465 ARG A 207
REMARK 465 GLY A 260
REMARK 465 PRO A 261
REMARK 465 LEU A 262
REMARK 465 ASP A 263
REMARK 465 ASP A 264
REMARK 465 ASP A 265
REMARK 465 LEU A 266
REMARK 465 GLU A 267
REMARK 465 HIS A 268
REMARK 465 HIS A 269
REMARK 465 HIS A 270
REMARK 465 HIS A 271
REMARK 465 HIS A 272
REMARK 465 HIS A 273
REMARK 465 MET B 1
REMARK 465 ARG B 196
REMARK 465 THR B 197
REMARK 465 LEU B 198
REMARK 465 ALA B 199
REMARK 465 ALA B 200
REMARK 465 SER B 201
REMARK 465 GLY B 202
REMARK 465 ILE B 203
REMARK 465 LYS B 204
REMARK 465 SER B 205
REMARK 465 PHE B 206
REMARK 465 ARG B 207
REMARK 465 LYS B 208
REMARK 465 MET B 209
REMARK 465 MET B 259
REMARK 465 GLY B 260
REMARK 465 PRO B 261
REMARK 465 LEU B 262
REMARK 465 ASP B 263
REMARK 465 ASP B 264
REMARK 465 ASP B 265
REMARK 465 LEU B 266
REMARK 465 GLU B 267
REMARK 465 HIS B 268
REMARK 465 HIS B 269
REMARK 465 HIS B 270
REMARK 465 HIS B 271
REMARK 465 HIS B 272
REMARK 465 HIS B 273
REMARK 465 MET C 1
REMARK 465 ARG C 196
REMARK 465 THR C 197
REMARK 465 LEU C 198
REMARK 465 ALA C 199
REMARK 465 ALA C 200
REMARK 465 SER C 201
REMARK 465 GLY C 202
REMARK 465 ILE C 203
REMARK 465 LYS C 204
REMARK 465 SER C 205
REMARK 465 PHE C 206
REMARK 465 ARG C 207
REMARK 465 LYS C 208
REMARK 465 GLY C 260
REMARK 465 PRO C 261
REMARK 465 LEU C 262
REMARK 465 ASP C 263
REMARK 465 ASP C 264
REMARK 465 ASP C 265
REMARK 465 LEU C 266
REMARK 465 GLU C 267
REMARK 465 HIS C 268
REMARK 465 HIS C 269
REMARK 465 HIS C 270
REMARK 465 HIS C 271
REMARK 465 HIS C 272
REMARK 465 HIS C 273
REMARK 465 MET D 1
REMARK 465 ARG D 196
REMARK 465 THR D 197
REMARK 465 LEU D 198
REMARK 465 ALA D 199
REMARK 465 ALA D 200
REMARK 465 SER D 201
REMARK 465 GLY D 202
REMARK 465 ILE D 203
REMARK 465 LYS D 204
REMARK 465 SER D 205
REMARK 465 PHE D 206
REMARK 465 ARG D 207
REMARK 465 GLY D 260
REMARK 465 PRO D 261
REMARK 465 LEU D 262
REMARK 465 ASP D 263
REMARK 465 ASP D 264
REMARK 465 ASP D 265
REMARK 465 LEU D 266
REMARK 465 GLU D 267
REMARK 465 HIS D 268
REMARK 465 HIS D 269
REMARK 465 HIS D 270
REMARK 465 HIS D 271
REMARK 465 HIS D 272
REMARK 465 HIS D 273
REMARK 465 MET E 1
REMARK 465 ARG E 196
REMARK 465 THR E 197
REMARK 465 LEU E 198
REMARK 465 ALA E 199
REMARK 465 ALA E 200
REMARK 465 SER E 201
REMARK 465 GLY E 202
REMARK 465 ILE E 203
REMARK 465 LYS E 204
REMARK 465 SER E 205
REMARK 465 PHE E 206
REMARK 465 ARG E 207
REMARK 465 LYS E 208
REMARK 465 MET E 209
REMARK 465 GLY E 260
REMARK 465 PRO E 261
REMARK 465 LEU E 262
REMARK 465 ASP E 263
REMARK 465 ASP E 264
REMARK 465 ASP E 265
REMARK 465 LEU E 266
REMARK 465 GLU E 267
REMARK 465 HIS E 268
REMARK 465 HIS E 269
REMARK 465 HIS E 270
REMARK 465 HIS E 271
REMARK 465 HIS E 272
REMARK 465 HIS E 273
REMARK 465 MET F 1
REMARK 465 THR F 197
REMARK 465 LEU F 198
REMARK 465 ALA F 199
REMARK 465 ALA F 200
REMARK 465 SER F 201
REMARK 465 GLY F 202
REMARK 465 ILE F 203
REMARK 465 LYS F 204
REMARK 465 SER F 205
REMARK 465 PHE F 206
REMARK 465 ARG F 207
REMARK 465 LYS F 208
REMARK 465 MET F 209
REMARK 465 GLY F 260
REMARK 465 PRO F 261
REMARK 465 LEU F 262
REMARK 465 ASP F 263
REMARK 465 ASP F 264
REMARK 465 ASP F 265
REMARK 465 LEU F 266
REMARK 465 GLU F 267
REMARK 465 HIS F 268
REMARK 465 HIS F 269
REMARK 465 HIS F 270
REMARK 465 HIS F 271
REMARK 465 HIS F 272
REMARK 465 HIS F 273
REMARK 465 MET G 1
REMARK 465 ARG G 196
REMARK 465 THR G 197
REMARK 465 LEU G 198
REMARK 465 ALA G 199
REMARK 465 ALA G 200
REMARK 465 SER G 201
REMARK 465 GLY G 202
REMARK 465 ILE G 203
REMARK 465 LYS G 204
REMARK 465 SER G 205
REMARK 465 PHE G 206
REMARK 465 ARG G 207
REMARK 465 LYS G 208
REMARK 465 MET G 209
REMARK 465 GLY G 260
REMARK 465 PRO G 261
REMARK 465 LEU G 262
REMARK 465 ASP G 263
REMARK 465 ASP G 264
REMARK 465 ASP G 265
REMARK 465 LEU G 266
REMARK 465 GLU G 267
REMARK 465 HIS G 268
REMARK 465 HIS G 269
REMARK 465 HIS G 270
REMARK 465 HIS G 271
REMARK 465 HIS G 272
REMARK 465 HIS G 273
REMARK 465 MET H 1
REMARK 465 THR H 197
REMARK 465 LEU H 198
REMARK 465 ALA H 199
REMARK 465 ALA H 200
REMARK 465 SER H 201
REMARK 465 GLY H 202
REMARK 465 ILE H 203
REMARK 465 LYS H 204
REMARK 465 SER H 205
REMARK 465 PHE H 206
REMARK 465 GLY H 260
REMARK 465 PRO H 261
REMARK 465 LEU H 262
REMARK 465 ASP H 263
REMARK 465 ASP H 264
REMARK 465 ASP H 265
REMARK 465 LEU H 266
REMARK 465 GLU H 267
REMARK 465 HIS H 268
REMARK 465 HIS H 269
REMARK 465 HIS H 270
REMARK 465 HIS H 271
REMARK 465 HIS H 272
REMARK 465 HIS H 273
REMARK 465 MET I 1
REMARK 465 ARG I 196
REMARK 465 THR I 197
REMARK 465 LEU I 198
REMARK 465 ALA I 199
REMARK 465 ALA I 200
REMARK 465 SER I 201
REMARK 465 GLY I 202
REMARK 465 ILE I 203
REMARK 465 LYS I 204
REMARK 465 SER I 205
REMARK 465 PHE I 206
REMARK 465 ARG I 207
REMARK 465 LYS I 208
REMARK 465 MET I 209
REMARK 465 GLY I 260
REMARK 465 PRO I 261
REMARK 465 LEU I 262
REMARK 465 ASP I 263
REMARK 465 ASP I 264
REMARK 465 ASP I 265
REMARK 465 LEU I 266
REMARK 465 GLU I 267
REMARK 465 HIS I 268
REMARK 465 HIS I 269
REMARK 465 HIS I 270
REMARK 465 HIS I 271
REMARK 465 HIS I 272
REMARK 465 HIS I 273
REMARK 465 MET J 1
REMARK 465 ARG J 196
REMARK 465 THR J 197
REMARK 465 LEU J 198
REMARK 465 ALA J 199
REMARK 465 ALA J 200
REMARK 465 SER J 201
REMARK 465 GLY J 202
REMARK 465 ILE J 203
REMARK 465 LYS J 204
REMARK 465 SER J 205
REMARK 465 PHE J 206
REMARK 465 ARG J 207
REMARK 465 LYS J 208
REMARK 465 GLY J 260
REMARK 465 PRO J 261
REMARK 465 LEU J 262
REMARK 465 ASP J 263
REMARK 465 ASP J 264
REMARK 465 ASP J 265
REMARK 465 LEU J 266
REMARK 465 GLU J 267
REMARK 465 HIS J 268
REMARK 465 HIS J 269
REMARK 465 HIS J 270
REMARK 465 HIS J 271
REMARK 465 HIS J 272
REMARK 465 HIS J 273
REMARK 465 MET K 1
REMARK 465 THR K 197
REMARK 465 LEU K 198
REMARK 465 ALA K 199
REMARK 465 ALA K 200
REMARK 465 SER K 201
REMARK 465 GLY K 202
REMARK 465 ILE K 203
REMARK 465 LYS K 204
REMARK 465 SER K 205
REMARK 465 PHE K 206
REMARK 465 ARG K 207
REMARK 465 LYS K 208
REMARK 465 GLY K 260
REMARK 465 PRO K 261
REMARK 465 LEU K 262
REMARK 465 ASP K 263
REMARK 465 ASP K 264
REMARK 465 ASP K 265
REMARK 465 LEU K 266
REMARK 465 GLU K 267
REMARK 465 HIS K 268
REMARK 465 HIS K 269
REMARK 465 HIS K 270
REMARK 465 HIS K 271
REMARK 465 HIS K 272
REMARK 465 HIS K 273
REMARK 465 MET L 1
REMARK 465 THR L 197
REMARK 465 LEU L 198
REMARK 465 ALA L 199
REMARK 465 ALA L 200
REMARK 465 SER L 201
REMARK 465 GLY L 202
REMARK 465 ILE L 203
REMARK 465 LYS L 204
REMARK 465 SER L 205
REMARK 465 PHE L 206
REMARK 465 ARG L 207
REMARK 465 LYS L 208
REMARK 465 MET L 209
REMARK 465 MET L 259
REMARK 465 GLY L 260
REMARK 465 PRO L 261
REMARK 465 LEU L 262
REMARK 465 ASP L 263
REMARK 465 ASP L 264
REMARK 465 ASP L 265
REMARK 465 LEU L 266
REMARK 465 GLU L 267
REMARK 465 HIS L 268
REMARK 465 HIS L 269
REMARK 465 HIS L 270
REMARK 465 HIS L 271
REMARK 465 HIS L 272
REMARK 465 HIS L 273
REMARK 465 MET M 1
REMARK 465 THR M 197
REMARK 465 LEU M 198
REMARK 465 ALA M 199
REMARK 465 ALA M 200
REMARK 465 SER M 201
REMARK 465 GLY M 202
REMARK 465 ILE M 203
REMARK 465 LYS M 204
REMARK 465 SER M 205
REMARK 465 PHE M 206
REMARK 465 ARG M 207
REMARK 465 LYS M 208
REMARK 465 MET M 259
REMARK 465 GLY M 260
REMARK 465 PRO M 261
REMARK 465 LEU M 262
REMARK 465 ASP M 263
REMARK 465 ASP M 264
REMARK 465 ASP M 265
REMARK 465 LEU M 266
REMARK 465 GLU M 267
REMARK 465 HIS M 268
REMARK 465 HIS M 269
REMARK 465 HIS M 270
REMARK 465 HIS M 271
REMARK 465 HIS M 272
REMARK 465 HIS M 273
REMARK 465 MET N 1
REMARK 465 THR N 197
REMARK 465 LEU N 198
REMARK 465 ALA N 199
REMARK 465 ALA N 200
REMARK 465 SER N 201
REMARK 465 GLY N 202
REMARK 465 ILE N 203
REMARK 465 LYS N 204
REMARK 465 SER N 205
REMARK 465 PHE N 206
REMARK 465 ARG N 207
REMARK 465 LYS N 208
REMARK 465 ALA N 258
REMARK 465 MET N 259
REMARK 465 GLY N 260
REMARK 465 PRO N 261
REMARK 465 LEU N 262
REMARK 465 ASP N 263
REMARK 465 ASP N 264
REMARK 465 ASP N 265
REMARK 465 LEU N 266
REMARK 465 GLU N 267
REMARK 465 HIS N 268
REMARK 465 HIS N 269
REMARK 465 HIS N 270
REMARK 465 HIS N 271
REMARK 465 HIS N 272
REMARK 465 HIS N 273
REMARK 465 MET O 1
REMARK 465 THR O 197
REMARK 465 LEU O 198
REMARK 465 ALA O 199
REMARK 465 ALA O 200
REMARK 465 SER O 201
REMARK 465 GLY O 202
REMARK 465 ILE O 203
REMARK 465 LYS O 204
REMARK 465 SER O 205
REMARK 465 PHE O 206
REMARK 465 MET O 259
REMARK 465 GLY O 260
REMARK 465 PRO O 261
REMARK 465 LEU O 262
REMARK 465 ASP O 263
REMARK 465 ASP O 264
REMARK 465 ASP O 265
REMARK 465 LEU O 266
REMARK 465 GLU O 267
REMARK 465 HIS O 268
REMARK 465 HIS O 269
REMARK 465 HIS O 270
REMARK 465 HIS O 271
REMARK 465 HIS O 272
REMARK 465 HIS O 273
REMARK 465 MET P 1
REMARK 465 THR P 197
REMARK 465 LEU P 198
REMARK 465 ALA P 199
REMARK 465 ALA P 200
REMARK 465 SER P 201
REMARK 465 GLY P 202
REMARK 465 ILE P 203
REMARK 465 LYS P 204
REMARK 465 SER P 205
REMARK 465 PHE P 206
REMARK 465 ARG P 207
REMARK 465 PRO P 261
REMARK 465 LEU P 262
REMARK 465 ASP P 263
REMARK 465 ASP P 264
REMARK 465 ASP P 265
REMARK 465 LEU P 266
REMARK 465 GLU P 267
REMARK 465 HIS P 268
REMARK 465 HIS P 269
REMARK 465 HIS P 270
REMARK 465 HIS P 271
REMARK 465 HIS P 272
REMARK 465 HIS P 273
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 OE1 GLU G 153 OH TYR G 249 1.88
REMARK 500 O ASN N 188 O HOH N 303 1.91
REMARK 500 N THR N 146 O HOH N 303 1.99
REMARK 500 OD1 ASP L 251 O HOH L 311 2.00
REMARK 500 OD1 ASP D 42 O HOH D 302 2.06
REMARK 500 O ILE C 195 O HOH C 324 2.06
REMARK 500 O GLU E 74 O HOH E 306 2.08
REMARK 500 O ILE P 11 O HOH P 315 2.09
REMARK 500 O THR O 107 NZ LYS P 131 2.09
REMARK 500 O ASP C 66 O HOH C 320 2.09
REMARK 500 O SER D 16 OG SER D 22 2.10
REMARK 500 O GLY A 13 O HOH A 318 2.12
REMARK 500 O GLY L 32 O HOH L 301 2.12
REMARK 500 O ALA G 192 O HOH G 307 2.12
REMARK 500 O SER H 57 O HOH H 327 2.12
REMARK 500 O HOH J 306 O HOH J 309 2.12
REMARK 500 O ALA O 258 O HOH O 311 2.13
REMARK 500 NH2 ARG C 134 OE2 GLU C 183 2.13
REMARK 500 OE1 GLU O 153 OH TYR O 249 2.13
REMARK 500 OH TYR N 124 O HOH N 321 2.14
REMARK 500 O ALA L 211 O HOH L 303 2.14
REMARK 500 O HOH O 309 O HOH O 311 2.14
REMARK 500 NZ LYS C 131 O HOH C 328 2.14
REMARK 500 O LEU F 210 O HOH F 318 2.15
REMARK 500 OE2 GLU K 226 O HOH K 308 2.15
REMARK 500 O SER L 244 O HOH L 302 2.15
REMARK 500 O LYS A 208 O HOH A 327 2.16
REMARK 500 OG SER O 148 OE2 GLU O 170 2.16
REMARK 500 OE2 GLU O 214 ND2 ASN O 222 2.16
REMARK 500 OE2 GLU E 31 O HOH E 309 2.17
REMARK 500 O CYS F 236 O HOH F 311 2.17
REMARK 500 O ASP J 238 OG SER J 241 2.17
REMARK 500 OG SER G 148 OE2 GLU G 170 2.18
REMARK 500 O GLY F 32 O HOH F 303 2.18
REMARK 500 NH1 ARG J 186 O ALA J 240 2.18
REMARK 500 O MET F 259 O HOH F 301 2.18
REMARK 500 O ASP E 238 OG SER E 241 2.18
REMARK 500 O HOH G 309 O HOH G 320 2.19
REMARK 500 OG SER I 241 OE2 GLU K 227 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NH2 ARG G 47 O CYS I 62 2555 2.17
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 PRO O 59 C - N - CA ANGL. DEV. = 11.5 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 VAL A 14 106.80 -57.31
REMARK 500 ASN A 41 -172.04 179.58
REMARK 500 CYS A 65 115.93 -169.06
REMARK 500 LEU A 102 42.46 -101.56
REMARK 500 ASP A 103 105.68 -161.06
REMARK 500 PHE A 106 -74.78 -42.36
REMARK 500 ALA A 123 -60.63 -122.02
REMARK 500 LYS A 131 -79.91 -59.56
REMARK 500 ALA A 132 -29.24 -35.99
REMARK 500 ASN A 160 -135.66 38.80
REMARK 500 PRO A 218 -37.05 -39.86
REMARK 500 ALA A 240 40.44 -103.39
REMARK 500 ALA B 15 -18.30 -146.83
REMARK 500 GLN B 40 -74.98 -55.74
REMARK 500 LEU B 44 -11.32 58.67
REMARK 500 ARG B 45 -70.82 -54.72
REMARK 500 VAL B 67 -6.17 -59.75
REMARK 500 ALA B 123 -41.23 -142.39
REMARK 500 SER B 143 145.56 -175.63
REMARK 500 ASN B 160 -128.22 45.37
REMARK 500 ASP B 251 15.40 -155.45
REMARK 500 ALA C 25 -39.11 -39.04
REMARK 500 VAL C 67 11.44 -59.29
REMARK 500 SER C 93 55.02 -119.81
REMARK 500 ALA C 123 -69.42 -130.53
REMARK 500 MET C 156 148.93 -178.09
REMARK 500 PRO C 157 126.01 -34.34
REMARK 500 ASN C 158 -7.11 61.61
REMARK 500 ASN C 160 -126.36 41.43
REMARK 500 ALA C 182 -57.08 -26.68
REMARK 500 GLU C 226 -70.37 -47.44
REMARK 500 SER C 241 -2.54 -56.54
REMARK 500 ASP C 251 28.46 -140.18
REMARK 500 SER D 19 171.03 -52.54
REMARK 500 GLU D 50 -70.18 -53.04
REMARK 500 PRO D 59 -33.48 -20.32
REMARK 500 VAL D 67 -9.25 -58.58
REMARK 500 ASP D 103 107.42 -162.16
REMARK 500 ASN D 158 -8.70 65.88
REMARK 500 ASN D 160 -129.29 52.60
REMARK 500 VAL D 250 78.40 -106.86
REMARK 500 ASP D 251 35.67 -142.17
REMARK 500 ALA D 258 -61.15 -126.24
REMARK 500 THR E 5 97.38 -49.86
REMARK 500 ALA E 15 -11.69 -140.96
REMARK 500 ALA E 26 -71.92 -60.54
REMARK 500 LYS E 43 -72.09 -71.48
REMARK 500 LEU E 44 -0.89 -59.86
REMARK 500 PRO E 59 -26.26 -36.71
REMARK 500 CYS E 65 110.99 -171.08
REMARK 500
REMARK 500 THIS ENTRY HAS 200 RAMACHANDRAN OUTLIERS.
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 GLU O 60 LEU O 61 147.63
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4NR0 RELATED DB: PDB
DBREF 4NQZ A 1 265 UNP Q9ZFE4 FABI_PSEAE 1 265
DBREF 4NQZ B 1 265 UNP Q9ZFE4 FABI_PSEAE 1 265
DBREF 4NQZ C 1 265 UNP Q9ZFE4 FABI_PSEAE 1 265
DBREF 4NQZ D 1 265 UNP Q9ZFE4 FABI_PSEAE 1 265
DBREF 4NQZ E 1 265 UNP Q9ZFE4 FABI_PSEAE 1 265
DBREF 4NQZ F 1 265 UNP Q9ZFE4 FABI_PSEAE 1 265
DBREF 4NQZ G 1 265 UNP Q9ZFE4 FABI_PSEAE 1 265
DBREF 4NQZ H 1 265 UNP Q9ZFE4 FABI_PSEAE 1 265
DBREF 4NQZ I 1 265 UNP Q9ZFE4 FABI_PSEAE 1 265
DBREF 4NQZ J 1 265 UNP Q9ZFE4 FABI_PSEAE 1 265
DBREF 4NQZ K 1 265 UNP Q9ZFE4 FABI_PSEAE 1 265
DBREF 4NQZ L 1 265 UNP Q9ZFE4 FABI_PSEAE 1 265
DBREF 4NQZ M 1 265 UNP Q9ZFE4 FABI_PSEAE 1 265
DBREF 4NQZ N 1 265 UNP Q9ZFE4 FABI_PSEAE 1 265
DBREF 4NQZ O 1 265 UNP Q9ZFE4 FABI_PSEAE 1 265
DBREF 4NQZ P 1 265 UNP Q9ZFE4 FABI_PSEAE 1 265
SEQADV 4NQZ LEU A 266 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ GLU A 267 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS A 268 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS A 269 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS A 270 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS A 271 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS A 272 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS A 273 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ LEU B 266 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ GLU B 267 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS B 268 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS B 269 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS B 270 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS B 271 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS B 272 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS B 273 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ LEU C 266 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ GLU C 267 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS C 268 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS C 269 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS C 270 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS C 271 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS C 272 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS C 273 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ LEU D 266 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ GLU D 267 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS D 268 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS D 269 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS D 270 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS D 271 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS D 272 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS D 273 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ LEU E 266 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ GLU E 267 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS E 268 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS E 269 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS E 270 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS E 271 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS E 272 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS E 273 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ LEU F 266 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ GLU F 267 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS F 268 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS F 269 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS F 270 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS F 271 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS F 272 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS F 273 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ LEU G 266 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ GLU G 267 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS G 268 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS G 269 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS G 270 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS G 271 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS G 272 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS G 273 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ LEU H 266 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ GLU H 267 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS H 268 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS H 269 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS H 270 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS H 271 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS H 272 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS H 273 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ LEU I 266 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ GLU I 267 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS I 268 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS I 269 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS I 270 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS I 271 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS I 272 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS I 273 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ LEU J 266 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ GLU J 267 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS J 268 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS J 269 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS J 270 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS J 271 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS J 272 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS J 273 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ LEU K 266 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ GLU K 267 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS K 268 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS K 269 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS K 270 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS K 271 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS K 272 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS K 273 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ LEU L 266 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ GLU L 267 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS L 268 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS L 269 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS L 270 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS L 271 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS L 272 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS L 273 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ LEU M 266 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ GLU M 267 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS M 268 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS M 269 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS M 270 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS M 271 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS M 272 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS M 273 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ LEU N 266 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ GLU N 267 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS N 268 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS N 269 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS N 270 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS N 271 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS N 272 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS N 273 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ LEU O 266 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ GLU O 267 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS O 268 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS O 269 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS O 270 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS O 271 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS O 272 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS O 273 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ LEU P 266 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ GLU P 267 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS P 268 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS P 269 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS P 270 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS P 271 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS P 272 UNP Q9ZFE4 EXPRESSION TAG
SEQADV 4NQZ HIS P 273 UNP Q9ZFE4 EXPRESSION TAG
SEQRES 1 A 273 MET GLY PHE LEU THR GLY LYS ARG ALA LEU ILE VAL GLY
SEQRES 2 A 273 VAL ALA SER LYS LEU SER ILE ALA SER GLY ILE ALA ALA
SEQRES 3 A 273 ALA MET HIS ARG GLU GLY ALA GLU LEU ALA PHE THR TYR
SEQRES 4 A 273 GLN ASN ASP LYS LEU ARG GLY ARG VAL GLU GLU PHE ALA
SEQRES 5 A 273 SER GLY TRP GLY SER ARG PRO GLU LEU CYS PHE PRO CYS
SEQRES 6 A 273 ASP VAL ALA ASP ASP SER GLN ILE GLU ALA VAL PHE ALA
SEQRES 7 A 273 ALA LEU GLY LYS HIS TRP ASP GLY LEU ASP ILE ILE VAL
SEQRES 8 A 273 HIS SER VAL GLY PHE ALA PRO GLY ASP GLN LEU ASP GLY
SEQRES 9 A 273 ASP PHE THR ALA VAL THR THR ARG GLU GLY PHE ARG ILE
SEQRES 10 A 273 ALA HIS ASP ILE SER ALA TYR SER PHE ILE ALA LEU ALA
SEQRES 11 A 273 LYS ALA GLY ARG GLU MET MET LYS GLY ARG ASN GLY SER
SEQRES 12 A 273 LEU LEU THR LEU SER TYR LEU GLY ALA GLU ARG THR MET
SEQRES 13 A 273 PRO ASN TYR ASN VAL MET GLY MET ALA LYS ALA SER LEU
SEQRES 14 A 273 GLU ALA GLY VAL ARG TYR LEU ALA GLY SER LEU GLY ALA
SEQRES 15 A 273 GLU GLY THR ARG VAL ASN ALA VAL SER ALA GLY PRO ILE
SEQRES 16 A 273 ARG THR LEU ALA ALA SER GLY ILE LYS SER PHE ARG LYS
SEQRES 17 A 273 MET LEU ALA ALA ASN GLU ARG GLN THR PRO LEU ARG ARG
SEQRES 18 A 273 ASN VAL THR ILE GLU GLU VAL GLY ASN ALA GLY ALA PHE
SEQRES 19 A 273 LEU CYS SER ASP LEU ALA SER GLY ILE SER GLY GLU ILE
SEQRES 20 A 273 LEU TYR VAL ASP GLY GLY PHE ASN THR THR ALA MET GLY
SEQRES 21 A 273 PRO LEU ASP ASP ASP LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 273 MET GLY PHE LEU THR GLY LYS ARG ALA LEU ILE VAL GLY
SEQRES 2 B 273 VAL ALA SER LYS LEU SER ILE ALA SER GLY ILE ALA ALA
SEQRES 3 B 273 ALA MET HIS ARG GLU GLY ALA GLU LEU ALA PHE THR TYR
SEQRES 4 B 273 GLN ASN ASP LYS LEU ARG GLY ARG VAL GLU GLU PHE ALA
SEQRES 5 B 273 SER GLY TRP GLY SER ARG PRO GLU LEU CYS PHE PRO CYS
SEQRES 6 B 273 ASP VAL ALA ASP ASP SER GLN ILE GLU ALA VAL PHE ALA
SEQRES 7 B 273 ALA LEU GLY LYS HIS TRP ASP GLY LEU ASP ILE ILE VAL
SEQRES 8 B 273 HIS SER VAL GLY PHE ALA PRO GLY ASP GLN LEU ASP GLY
SEQRES 9 B 273 ASP PHE THR ALA VAL THR THR ARG GLU GLY PHE ARG ILE
SEQRES 10 B 273 ALA HIS ASP ILE SER ALA TYR SER PHE ILE ALA LEU ALA
SEQRES 11 B 273 LYS ALA GLY ARG GLU MET MET LYS GLY ARG ASN GLY SER
SEQRES 12 B 273 LEU LEU THR LEU SER TYR LEU GLY ALA GLU ARG THR MET
SEQRES 13 B 273 PRO ASN TYR ASN VAL MET GLY MET ALA LYS ALA SER LEU
SEQRES 14 B 273 GLU ALA GLY VAL ARG TYR LEU ALA GLY SER LEU GLY ALA
SEQRES 15 B 273 GLU GLY THR ARG VAL ASN ALA VAL SER ALA GLY PRO ILE
SEQRES 16 B 273 ARG THR LEU ALA ALA SER GLY ILE LYS SER PHE ARG LYS
SEQRES 17 B 273 MET LEU ALA ALA ASN GLU ARG GLN THR PRO LEU ARG ARG
SEQRES 18 B 273 ASN VAL THR ILE GLU GLU VAL GLY ASN ALA GLY ALA PHE
SEQRES 19 B 273 LEU CYS SER ASP LEU ALA SER GLY ILE SER GLY GLU ILE
SEQRES 20 B 273 LEU TYR VAL ASP GLY GLY PHE ASN THR THR ALA MET GLY
SEQRES 21 B 273 PRO LEU ASP ASP ASP LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 C 273 MET GLY PHE LEU THR GLY LYS ARG ALA LEU ILE VAL GLY
SEQRES 2 C 273 VAL ALA SER LYS LEU SER ILE ALA SER GLY ILE ALA ALA
SEQRES 3 C 273 ALA MET HIS ARG GLU GLY ALA GLU LEU ALA PHE THR TYR
SEQRES 4 C 273 GLN ASN ASP LYS LEU ARG GLY ARG VAL GLU GLU PHE ALA
SEQRES 5 C 273 SER GLY TRP GLY SER ARG PRO GLU LEU CYS PHE PRO CYS
SEQRES 6 C 273 ASP VAL ALA ASP ASP SER GLN ILE GLU ALA VAL PHE ALA
SEQRES 7 C 273 ALA LEU GLY LYS HIS TRP ASP GLY LEU ASP ILE ILE VAL
SEQRES 8 C 273 HIS SER VAL GLY PHE ALA PRO GLY ASP GLN LEU ASP GLY
SEQRES 9 C 273 ASP PHE THR ALA VAL THR THR ARG GLU GLY PHE ARG ILE
SEQRES 10 C 273 ALA HIS ASP ILE SER ALA TYR SER PHE ILE ALA LEU ALA
SEQRES 11 C 273 LYS ALA GLY ARG GLU MET MET LYS GLY ARG ASN GLY SER
SEQRES 12 C 273 LEU LEU THR LEU SER TYR LEU GLY ALA GLU ARG THR MET
SEQRES 13 C 273 PRO ASN TYR ASN VAL MET GLY MET ALA LYS ALA SER LEU
SEQRES 14 C 273 GLU ALA GLY VAL ARG TYR LEU ALA GLY SER LEU GLY ALA
SEQRES 15 C 273 GLU GLY THR ARG VAL ASN ALA VAL SER ALA GLY PRO ILE
SEQRES 16 C 273 ARG THR LEU ALA ALA SER GLY ILE LYS SER PHE ARG LYS
SEQRES 17 C 273 MET LEU ALA ALA ASN GLU ARG GLN THR PRO LEU ARG ARG
SEQRES 18 C 273 ASN VAL THR ILE GLU GLU VAL GLY ASN ALA GLY ALA PHE
SEQRES 19 C 273 LEU CYS SER ASP LEU ALA SER GLY ILE SER GLY GLU ILE
SEQRES 20 C 273 LEU TYR VAL ASP GLY GLY PHE ASN THR THR ALA MET GLY
SEQRES 21 C 273 PRO LEU ASP ASP ASP LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 D 273 MET GLY PHE LEU THR GLY LYS ARG ALA LEU ILE VAL GLY
SEQRES 2 D 273 VAL ALA SER LYS LEU SER ILE ALA SER GLY ILE ALA ALA
SEQRES 3 D 273 ALA MET HIS ARG GLU GLY ALA GLU LEU ALA PHE THR TYR
SEQRES 4 D 273 GLN ASN ASP LYS LEU ARG GLY ARG VAL GLU GLU PHE ALA
SEQRES 5 D 273 SER GLY TRP GLY SER ARG PRO GLU LEU CYS PHE PRO CYS
SEQRES 6 D 273 ASP VAL ALA ASP ASP SER GLN ILE GLU ALA VAL PHE ALA
SEQRES 7 D 273 ALA LEU GLY LYS HIS TRP ASP GLY LEU ASP ILE ILE VAL
SEQRES 8 D 273 HIS SER VAL GLY PHE ALA PRO GLY ASP GLN LEU ASP GLY
SEQRES 9 D 273 ASP PHE THR ALA VAL THR THR ARG GLU GLY PHE ARG ILE
SEQRES 10 D 273 ALA HIS ASP ILE SER ALA TYR SER PHE ILE ALA LEU ALA
SEQRES 11 D 273 LYS ALA GLY ARG GLU MET MET LYS GLY ARG ASN GLY SER
SEQRES 12 D 273 LEU LEU THR LEU SER TYR LEU GLY ALA GLU ARG THR MET
SEQRES 13 D 273 PRO ASN TYR ASN VAL MET GLY MET ALA LYS ALA SER LEU
SEQRES 14 D 273 GLU ALA GLY VAL ARG TYR LEU ALA GLY SER LEU GLY ALA
SEQRES 15 D 273 GLU GLY THR ARG VAL ASN ALA VAL SER ALA GLY PRO ILE
SEQRES 16 D 273 ARG THR LEU ALA ALA SER GLY ILE LYS SER PHE ARG LYS
SEQRES 17 D 273 MET LEU ALA ALA ASN GLU ARG GLN THR PRO LEU ARG ARG
SEQRES 18 D 273 ASN VAL THR ILE GLU GLU VAL GLY ASN ALA GLY ALA PHE
SEQRES 19 D 273 LEU CYS SER ASP LEU ALA SER GLY ILE SER GLY GLU ILE
SEQRES 20 D 273 LEU TYR VAL ASP GLY GLY PHE ASN THR THR ALA MET GLY
SEQRES 21 D 273 PRO LEU ASP ASP ASP LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 E 273 MET GLY PHE LEU THR GLY LYS ARG ALA LEU ILE VAL GLY
SEQRES 2 E 273 VAL ALA SER LYS LEU SER ILE ALA SER GLY ILE ALA ALA
SEQRES 3 E 273 ALA MET HIS ARG GLU GLY ALA GLU LEU ALA PHE THR TYR
SEQRES 4 E 273 GLN ASN ASP LYS LEU ARG GLY ARG VAL GLU GLU PHE ALA
SEQRES 5 E 273 SER GLY TRP GLY SER ARG PRO GLU LEU CYS PHE PRO CYS
SEQRES 6 E 273 ASP VAL ALA ASP ASP SER GLN ILE GLU ALA VAL PHE ALA
SEQRES 7 E 273 ALA LEU GLY LYS HIS TRP ASP GLY LEU ASP ILE ILE VAL
SEQRES 8 E 273 HIS SER VAL GLY PHE ALA PRO GLY ASP GLN LEU ASP GLY
SEQRES 9 E 273 ASP PHE THR ALA VAL THR THR ARG GLU GLY PHE ARG ILE
SEQRES 10 E 273 ALA HIS ASP ILE SER ALA TYR SER PHE ILE ALA LEU ALA
SEQRES 11 E 273 LYS ALA GLY ARG GLU MET MET LYS GLY ARG ASN GLY SER
SEQRES 12 E 273 LEU LEU THR LEU SER TYR LEU GLY ALA GLU ARG THR MET
SEQRES 13 E 273 PRO ASN TYR ASN VAL MET GLY MET ALA LYS ALA SER LEU
SEQRES 14 E 273 GLU ALA GLY VAL ARG TYR LEU ALA GLY SER LEU GLY ALA
SEQRES 15 E 273 GLU GLY THR ARG VAL ASN ALA VAL SER ALA GLY PRO ILE
SEQRES 16 E 273 ARG THR LEU ALA ALA SER GLY ILE LYS SER PHE ARG LYS
SEQRES 17 E 273 MET LEU ALA ALA ASN GLU ARG GLN THR PRO LEU ARG ARG
SEQRES 18 E 273 ASN VAL THR ILE GLU GLU VAL GLY ASN ALA GLY ALA PHE
SEQRES 19 E 273 LEU CYS SER ASP LEU ALA SER GLY ILE SER GLY GLU ILE
SEQRES 20 E 273 LEU TYR VAL ASP GLY GLY PHE ASN THR THR ALA MET GLY
SEQRES 21 E 273 PRO LEU ASP ASP ASP LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 F 273 MET GLY PHE LEU THR GLY LYS ARG ALA LEU ILE VAL GLY
SEQRES 2 F 273 VAL ALA SER LYS LEU SER ILE ALA SER GLY ILE ALA ALA
SEQRES 3 F 273 ALA MET HIS ARG GLU GLY ALA GLU LEU ALA PHE THR TYR
SEQRES 4 F 273 GLN ASN ASP LYS LEU ARG GLY ARG VAL GLU GLU PHE ALA
SEQRES 5 F 273 SER GLY TRP GLY SER ARG PRO GLU LEU CYS PHE PRO CYS
SEQRES 6 F 273 ASP VAL ALA ASP ASP SER GLN ILE GLU ALA VAL PHE ALA
SEQRES 7 F 273 ALA LEU GLY LYS HIS TRP ASP GLY LEU ASP ILE ILE VAL
SEQRES 8 F 273 HIS SER VAL GLY PHE ALA PRO GLY ASP GLN LEU ASP GLY
SEQRES 9 F 273 ASP PHE THR ALA VAL THR THR ARG GLU GLY PHE ARG ILE
SEQRES 10 F 273 ALA HIS ASP ILE SER ALA TYR SER PHE ILE ALA LEU ALA
SEQRES 11 F 273 LYS ALA GLY ARG GLU MET MET LYS GLY ARG ASN GLY SER
SEQRES 12 F 273 LEU LEU THR LEU SER TYR LEU GLY ALA GLU ARG THR MET
SEQRES 13 F 273 PRO ASN TYR ASN VAL MET GLY MET ALA LYS ALA SER LEU
SEQRES 14 F 273 GLU ALA GLY VAL ARG TYR LEU ALA GLY SER LEU GLY ALA
SEQRES 15 F 273 GLU GLY THR ARG VAL ASN ALA VAL SER ALA GLY PRO ILE
SEQRES 16 F 273 ARG THR LEU ALA ALA SER GLY ILE LYS SER PHE ARG LYS
SEQRES 17 F 273 MET LEU ALA ALA ASN GLU ARG GLN THR PRO LEU ARG ARG
SEQRES 18 F 273 ASN VAL THR ILE GLU GLU VAL GLY ASN ALA GLY ALA PHE
SEQRES 19 F 273 LEU CYS SER ASP LEU ALA SER GLY ILE SER GLY GLU ILE
SEQRES 20 F 273 LEU TYR VAL ASP GLY GLY PHE ASN THR THR ALA MET GLY
SEQRES 21 F 273 PRO LEU ASP ASP ASP LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 G 273 MET GLY PHE LEU THR GLY LYS ARG ALA LEU ILE VAL GLY
SEQRES 2 G 273 VAL ALA SER LYS LEU SER ILE ALA SER GLY ILE ALA ALA
SEQRES 3 G 273 ALA MET HIS ARG GLU GLY ALA GLU LEU ALA PHE THR TYR
SEQRES 4 G 273 GLN ASN ASP LYS LEU ARG GLY ARG VAL GLU GLU PHE ALA
SEQRES 5 G 273 SER GLY TRP GLY SER ARG PRO GLU LEU CYS PHE PRO CYS
SEQRES 6 G 273 ASP VAL ALA ASP ASP SER GLN ILE GLU ALA VAL PHE ALA
SEQRES 7 G 273 ALA LEU GLY LYS HIS TRP ASP GLY LEU ASP ILE ILE VAL
SEQRES 8 G 273 HIS SER VAL GLY PHE ALA PRO GLY ASP GLN LEU ASP GLY
SEQRES 9 G 273 ASP PHE THR ALA VAL THR THR ARG GLU GLY PHE ARG ILE
SEQRES 10 G 273 ALA HIS ASP ILE SER ALA TYR SER PHE ILE ALA LEU ALA
SEQRES 11 G 273 LYS ALA GLY ARG GLU MET MET LYS GLY ARG ASN GLY SER
SEQRES 12 G 273 LEU LEU THR LEU SER TYR LEU GLY ALA GLU ARG THR MET
SEQRES 13 G 273 PRO ASN TYR ASN VAL MET GLY MET ALA LYS ALA SER LEU
SEQRES 14 G 273 GLU ALA GLY VAL ARG TYR LEU ALA GLY SER LEU GLY ALA
SEQRES 15 G 273 GLU GLY THR ARG VAL ASN ALA VAL SER ALA GLY PRO ILE
SEQRES 16 G 273 ARG THR LEU ALA ALA SER GLY ILE LYS SER PHE ARG LYS
SEQRES 17 G 273 MET LEU ALA ALA ASN GLU ARG GLN THR PRO LEU ARG ARG
SEQRES 18 G 273 ASN VAL THR ILE GLU GLU VAL GLY ASN ALA GLY ALA PHE
SEQRES 19 G 273 LEU CYS SER ASP LEU ALA SER GLY ILE SER GLY GLU ILE
SEQRES 20 G 273 LEU TYR VAL ASP GLY GLY PHE ASN THR THR ALA MET GLY
SEQRES 21 G 273 PRO LEU ASP ASP ASP LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 H 273 MET GLY PHE LEU THR GLY LYS ARG ALA LEU ILE VAL GLY
SEQRES 2 H 273 VAL ALA SER LYS LEU SER ILE ALA SER GLY ILE ALA ALA
SEQRES 3 H 273 ALA MET HIS ARG GLU GLY ALA GLU LEU ALA PHE THR TYR
SEQRES 4 H 273 GLN ASN ASP LYS LEU ARG GLY ARG VAL GLU GLU PHE ALA
SEQRES 5 H 273 SER GLY TRP GLY SER ARG PRO GLU LEU CYS PHE PRO CYS
SEQRES 6 H 273 ASP VAL ALA ASP ASP SER GLN ILE GLU ALA VAL PHE ALA
SEQRES 7 H 273 ALA LEU GLY LYS HIS TRP ASP GLY LEU ASP ILE ILE VAL
SEQRES 8 H 273 HIS SER VAL GLY PHE ALA PRO GLY ASP GLN LEU ASP GLY
SEQRES 9 H 273 ASP PHE THR ALA VAL THR THR ARG GLU GLY PHE ARG ILE
SEQRES 10 H 273 ALA HIS ASP ILE SER ALA TYR SER PHE ILE ALA LEU ALA
SEQRES 11 H 273 LYS ALA GLY ARG GLU MET MET LYS GLY ARG ASN GLY SER
SEQRES 12 H 273 LEU LEU THR LEU SER TYR LEU GLY ALA GLU ARG THR MET
SEQRES 13 H 273 PRO ASN TYR ASN VAL MET GLY MET ALA LYS ALA SER LEU
SEQRES 14 H 273 GLU ALA GLY VAL ARG TYR LEU ALA GLY SER LEU GLY ALA
SEQRES 15 H 273 GLU GLY THR ARG VAL ASN ALA VAL SER ALA GLY PRO ILE
SEQRES 16 H 273 ARG THR LEU ALA ALA SER GLY ILE LYS SER PHE ARG LYS
SEQRES 17 H 273 MET LEU ALA ALA ASN GLU ARG GLN THR PRO LEU ARG ARG
SEQRES 18 H 273 ASN VAL THR ILE GLU GLU VAL GLY ASN ALA GLY ALA PHE
SEQRES 19 H 273 LEU CYS SER ASP LEU ALA SER GLY ILE SER GLY GLU ILE
SEQRES 20 H 273 LEU TYR VAL ASP GLY GLY PHE ASN THR THR ALA MET GLY
SEQRES 21 H 273 PRO LEU ASP ASP ASP LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 I 273 MET GLY PHE LEU THR GLY LYS ARG ALA LEU ILE VAL GLY
SEQRES 2 I 273 VAL ALA SER LYS LEU SER ILE ALA SER GLY ILE ALA ALA
SEQRES 3 I 273 ALA MET HIS ARG GLU GLY ALA GLU LEU ALA PHE THR TYR
SEQRES 4 I 273 GLN ASN ASP LYS LEU ARG GLY ARG VAL GLU GLU PHE ALA
SEQRES 5 I 273 SER GLY TRP GLY SER ARG PRO GLU LEU CYS PHE PRO CYS
SEQRES 6 I 273 ASP VAL ALA ASP ASP SER GLN ILE GLU ALA VAL PHE ALA
SEQRES 7 I 273 ALA LEU GLY LYS HIS TRP ASP GLY LEU ASP ILE ILE VAL
SEQRES 8 I 273 HIS SER VAL GLY PHE ALA PRO GLY ASP GLN LEU ASP GLY
SEQRES 9 I 273 ASP PHE THR ALA VAL THR THR ARG GLU GLY PHE ARG ILE
SEQRES 10 I 273 ALA HIS ASP ILE SER ALA TYR SER PHE ILE ALA LEU ALA
SEQRES 11 I 273 LYS ALA GLY ARG GLU MET MET LYS GLY ARG ASN GLY SER
SEQRES 12 I 273 LEU LEU THR LEU SER TYR LEU GLY ALA GLU ARG THR MET
SEQRES 13 I 273 PRO ASN TYR ASN VAL MET GLY MET ALA LYS ALA SER LEU
SEQRES 14 I 273 GLU ALA GLY VAL ARG TYR LEU ALA GLY SER LEU GLY ALA
SEQRES 15 I 273 GLU GLY THR ARG VAL ASN ALA VAL SER ALA GLY PRO ILE
SEQRES 16 I 273 ARG THR LEU ALA ALA SER GLY ILE LYS SER PHE ARG LYS
SEQRES 17 I 273 MET LEU ALA ALA ASN GLU ARG GLN THR PRO LEU ARG ARG
SEQRES 18 I 273 ASN VAL THR ILE GLU GLU VAL GLY ASN ALA GLY ALA PHE
SEQRES 19 I 273 LEU CYS SER ASP LEU ALA SER GLY ILE SER GLY GLU ILE
SEQRES 20 I 273 LEU TYR VAL ASP GLY GLY PHE ASN THR THR ALA MET GLY
SEQRES 21 I 273 PRO LEU ASP ASP ASP LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 J 273 MET GLY PHE LEU THR GLY LYS ARG ALA LEU ILE VAL GLY
SEQRES 2 J 273 VAL ALA SER LYS LEU SER ILE ALA SER GLY ILE ALA ALA
SEQRES 3 J 273 ALA MET HIS ARG GLU GLY ALA GLU LEU ALA PHE THR TYR
SEQRES 4 J 273 GLN ASN ASP LYS LEU ARG GLY ARG VAL GLU GLU PHE ALA
SEQRES 5 J 273 SER GLY TRP GLY SER ARG PRO GLU LEU CYS PHE PRO CYS
SEQRES 6 J 273 ASP VAL ALA ASP ASP SER GLN ILE GLU ALA VAL PHE ALA
SEQRES 7 J 273 ALA LEU GLY LYS HIS TRP ASP GLY LEU ASP ILE ILE VAL
SEQRES 8 J 273 HIS SER VAL GLY PHE ALA PRO GLY ASP GLN LEU ASP GLY
SEQRES 9 J 273 ASP PHE THR ALA VAL THR THR ARG GLU GLY PHE ARG ILE
SEQRES 10 J 273 ALA HIS ASP ILE SER ALA TYR SER PHE ILE ALA LEU ALA
SEQRES 11 J 273 LYS ALA GLY ARG GLU MET MET LYS GLY ARG ASN GLY SER
SEQRES 12 J 273 LEU LEU THR LEU SER TYR LEU GLY ALA GLU ARG THR MET
SEQRES 13 J 273 PRO ASN TYR ASN VAL MET GLY MET ALA LYS ALA SER LEU
SEQRES 14 J 273 GLU ALA GLY VAL ARG TYR LEU ALA GLY SER LEU GLY ALA
SEQRES 15 J 273 GLU GLY THR ARG VAL ASN ALA VAL SER ALA GLY PRO ILE
SEQRES 16 J 273 ARG THR LEU ALA ALA SER GLY ILE LYS SER PHE ARG LYS
SEQRES 17 J 273 MET LEU ALA ALA ASN GLU ARG GLN THR PRO LEU ARG ARG
SEQRES 18 J 273 ASN VAL THR ILE GLU GLU VAL GLY ASN ALA GLY ALA PHE
SEQRES 19 J 273 LEU CYS SER ASP LEU ALA SER GLY ILE SER GLY GLU ILE
SEQRES 20 J 273 LEU TYR VAL ASP GLY GLY PHE ASN THR THR ALA MET GLY
SEQRES 21 J 273 PRO LEU ASP ASP ASP LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 K 273 MET GLY PHE LEU THR GLY LYS ARG ALA LEU ILE VAL GLY
SEQRES 2 K 273 VAL ALA SER LYS LEU SER ILE ALA SER GLY ILE ALA ALA
SEQRES 3 K 273 ALA MET HIS ARG GLU GLY ALA GLU LEU ALA PHE THR TYR
SEQRES 4 K 273 GLN ASN ASP LYS LEU ARG GLY ARG VAL GLU GLU PHE ALA
SEQRES 5 K 273 SER GLY TRP GLY SER ARG PRO GLU LEU CYS PHE PRO CYS
SEQRES 6 K 273 ASP VAL ALA ASP ASP SER GLN ILE GLU ALA VAL PHE ALA
SEQRES 7 K 273 ALA LEU GLY LYS HIS TRP ASP GLY LEU ASP ILE ILE VAL
SEQRES 8 K 273 HIS SER VAL GLY PHE ALA PRO GLY ASP GLN LEU ASP GLY
SEQRES 9 K 273 ASP PHE THR ALA VAL THR THR ARG GLU GLY PHE ARG ILE
SEQRES 10 K 273 ALA HIS ASP ILE SER ALA TYR SER PHE ILE ALA LEU ALA
SEQRES 11 K 273 LYS ALA GLY ARG GLU MET MET LYS GLY ARG ASN GLY SER
SEQRES 12 K 273 LEU LEU THR LEU SER TYR LEU GLY ALA GLU ARG THR MET
SEQRES 13 K 273 PRO ASN TYR ASN VAL MET GLY MET ALA LYS ALA SER LEU
SEQRES 14 K 273 GLU ALA GLY VAL ARG TYR LEU ALA GLY SER LEU GLY ALA
SEQRES 15 K 273 GLU GLY THR ARG VAL ASN ALA VAL SER ALA GLY PRO ILE
SEQRES 16 K 273 ARG THR LEU ALA ALA SER GLY ILE LYS SER PHE ARG LYS
SEQRES 17 K 273 MET LEU ALA ALA ASN GLU ARG GLN THR PRO LEU ARG ARG
SEQRES 18 K 273 ASN VAL THR ILE GLU GLU VAL GLY ASN ALA GLY ALA PHE
SEQRES 19 K 273 LEU CYS SER ASP LEU ALA SER GLY ILE SER GLY GLU ILE
SEQRES 20 K 273 LEU TYR VAL ASP GLY GLY PHE ASN THR THR ALA MET GLY
SEQRES 21 K 273 PRO LEU ASP ASP ASP LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 L 273 MET GLY PHE LEU THR GLY LYS ARG ALA LEU ILE VAL GLY
SEQRES 2 L 273 VAL ALA SER LYS LEU SER ILE ALA SER GLY ILE ALA ALA
SEQRES 3 L 273 ALA MET HIS ARG GLU GLY ALA GLU LEU ALA PHE THR TYR
SEQRES 4 L 273 GLN ASN ASP LYS LEU ARG GLY ARG VAL GLU GLU PHE ALA
SEQRES 5 L 273 SER GLY TRP GLY SER ARG PRO GLU LEU CYS PHE PRO CYS
SEQRES 6 L 273 ASP VAL ALA ASP ASP SER GLN ILE GLU ALA VAL PHE ALA
SEQRES 7 L 273 ALA LEU GLY LYS HIS TRP ASP GLY LEU ASP ILE ILE VAL
SEQRES 8 L 273 HIS SER VAL GLY PHE ALA PRO GLY ASP GLN LEU ASP GLY
SEQRES 9 L 273 ASP PHE THR ALA VAL THR THR ARG GLU GLY PHE ARG ILE
SEQRES 10 L 273 ALA HIS ASP ILE SER ALA TYR SER PHE ILE ALA LEU ALA
SEQRES 11 L 273 LYS ALA GLY ARG GLU MET MET LYS GLY ARG ASN GLY SER
SEQRES 12 L 273 LEU LEU THR LEU SER TYR LEU GLY ALA GLU ARG THR MET
SEQRES 13 L 273 PRO ASN TYR ASN VAL MET GLY MET ALA LYS ALA SER LEU
SEQRES 14 L 273 GLU ALA GLY VAL ARG TYR LEU ALA GLY SER LEU GLY ALA
SEQRES 15 L 273 GLU GLY THR ARG VAL ASN ALA VAL SER ALA GLY PRO ILE
SEQRES 16 L 273 ARG THR LEU ALA ALA SER GLY ILE LYS SER PHE ARG LYS
SEQRES 17 L 273 MET LEU ALA ALA ASN GLU ARG GLN THR PRO LEU ARG ARG
SEQRES 18 L 273 ASN VAL THR ILE GLU GLU VAL GLY ASN ALA GLY ALA PHE
SEQRES 19 L 273 LEU CYS SER ASP LEU ALA SER GLY ILE SER GLY GLU ILE
SEQRES 20 L 273 LEU TYR VAL ASP GLY GLY PHE ASN THR THR ALA MET GLY
SEQRES 21 L 273 PRO LEU ASP ASP ASP LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 M 273 MET GLY PHE LEU THR GLY LYS ARG ALA LEU ILE VAL GLY
SEQRES 2 M 273 VAL ALA SER LYS LEU SER ILE ALA SER GLY ILE ALA ALA
SEQRES 3 M 273 ALA MET HIS ARG GLU GLY ALA GLU LEU ALA PHE THR TYR
SEQRES 4 M 273 GLN ASN ASP LYS LEU ARG GLY ARG VAL GLU GLU PHE ALA
SEQRES 5 M 273 SER GLY TRP GLY SER ARG PRO GLU LEU CYS PHE PRO CYS
SEQRES 6 M 273 ASP VAL ALA ASP ASP SER GLN ILE GLU ALA VAL PHE ALA
SEQRES 7 M 273 ALA LEU GLY LYS HIS TRP ASP GLY LEU ASP ILE ILE VAL
SEQRES 8 M 273 HIS SER VAL GLY PHE ALA PRO GLY ASP GLN LEU ASP GLY
SEQRES 9 M 273 ASP PHE THR ALA VAL THR THR ARG GLU GLY PHE ARG ILE
SEQRES 10 M 273 ALA HIS ASP ILE SER ALA TYR SER PHE ILE ALA LEU ALA
SEQRES 11 M 273 LYS ALA GLY ARG GLU MET MET LYS GLY ARG ASN GLY SER
SEQRES 12 M 273 LEU LEU THR LEU SER TYR LEU GLY ALA GLU ARG THR MET
SEQRES 13 M 273 PRO ASN TYR ASN VAL MET GLY MET ALA LYS ALA SER LEU
SEQRES 14 M 273 GLU ALA GLY VAL ARG TYR LEU ALA GLY SER LEU GLY ALA
SEQRES 15 M 273 GLU GLY THR ARG VAL ASN ALA VAL SER ALA GLY PRO ILE
SEQRES 16 M 273 ARG THR LEU ALA ALA SER GLY ILE LYS SER PHE ARG LYS
SEQRES 17 M 273 MET LEU ALA ALA ASN GLU ARG GLN THR PRO LEU ARG ARG
SEQRES 18 M 273 ASN VAL THR ILE GLU GLU VAL GLY ASN ALA GLY ALA PHE
SEQRES 19 M 273 LEU CYS SER ASP LEU ALA SER GLY ILE SER GLY GLU ILE
SEQRES 20 M 273 LEU TYR VAL ASP GLY GLY PHE ASN THR THR ALA MET GLY
SEQRES 21 M 273 PRO LEU ASP ASP ASP LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 N 273 MET GLY PHE LEU THR GLY LYS ARG ALA LEU ILE VAL GLY
SEQRES 2 N 273 VAL ALA SER LYS LEU SER ILE ALA SER GLY ILE ALA ALA
SEQRES 3 N 273 ALA MET HIS ARG GLU GLY ALA GLU LEU ALA PHE THR TYR
SEQRES 4 N 273 GLN ASN ASP LYS LEU ARG GLY ARG VAL GLU GLU PHE ALA
SEQRES 5 N 273 SER GLY TRP GLY SER ARG PRO GLU LEU CYS PHE PRO CYS
SEQRES 6 N 273 ASP VAL ALA ASP ASP SER GLN ILE GLU ALA VAL PHE ALA
SEQRES 7 N 273 ALA LEU GLY LYS HIS TRP ASP GLY LEU ASP ILE ILE VAL
SEQRES 8 N 273 HIS SER VAL GLY PHE ALA PRO GLY ASP GLN LEU ASP GLY
SEQRES 9 N 273 ASP PHE THR ALA VAL THR THR ARG GLU GLY PHE ARG ILE
SEQRES 10 N 273 ALA HIS ASP ILE SER ALA TYR SER PHE ILE ALA LEU ALA
SEQRES 11 N 273 LYS ALA GLY ARG GLU MET MET LYS GLY ARG ASN GLY SER
SEQRES 12 N 273 LEU LEU THR LEU SER TYR LEU GLY ALA GLU ARG THR MET
SEQRES 13 N 273 PRO ASN TYR ASN VAL MET GLY MET ALA LYS ALA SER LEU
SEQRES 14 N 273 GLU ALA GLY VAL ARG TYR LEU ALA GLY SER LEU GLY ALA
SEQRES 15 N 273 GLU GLY THR ARG VAL ASN ALA VAL SER ALA GLY PRO ILE
SEQRES 16 N 273 ARG THR LEU ALA ALA SER GLY ILE LYS SER PHE ARG LYS
SEQRES 17 N 273 MET LEU ALA ALA ASN GLU ARG GLN THR PRO LEU ARG ARG
SEQRES 18 N 273 ASN VAL THR ILE GLU GLU VAL GLY ASN ALA GLY ALA PHE
SEQRES 19 N 273 LEU CYS SER ASP LEU ALA SER GLY ILE SER GLY GLU ILE
SEQRES 20 N 273 LEU TYR VAL ASP GLY GLY PHE ASN THR THR ALA MET GLY
SEQRES 21 N 273 PRO LEU ASP ASP ASP LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 O 273 MET GLY PHE LEU THR GLY LYS ARG ALA LEU ILE VAL GLY
SEQRES 2 O 273 VAL ALA SER LYS LEU SER ILE ALA SER GLY ILE ALA ALA
SEQRES 3 O 273 ALA MET HIS ARG GLU GLY ALA GLU LEU ALA PHE THR TYR
SEQRES 4 O 273 GLN ASN ASP LYS LEU ARG GLY ARG VAL GLU GLU PHE ALA
SEQRES 5 O 273 SER GLY TRP GLY SER ARG PRO GLU LEU CYS PHE PRO CYS
SEQRES 6 O 273 ASP VAL ALA ASP ASP SER GLN ILE GLU ALA VAL PHE ALA
SEQRES 7 O 273 ALA LEU GLY LYS HIS TRP ASP GLY LEU ASP ILE ILE VAL
SEQRES 8 O 273 HIS SER VAL GLY PHE ALA PRO GLY ASP GLN LEU ASP GLY
SEQRES 9 O 273 ASP PHE THR ALA VAL THR THR ARG GLU GLY PHE ARG ILE
SEQRES 10 O 273 ALA HIS ASP ILE SER ALA TYR SER PHE ILE ALA LEU ALA
SEQRES 11 O 273 LYS ALA GLY ARG GLU MET MET LYS GLY ARG ASN GLY SER
SEQRES 12 O 273 LEU LEU THR LEU SER TYR LEU GLY ALA GLU ARG THR MET
SEQRES 13 O 273 PRO ASN TYR ASN VAL MET GLY MET ALA LYS ALA SER LEU
SEQRES 14 O 273 GLU ALA GLY VAL ARG TYR LEU ALA GLY SER LEU GLY ALA
SEQRES 15 O 273 GLU GLY THR ARG VAL ASN ALA VAL SER ALA GLY PRO ILE
SEQRES 16 O 273 ARG THR LEU ALA ALA SER GLY ILE LYS SER PHE ARG LYS
SEQRES 17 O 273 MET LEU ALA ALA ASN GLU ARG GLN THR PRO LEU ARG ARG
SEQRES 18 O 273 ASN VAL THR ILE GLU GLU VAL GLY ASN ALA GLY ALA PHE
SEQRES 19 O 273 LEU CYS SER ASP LEU ALA SER GLY ILE SER GLY GLU ILE
SEQRES 20 O 273 LEU TYR VAL ASP GLY GLY PHE ASN THR THR ALA MET GLY
SEQRES 21 O 273 PRO LEU ASP ASP ASP LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 P 273 MET GLY PHE LEU THR GLY LYS ARG ALA LEU ILE VAL GLY
SEQRES 2 P 273 VAL ALA SER LYS LEU SER ILE ALA SER GLY ILE ALA ALA
SEQRES 3 P 273 ALA MET HIS ARG GLU GLY ALA GLU LEU ALA PHE THR TYR
SEQRES 4 P 273 GLN ASN ASP LYS LEU ARG GLY ARG VAL GLU GLU PHE ALA
SEQRES 5 P 273 SER GLY TRP GLY SER ARG PRO GLU LEU CYS PHE PRO CYS
SEQRES 6 P 273 ASP VAL ALA ASP ASP SER GLN ILE GLU ALA VAL PHE ALA
SEQRES 7 P 273 ALA LEU GLY LYS HIS TRP ASP GLY LEU ASP ILE ILE VAL
SEQRES 8 P 273 HIS SER VAL GLY PHE ALA PRO GLY ASP GLN LEU ASP GLY
SEQRES 9 P 273 ASP PHE THR ALA VAL THR THR ARG GLU GLY PHE ARG ILE
SEQRES 10 P 273 ALA HIS ASP ILE SER ALA TYR SER PHE ILE ALA LEU ALA
SEQRES 11 P 273 LYS ALA GLY ARG GLU MET MET LYS GLY ARG ASN GLY SER
SEQRES 12 P 273 LEU LEU THR LEU SER TYR LEU GLY ALA GLU ARG THR MET
SEQRES 13 P 273 PRO ASN TYR ASN VAL MET GLY MET ALA LYS ALA SER LEU
SEQRES 14 P 273 GLU ALA GLY VAL ARG TYR LEU ALA GLY SER LEU GLY ALA
SEQRES 15 P 273 GLU GLY THR ARG VAL ASN ALA VAL SER ALA GLY PRO ILE
SEQRES 16 P 273 ARG THR LEU ALA ALA SER GLY ILE LYS SER PHE ARG LYS
SEQRES 17 P 273 MET LEU ALA ALA ASN GLU ARG GLN THR PRO LEU ARG ARG
SEQRES 18 P 273 ASN VAL THR ILE GLU GLU VAL GLY ASN ALA GLY ALA PHE
SEQRES 19 P 273 LEU CYS SER ASP LEU ALA SER GLY ILE SER GLY GLU ILE
SEQRES 20 P 273 LEU TYR VAL ASP GLY GLY PHE ASN THR THR ALA MET GLY
SEQRES 21 P 273 PRO LEU ASP ASP ASP LEU GLU HIS HIS HIS HIS HIS HIS
FORMUL 17 HOH *357(H2 O)
HELIX 1 1 SER A 19 GLU A 31 1 13
HELIX 2 2 LEU A 44 TRP A 55 1 12
HELIX 3 3 ARG A 58 GLU A 60 5 3
HELIX 4 4 ASP A 69 GLY A 81 1 13
HELIX 5 5 PRO A 98 ASP A 103 5 6
HELIX 6 6 ASP A 105 THR A 110 1 6
HELIX 7 7 THR A 111 ALA A 123 1 13
HELIX 8 8 ALA A 123 GLY A 133 1 11
HELIX 9 9 GLY A 133 LYS A 138 1 6
HELIX 10 10 TYR A 149 GLU A 153 5 5
HELIX 11 11 ASN A 160 ALA A 182 1 23
HELIX 12 12 MET A 209 THR A 217 1 9
HELIX 13 13 THR A 224 CYS A 236 1 13
HELIX 14 14 SER A 237 SER A 241 5 5
HELIX 15 15 GLY A 253 THR A 257 5 5
HELIX 16 16 SER B 19 GLU B 31 1 13
HELIX 17 17 LEU B 44 GLY B 54 1 11
HELIX 18 18 ARG B 58 GLU B 60 5 3
HELIX 19 19 ASP B 69 GLY B 81 1 13
HELIX 20 20 PRO B 98 ASP B 103 5 6
HELIX 21 21 ASP B 105 THR B 110 1 6
HELIX 22 22 THR B 111 ALA B 123 1 13
HELIX 23 23 ALA B 123 GLY B 133 1 11
HELIX 24 24 TYR B 149 GLU B 153 5 5
HELIX 25 25 ASN B 160 GLY B 178 1 19
HELIX 26 26 ALA B 211 THR B 217 1 7
HELIX 27 27 THR B 224 SER B 237 1 14
HELIX 28 28 ASP B 238 SER B 241 5 4
HELIX 29 29 SER C 19 GLU C 31 1 13
HELIX 30 30 ASN C 41 TRP C 55 1 15
HELIX 31 31 ARG C 58 GLU C 60 5 3
HELIX 32 32 ASP C 69 GLY C 81 1 13
HELIX 33 33 PRO C 98 ASP C 103 5 6
HELIX 34 34 ASP C 105 THR C 110 1 6
HELIX 35 35 THR C 111 ALA C 123 1 13
HELIX 36 36 ALA C 123 GLY C 133 1 11
HELIX 37 37 TYR C 149 GLU C 153 5 5
HELIX 38 38 VAL C 161 GLY C 181 1 21
HELIX 39 39 LEU C 210 THR C 217 1 8
HELIX 40 40 THR C 224 CYS C 236 1 13
HELIX 41 41 SER C 237 SER C 241 5 5
HELIX 42 42 GLY C 253 THR C 257 5 5
HELIX 43 43 ILE D 20 GLU D 31 1 12
HELIX 44 44 ASN D 41 TRP D 55 1 15
HELIX 45 45 ARG D 58 GLU D 60 5 3
HELIX 46 46 ASP D 69 GLY D 81 1 13
HELIX 47 47 PRO D 98 LEU D 102 5 5
HELIX 48 48 ASP D 105 THR D 110 1 6
HELIX 49 49 THR D 111 ALA D 123 1 13
HELIX 50 50 ALA D 123 ALA D 132 1 10
HELIX 51 51 GLY D 133 LYS D 138 5 6
HELIX 52 52 TYR D 149 GLU D 153 5 5
HELIX 53 53 VAL D 161 GLY D 181 1 21
HELIX 54 54 MET D 209 ARG D 215 1 7
HELIX 55 55 THR D 224 LEU D 235 1 12
HELIX 56 56 CYS D 236 SER D 241 5 6
HELIX 57 57 GLY D 253 THR D 257 5 5
HELIX 58 58 SER E 19 GLU E 31 1 13
HELIX 59 59 LEU E 44 SER E 53 1 10
HELIX 60 60 ASP E 69 TRP E 84 1 16
HELIX 61 61 PRO E 98 ASP E 103 5 6
HELIX 62 62 ASP E 105 THR E 110 1 6
HELIX 63 63 THR E 111 ALA E 123 1 13
HELIX 64 64 ALA E 123 GLY E 133 1 11
HELIX 65 65 GLY E 133 LYS E 138 1 6
HELIX 66 66 VAL E 161 LEU E 180 1 20
HELIX 67 67 ALA E 212 THR E 217 1 6
HELIX 68 68 THR E 224 CYS E 236 1 13
HELIX 69 69 SER E 237 SER E 241 5 5
HELIX 70 70 GLY E 253 THR E 257 5 5
HELIX 71 71 SER F 19 GLU F 31 1 13
HELIX 72 72 ASN F 41 LYS F 43 5 3
HELIX 73 73 LEU F 44 TRP F 55 1 12
HELIX 74 74 ARG F 58 GLU F 60 5 3
HELIX 75 75 ASP F 69 GLY F 81 1 13
HELIX 76 76 PRO F 98 LEU F 102 5 5
HELIX 77 77 ASP F 105 THR F 110 1 6
HELIX 78 78 THR F 111 GLY F 133 1 23
HELIX 79 79 GLY F 133 LYS F 138 1 6
HELIX 80 80 TYR F 149 GLU F 153 5 5
HELIX 81 81 ASN F 160 LEU F 180 1 21
HELIX 82 82 ALA F 211 THR F 217 1 7
HELIX 83 83 THR F 224 CYS F 236 1 13
HELIX 84 84 SER F 237 SER F 241 5 5
HELIX 85 85 GLY F 253 THR F 257 5 5
HELIX 86 86 ILE G 20 GLU G 31 1 12
HELIX 87 87 ASN G 41 SER G 53 1 13
HELIX 88 88 ARG G 58 GLU G 60 5 3
HELIX 89 89 ASP G 69 GLY G 81 1 13
HELIX 90 90 PRO G 98 ASP G 103 5 6
HELIX 91 91 ASP G 105 THR G 110 1 6
HELIX 92 92 THR G 111 ALA G 123 1 13
HELIX 93 93 ALA G 123 GLY G 133 1 11
HELIX 94 94 TYR G 149 GLU G 153 5 5
HELIX 95 95 ASN G 160 GLY G 181 1 22
HELIX 96 96 ALA G 212 GLN G 216 5 5
HELIX 97 97 THR G 224 CYS G 236 1 13
HELIX 98 98 SER G 237 SER G 241 5 5
HELIX 99 99 GLY G 253 THR G 257 5 5
HELIX 100 100 SER H 19 GLU H 31 1 13
HELIX 101 101 LEU H 44 TRP H 55 1 12
HELIX 102 102 ARG H 58 GLU H 60 5 3
HELIX 103 103 ASP H 69 GLY H 81 1 13
HELIX 104 104 PRO H 98 ASP H 103 5 6
HELIX 105 105 ASP H 105 THR H 110 1 6
HELIX 106 106 THR H 111 GLY H 133 1 23
HELIX 107 107 ARG H 134 LYS H 138 5 5
HELIX 108 108 TYR H 149 GLU H 153 5 5
HELIX 109 109 TYR H 159 LEU H 180 1 22
HELIX 110 110 LYS H 208 THR H 217 1 10
HELIX 111 111 THR H 224 CYS H 236 1 13
HELIX 112 112 SER H 237 SER H 241 5 5
HELIX 113 113 GLY H 253 THR H 257 5 5
HELIX 114 114 SER I 19 GLU I 31 1 13
HELIX 115 115 ASN I 41 LYS I 43 5 3
HELIX 116 116 LEU I 44 SER I 53 1 10
HELIX 117 117 ARG I 58 GLU I 60 5 3
HELIX 118 118 ASP I 69 GLY I 81 1 13
HELIX 119 119 PRO I 98 ASP I 103 5 6
HELIX 120 120 ASP I 105 THR I 110 1 6
HELIX 121 121 THR I 111 GLY I 133 1 23
HELIX 122 122 TYR I 149 GLU I 153 5 5
HELIX 123 123 ASN I 160 ALA I 182 1 23
HELIX 124 124 ALA I 211 THR I 217 1 7
HELIX 125 125 THR I 224 CYS I 236 1 13
HELIX 126 126 SER I 237 SER I 241 5 5
HELIX 127 127 GLY I 253 THR I 257 5 5
HELIX 128 128 SER J 19 GLU J 31 1 13
HELIX 129 129 LEU J 44 TRP J 55 1 12
HELIX 130 130 ARG J 58 GLU J 60 5 3
HELIX 131 131 ASP J 69 GLY J 81 1 13
HELIX 132 132 ASP J 105 THR J 110 1 6
HELIX 133 133 THR J 111 ALA J 123 1 13
HELIX 134 134 ALA J 123 GLY J 133 1 11
HELIX 135 135 GLY J 133 LYS J 138 1 6
HELIX 136 136 TYR J 149 GLU J 153 5 5
HELIX 137 137 TYR J 159 GLY J 181 1 23
HELIX 138 138 ALA J 182 GLY J 184 5 3
HELIX 139 139 LEU J 210 THR J 217 1 8
HELIX 140 140 THR J 224 LEU J 235 1 12
HELIX 141 141 SER J 237 SER J 241 5 5
HELIX 142 142 GLY J 253 THR J 257 5 5
HELIX 143 143 SER K 19 ARG K 30 1 12
HELIX 144 144 LEU K 44 TRP K 55 1 12
HELIX 145 145 ARG K 58 GLU K 60 5 3
HELIX 146 146 ASP K 69 TRP K 84 1 16
HELIX 147 147 PRO K 98 ASP K 103 5 6
HELIX 148 148 ASP K 105 THR K 110 1 6
HELIX 149 149 THR K 111 GLY K 133 1 23
HELIX 150 150 TYR K 149 GLU K 153 5 5
HELIX 151 151 VAL K 161 LEU K 180 1 20
HELIX 152 152 ALA K 211 THR K 217 1 7
HELIX 153 153 THR K 224 CYS K 236 1 13
HELIX 154 154 GLY K 253 THR K 257 5 5
HELIX 155 155 ILE L 20 GLU L 31 1 12
HELIX 156 156 LEU L 44 SER L 53 1 10
HELIX 157 157 GLY L 54 GLY L 56 5 3
HELIX 158 158 ARG L 58 GLU L 60 5 3
HELIX 159 159 ASP L 69 GLY L 81 1 13
HELIX 160 160 PRO L 98 ASP L 103 5 6
HELIX 161 161 ASP L 105 THR L 110 1 6
HELIX 162 162 THR L 111 ALA L 123 1 13
HELIX 163 163 ALA L 123 GLY L 133 1 11
HELIX 164 164 TYR L 149 GLU L 153 5 5
HELIX 165 165 ASN L 160 GLY L 181 1 22
HELIX 166 166 ALA L 211 THR L 217 1 7
HELIX 167 167 THR L 224 SER L 237 1 14
HELIX 168 168 GLY L 253 THR L 257 5 5
HELIX 169 169 SER M 19 GLU M 31 1 13
HELIX 170 170 ASN M 41 LYS M 43 5 3
HELIX 171 171 LEU M 44 GLY M 54 1 11
HELIX 172 172 ARG M 58 GLU M 60 5 3
HELIX 173 173 ASP M 69 TRP M 84 1 16
HELIX 174 174 PRO M 98 LEU M 102 5 5
HELIX 175 175 ASP M 105 THR M 110 1 6
HELIX 176 176 THR M 111 ALA M 123 1 13
HELIX 177 177 ALA M 123 GLY M 133 1 11
HELIX 178 178 ARG M 134 LYS M 138 5 5
HELIX 179 179 TYR M 149 GLU M 153 5 5
HELIX 180 180 ASN M 160 GLY M 181 1 22
HELIX 181 181 ALA M 182 GLY M 184 5 3
HELIX 182 182 LEU M 210 THR M 217 1 8
HELIX 183 183 THR M 224 CYS M 236 1 13
HELIX 184 184 SER M 237 SER M 241 5 5
HELIX 185 185 GLY M 253 THR M 257 5 5
HELIX 186 186 SER N 19 GLU N 31 1 13
HELIX 187 187 ASP N 42 TRP N 55 1 14
HELIX 188 188 ARG N 58 GLU N 60 5 3
HELIX 189 189 ASP N 69 GLY N 81 1 13
HELIX 190 190 PRO N 98 LEU N 102 5 5
HELIX 191 191 ASP N 105 THR N 110 1 6
HELIX 192 192 THR N 111 ALA N 123 1 13
HELIX 193 193 ALA N 123 LYS N 138 1 16
HELIX 194 194 TYR N 149 GLU N 153 5 5
HELIX 195 195 VAL N 161 GLY N 181 1 21
HELIX 196 196 MET N 209 ALA N 211 5 3
HELIX 197 197 ALA N 212 THR N 217 1 6
HELIX 198 198 THR N 224 CYS N 236 1 13
HELIX 199 199 SER N 237 SER N 241 5 5
HELIX 200 200 GLY N 253 THR N 257 5 5
HELIX 201 201 SER O 19 GLU O 31 1 13
HELIX 202 202 LEU O 44 GLY O 54 1 11
HELIX 203 203 ASP O 69 GLY O 81 1 13
HELIX 204 204 PRO O 98 ASP O 103 5 6
HELIX 205 205 ASP O 105 THR O 110 1 6
HELIX 206 206 THR O 111 ILE O 121 1 11
HELIX 207 207 ALA O 123 LYS O 138 1 16
HELIX 208 208 TYR O 149 GLU O 153 5 5
HELIX 209 209 ASN O 160 GLY O 181 1 22
HELIX 210 210 ALA O 182 GLY O 184 5 3
HELIX 211 211 THR O 224 SER O 237 1 14
HELIX 212 212 ASP O 238 SER O 241 5 4
HELIX 213 213 SER P 19 GLU P 31 1 13
HELIX 214 214 ASN P 41 TRP P 55 1 15
HELIX 215 215 ARG P 58 GLU P 60 5 3
HELIX 216 216 ASP P 69 LYS P 82 1 14
HELIX 217 217 PRO P 98 ASP P 103 5 6
HELIX 218 218 ASP P 105 THR P 110 1 6
HELIX 219 219 THR P 111 ALA P 123 1 13
HELIX 220 220 ALA P 123 GLY P 133 1 11
HELIX 221 221 GLY P 133 LYS P 138 1 6
HELIX 222 222 TYR P 149 GLU P 153 5 5
HELIX 223 223 VAL P 161 LEU P 180 1 20
HELIX 224 224 MET P 209 THR P 217 1 9
HELIX 225 225 THR P 224 CYS P 236 1 13
HELIX 226 226 SER P 237 SER P 241 5 5
HELIX 227 227 GLY P 253 THR P 257 5 5
SHEET 1 A 7 CYS A 62 PRO A 64 0
SHEET 2 A 7 GLU A 34 TYR A 39 1 N TYR A 39 O PHE A 63
SHEET 3 A 7 ARG A 8 VAL A 12 1 N ILE A 11 O ALA A 36
SHEET 4 A 7 ILE A 89 HIS A 92 1 O VAL A 91 N VAL A 12
SHEET 5 A 7 SER A 143 LEU A 147 1 O LEU A 145 N HIS A 92
SHEET 6 A 7 ARG A 186 ALA A 192 1 O ARG A 186 N LEU A 144
SHEET 7 A 7 ILE A 247 VAL A 250 1 O LEU A 248 N ALA A 189
SHEET 1 B 7 CYS B 62 PRO B 64 0
SHEET 2 B 7 GLU B 34 TYR B 39 1 N PHE B 37 O PHE B 63
SHEET 3 B 7 ARG B 8 VAL B 12 1 N ILE B 11 O ALA B 36
SHEET 4 B 7 ILE B 89 HIS B 92 1 O ILE B 89 N LEU B 10
SHEET 5 B 7 SER B 143 SER B 148 1 O LEU B 145 N HIS B 92
SHEET 6 B 7 ARG B 186 ALA B 192 1 O VAL B 190 N SER B 148
SHEET 7 B 7 GLU B 246 VAL B 250 1 O LEU B 248 N SER B 191
SHEET 1 C 7 CYS C 62 PRO C 64 0
SHEET 2 C 7 GLU C 34 TYR C 39 1 N TYR C 39 O PHE C 63
SHEET 3 C 7 ARG C 8 VAL C 12 1 N ILE C 11 O ALA C 36
SHEET 4 C 7 ILE C 89 HIS C 92 1 O ILE C 89 N LEU C 10
SHEET 5 C 7 SER C 143 SER C 148 1 O LEU C 145 N HIS C 92
SHEET 6 C 7 ARG C 186 ALA C 192 1 O ASN C 188 N LEU C 144
SHEET 7 C 7 GLU C 246 VAL C 250 1 O LEU C 248 N ALA C 189
SHEET 1 D 7 CYS D 62 PRO D 64 0
SHEET 2 D 7 GLU D 34 TYR D 39 1 N TYR D 39 O PHE D 63
SHEET 3 D 7 ARG D 8 VAL D 12 1 N ALA D 9 O GLU D 34
SHEET 4 D 7 ILE D 89 HIS D 92 1 O ILE D 89 N LEU D 10
SHEET 5 D 7 SER D 143 SER D 148 1 O LEU D 145 N ILE D 90
SHEET 6 D 7 ARG D 186 ALA D 192 1 O VAL D 190 N THR D 146
SHEET 7 D 7 ILE D 247 VAL D 250 1 O LEU D 248 N SER D 191
SHEET 1 E 7 PHE E 63 PRO E 64 0
SHEET 2 E 7 GLU E 34 TYR E 39 1 N TYR E 39 O PHE E 63
SHEET 3 E 7 ARG E 8 VAL E 12 1 N ALA E 9 O ALA E 36
SHEET 4 E 7 ILE E 89 HIS E 92 1 O ILE E 89 N ARG E 8
SHEET 5 E 7 SER E 143 SER E 148 1 O LEU E 145 N ILE E 90
SHEET 6 E 7 ARG E 186 ALA E 192 1 O ARG E 186 N LEU E 144
SHEET 7 E 7 ILE E 247 VAL E 250 1 O LEU E 248 N SER E 191
SHEET 1 F 7 CYS F 62 PRO F 64 0
SHEET 2 F 7 GLU F 34 TYR F 39 1 N PHE F 37 O PHE F 63
SHEET 3 F 7 ARG F 8 VAL F 12 1 N ILE F 11 O ALA F 36
SHEET 4 F 7 ILE F 89 HIS F 92 1 O VAL F 91 N LEU F 10
SHEET 5 F 7 SER F 143 SER F 148 1 O LEU F 145 N ILE F 90
SHEET 6 F 7 ARG F 186 ALA F 192 1 O ASN F 188 N LEU F 144
SHEET 7 F 7 ILE F 247 VAL F 250 1 O LEU F 248 N SER F 191
SHEET 1 G 7 CYS G 62 PRO G 64 0
SHEET 2 G 7 GLU G 34 TYR G 39 1 N PHE G 37 O PHE G 63
SHEET 3 G 7 ARG G 8 VAL G 12 1 N ILE G 11 O ALA G 36
SHEET 4 G 7 ILE G 89 HIS G 92 1 O VAL G 91 N LEU G 10
SHEET 5 G 7 SER G 143 SER G 148 1 O LEU G 145 N ILE G 90
SHEET 6 G 7 ARG G 186 ALA G 192 1 O ASN G 188 N LEU G 144
SHEET 7 G 7 ILE G 247 VAL G 250 1 O LEU G 248 N SER G 191
SHEET 1 H 7 CYS H 62 PRO H 64 0
SHEET 2 H 7 GLU H 34 TYR H 39 1 N PHE H 37 O PHE H 63
SHEET 3 H 7 ARG H 8 VAL H 12 1 N ILE H 11 O ALA H 36
SHEET 4 H 7 ILE H 89 HIS H 92 1 O VAL H 91 N VAL H 12
SHEET 5 H 7 SER H 143 SER H 148 1 O LEU H 145 N ILE H 90
SHEET 6 H 7 ARG H 186 ALA H 192 1 O ARG H 186 N LEU H 144
SHEET 7 H 7 ILE H 247 VAL H 250 1 O LEU H 248 N ALA H 189
SHEET 1 I 7 CYS I 62 PRO I 64 0
SHEET 2 I 7 GLU I 34 TYR I 39 1 N TYR I 39 O PHE I 63
SHEET 3 I 7 ARG I 8 VAL I 12 1 N ALA I 9 O ALA I 36
SHEET 4 I 7 ILE I 89 HIS I 92 1 O VAL I 91 N LEU I 10
SHEET 5 I 7 SER I 143 SER I 148 1 O LEU I 145 N HIS I 92
SHEET 6 I 7 ARG I 186 ALA I 192 1 O ARG I 186 N LEU I 144
SHEET 7 I 7 ILE I 247 VAL I 250 1 O VAL I 250 N SER I 191
SHEET 1 J 7 CYS J 62 PRO J 64 0
SHEET 2 J 7 GLU J 34 TYR J 39 1 N PHE J 37 O PHE J 63
SHEET 3 J 7 ARG J 8 VAL J 12 1 N ILE J 11 O ALA J 36
SHEET 4 J 7 ILE J 89 HIS J 92 1 O ILE J 89 N LEU J 10
SHEET 5 J 7 SER J 143 SER J 148 1 O LEU J 145 N HIS J 92
SHEET 6 J 7 ARG J 186 ALA J 192 1 O ARG J 186 N LEU J 144
SHEET 7 J 7 GLU J 246 VAL J 250 1 O LEU J 248 N ALA J 189
SHEET 1 K 7 CYS K 62 PRO K 64 0
SHEET 2 K 7 GLU K 34 TYR K 39 1 N TYR K 39 O PHE K 63
SHEET 3 K 7 ARG K 8 VAL K 12 1 N ILE K 11 O ALA K 36
SHEET 4 K 7 ILE K 89 HIS K 92 1 O VAL K 91 N LEU K 10
SHEET 5 K 7 SER K 143 SER K 148 1 O LEU K 145 N HIS K 92
SHEET 6 K 7 ARG K 186 ALA K 192 1 O ARG K 186 N LEU K 144
SHEET 7 K 7 ILE K 247 VAL K 250 1 O LEU K 248 N SER K 191
SHEET 1 L 7 CYS L 62 PRO L 64 0
SHEET 2 L 7 GLU L 34 TYR L 39 1 N TYR L 39 O PHE L 63
SHEET 3 L 7 ARG L 8 VAL L 12 1 N ALA L 9 O ALA L 36
SHEET 4 L 7 ILE L 89 HIS L 92 1 O VAL L 91 N LEU L 10
SHEET 5 L 7 SER L 143 SER L 148 1 O LEU L 145 N ILE L 90
SHEET 6 L 7 ARG L 186 SER L 191 1 O ASN L 188 N LEU L 144
SHEET 7 L 7 GLU L 246 LEU L 248 1 O LEU L 248 N ALA L 189
SHEET 1 M 7 CYS M 62 PRO M 64 0
SHEET 2 M 7 GLU M 34 TYR M 39 1 N PHE M 37 O PHE M 63
SHEET 3 M 7 ARG M 8 VAL M 12 1 N ALA M 9 O GLU M 34
SHEET 4 M 7 ILE M 89 HIS M 92 1 O ILE M 89 N LEU M 10
SHEET 5 M 7 SER M 143 SER M 148 1 O LEU M 145 N HIS M 92
SHEET 6 M 7 ARG M 186 ALA M 192 1 O ARG M 186 N LEU M 144
SHEET 7 M 7 ILE M 247 VAL M 250 1 O LEU M 248 N SER M 191
SHEET 1 N 7 CYS N 62 PRO N 64 0
SHEET 2 N 7 GLU N 34 TYR N 39 1 N PHE N 37 O PHE N 63
SHEET 3 N 7 ARG N 8 VAL N 12 1 N ILE N 11 O ALA N 36
SHEET 4 N 7 ILE N 89 HIS N 92 1 O VAL N 91 N LEU N 10
SHEET 5 N 7 SER N 143 SER N 148 1 O LEU N 145 N HIS N 92
SHEET 6 N 7 ARG N 186 ALA N 192 1 O ARG N 186 N LEU N 144
SHEET 7 N 7 ILE N 247 VAL N 250 1 O VAL N 250 N SER N 191
SHEET 1 O 5 ALA O 9 VAL O 12 0
SHEET 2 O 5 ILE O 89 HIS O 92 1 O VAL O 91 N LEU O 10
SHEET 3 O 5 SER O 143 SER O 148 1 O LEU O 145 N ILE O 90
SHEET 4 O 5 ARG O 186 ALA O 192 1 O VAL O 190 N THR O 146
SHEET 5 O 5 GLU O 246 VAL O 250 1 O LEU O 248 N SER O 191
SHEET 1 P 2 PHE O 37 TYR O 39 0
SHEET 2 P 2 CYS O 62 PRO O 64 1 O PHE O 63 N TYR O 39
SHEET 1 Q 7 CYS P 62 PRO P 64 0
SHEET 2 Q 7 GLU P 34 TYR P 39 1 N TYR P 39 O PHE P 63
SHEET 3 Q 7 ARG P 8 VAL P 12 1 N ALA P 9 O GLU P 34
SHEET 4 Q 7 ILE P 89 HIS P 92 1 O ILE P 89 N LEU P 10
SHEET 5 Q 7 SER P 143 SER P 148 1 O LEU P 145 N HIS P 92
SHEET 6 Q 7 ARG P 186 ALA P 192 1 O ARG P 186 N LEU P 144
SHEET 7 Q 7 ILE P 247 VAL P 250 1 O LEU P 248 N SER P 191
CISPEP 1 ILE P 195 ARG P 196 0 10.38
CRYST1 117.322 155.844 129.448 90.00 111.06 90.00 P 1 21 1 32
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.008524 0.000000 0.003282 0.00000
SCALE2 0.000000 0.006417 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008278 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
