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HEADER HYDROLASE 11-MAY-22 7XRT
TITLE BACTEROIDES THETAIOTAOMICRON FERULIC ACID ESTERASE (BT_4077)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FERULIC ACID ESTERASE;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACTEROIDES THETAIOTAOMICRON VPI-5482;
SOURCE 3 ORGANISM_TAXID: 226186;
SOURCE 4 STRAIN: ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
SOURCE 5 VPI-5482 / E50;
SOURCE 6 GENE: BT_4077;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.M.DU,Y.L.WANG,F.J.XIN
REVDAT 1 22-NOV-23 7XRT 0
JRNL AUTH G.M.DU,Y.L.WANG,F.J.XIN
JRNL TITL INSIGHTS INTO THE REGULATORY MECHANISM OF BTFAE ACTIVITY BY
JRNL TITL 2 OLIGOMERIZATION AND A DISTINCT SUBSTRATE BINDING POCKET
JRNL TITL 3 ADJACENT TO THE ACTIVE SITE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.01 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.15.2_3472
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) : 2.01
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.35
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 229501
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.153
REMARK 3 R VALUE (WORKING SET) : 0.152
REMARK 3 FREE R VALUE : 0.172
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.920
REMARK 3 FREE R VALUE TEST SET COUNT : 11285
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 29.3510 - 6.2158 0.98 7706 374 0.1557 0.1552
REMARK 3 2 6.2158 - 4.9414 1.00 7533 404 0.1505 0.1785
REMARK 3 3 4.9414 - 4.3190 1.00 7491 383 0.1190 0.1319
REMARK 3 4 4.3190 - 3.9251 1.00 7382 406 0.1238 0.1234
REMARK 3 5 3.9251 - 3.6443 1.00 7397 415 0.1323 0.1450
REMARK 3 6 3.6443 - 3.4298 0.99 7393 368 0.1395 0.1552
REMARK 3 7 3.4298 - 3.2582 0.99 7378 377 0.1505 0.1743
REMARK 3 8 3.2582 - 3.1166 1.00 7348 388 0.1496 0.1702
REMARK 3 9 3.1166 - 2.9967 0.99 7355 379 0.1592 0.1889
REMARK 3 10 2.9967 - 2.8934 0.99 7296 371 0.1606 0.1768
REMARK 3 11 2.8934 - 2.8030 0.99 7351 358 0.1642 0.1831
REMARK 3 12 2.8030 - 2.7229 0.99 7318 371 0.1608 0.1935
REMARK 3 13 2.7229 - 2.6513 0.99 7289 380 0.1710 0.1928
REMARK 3 14 2.6513 - 2.5867 0.99 7294 384 0.1661 0.1872
REMARK 3 15 2.5867 - 2.5279 0.99 7247 399 0.1610 0.1978
REMARK 3 16 2.5279 - 2.4741 0.99 7227 407 0.1638 0.1702
REMARK 3 17 2.4741 - 2.4247 0.99 7244 389 0.1618 0.1894
REMARK 3 18 2.4247 - 2.3789 0.99 7294 372 0.1655 0.2016
REMARK 3 19 2.3789 - 2.3365 0.99 7232 378 0.1706 0.2128
REMARK 3 20 2.3365 - 2.2969 0.99 7222 360 0.1638 0.2039
REMARK 3 21 2.2969 - 2.2598 0.99 7235 347 0.1680 0.1854
REMARK 3 22 2.2598 - 2.2251 0.99 7256 328 0.1725 0.2125
REMARK 3 23 2.2251 - 2.1924 0.99 7218 397 0.1707 0.2156
REMARK 3 24 2.1924 - 2.1615 0.98 7187 387 0.1711 0.1911
REMARK 3 25 2.1615 - 2.1323 0.98 7184 369 0.1704 0.1985
REMARK 3 26 2.1323 - 2.1046 0.98 7204 380 0.1763 0.2179
REMARK 3 27 2.1046 - 2.0783 0.98 7175 387 0.1838 0.2220
REMARK 3 28 2.0783 - 2.0533 0.98 7223 333 0.1968 0.2194
REMARK 3 29 2.0533 - 2.0294 0.98 7188 357 0.1928 0.2218
REMARK 3 30 2.0294 - 2.0070 0.87 6349 337 0.1892 0.2291
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) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.060
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.03
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 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 7XRT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-MAY-22.
REMARK 100 THE DEPOSITION ID IS D_1300029462.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-NOV-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979183
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 : 229659
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 (%) : 98.9
REMARK 200 DATA REDUNDANCY : 12.10
REMARK 200 R MERGE (I) : 0.07600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.3000
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 (%) : 98.1
REMARK 200 DATA REDUNDANCY IN SHELL : 11.40
REMARK 200 R MERGE FOR SHELL (I) : 0.67500
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: 5VOL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.04 M SODIUM CACODYLATE TRIHYDRATE
REMARK 280 (PH 6.0), 60% (V/V) MPD, 0.04 M POTASSIUM CHLORIDE, 0.012 M
REMARK 280 SPERMINE TETRAHYDROCHLORIDE, 0.02 M TRIMETHYLAMINE HYDROCHLORIDE,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 56.69250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 96.02800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 80.08200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 96.02800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 56.69250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 80.08200
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: DECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 23210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 96160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -244.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J
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 -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 SER A 1
REMARK 465 HIS A 2
REMARK 465 HIS A 3
REMARK 465 HIS A 4
REMARK 465 HIS A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 SER A 8
REMARK 465 SER A 9
REMARK 465 GLY A 10
REMARK 465 LEU A 11
REMARK 465 VAL A 12
REMARK 465 PRO A 13
REMARK 465 ARG A 14
REMARK 465 GLY A 15
REMARK 465 SER A 16
REMARK 465 HIS A 17
REMARK 465 MET A 18
REMARK 465 LEU A 19
REMARK 465 GLU A 20
REMARK 465 MET B -2
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 SER B 1
REMARK 465 HIS B 2
REMARK 465 HIS B 3
REMARK 465 HIS B 4
REMARK 465 HIS B 5
REMARK 465 HIS B 6
REMARK 465 HIS B 7
REMARK 465 SER B 8
REMARK 465 SER B 9
REMARK 465 GLY B 10
REMARK 465 LEU B 11
REMARK 465 VAL B 12
REMARK 465 PRO B 13
REMARK 465 ARG B 14
REMARK 465 GLY B 15
REMARK 465 SER B 16
REMARK 465 HIS B 17
REMARK 465 MET B 18
REMARK 465 LEU B 19
REMARK 465 GLU B 20
REMARK 465 MET C -2
REMARK 465 GLY C -1
REMARK 465 SER C 0
REMARK 465 SER C 1
REMARK 465 HIS C 2
REMARK 465 HIS C 3
REMARK 465 HIS C 4
REMARK 465 HIS C 5
REMARK 465 HIS C 6
REMARK 465 HIS C 7
REMARK 465 SER C 8
REMARK 465 SER C 9
REMARK 465 GLY C 10
REMARK 465 LEU C 11
REMARK 465 VAL C 12
REMARK 465 PRO C 13
REMARK 465 ARG C 14
REMARK 465 GLY C 15
REMARK 465 SER C 16
REMARK 465 HIS C 17
REMARK 465 MET C 18
REMARK 465 LEU C 19
REMARK 465 GLU C 20
REMARK 465 MET D -2
REMARK 465 GLY D -1
REMARK 465 SER D 0
REMARK 465 SER D 1
REMARK 465 HIS D 2
REMARK 465 HIS D 3
REMARK 465 HIS D 4
REMARK 465 HIS D 5
REMARK 465 HIS D 6
REMARK 465 HIS D 7
REMARK 465 SER D 8
REMARK 465 SER D 9
REMARK 465 GLY D 10
REMARK 465 LEU D 11
REMARK 465 VAL D 12
REMARK 465 PRO D 13
REMARK 465 ARG D 14
REMARK 465 GLY D 15
REMARK 465 SER D 16
REMARK 465 HIS D 17
REMARK 465 MET D 18
REMARK 465 LEU D 19
REMARK 465 GLU D 20
REMARK 465 MET E -2
REMARK 465 GLY E -1
REMARK 465 SER E 0
REMARK 465 SER E 1
REMARK 465 HIS E 2
REMARK 465 HIS E 3
REMARK 465 HIS E 4
REMARK 465 HIS E 5
REMARK 465 HIS E 6
REMARK 465 HIS E 7
REMARK 465 SER E 8
REMARK 465 SER E 9
REMARK 465 GLY E 10
REMARK 465 LEU E 11
REMARK 465 VAL E 12
REMARK 465 PRO E 13
REMARK 465 ARG E 14
REMARK 465 GLY E 15
REMARK 465 SER E 16
REMARK 465 HIS E 17
REMARK 465 MET E 18
REMARK 465 LEU E 19
REMARK 465 GLU E 20
REMARK 465 MET F -2
REMARK 465 GLY F -1
REMARK 465 SER F 0
REMARK 465 SER F 1
REMARK 465 HIS F 2
REMARK 465 HIS F 3
REMARK 465 HIS F 4
REMARK 465 HIS F 5
REMARK 465 HIS F 6
REMARK 465 HIS F 7
REMARK 465 SER F 8
REMARK 465 SER F 9
REMARK 465 GLY F 10
REMARK 465 LEU F 11
REMARK 465 VAL F 12
REMARK 465 PRO F 13
REMARK 465 ARG F 14
REMARK 465 GLY F 15
REMARK 465 SER F 16
REMARK 465 HIS F 17
REMARK 465 MET F 18
REMARK 465 LEU F 19
REMARK 465 GLU F 20
REMARK 465 MET G -2
REMARK 465 GLY G -1
REMARK 465 SER G 0
REMARK 465 SER G 1
REMARK 465 HIS G 2
REMARK 465 HIS G 3
REMARK 465 HIS G 4
REMARK 465 HIS G 5
REMARK 465 HIS G 6
REMARK 465 HIS G 7
REMARK 465 SER G 8
REMARK 465 SER G 9
REMARK 465 GLY G 10
REMARK 465 LEU G 11
REMARK 465 VAL G 12
REMARK 465 PRO G 13
REMARK 465 ARG G 14
REMARK 465 GLY G 15
REMARK 465 SER G 16
REMARK 465 HIS G 17
REMARK 465 MET G 18
REMARK 465 LEU G 19
REMARK 465 GLU G 20
REMARK 465 MET H -2
REMARK 465 GLY H -1
REMARK 465 SER H 0
REMARK 465 SER H 1
REMARK 465 HIS H 2
REMARK 465 HIS H 3
REMARK 465 HIS H 4
REMARK 465 HIS H 5
REMARK 465 HIS H 6
REMARK 465 HIS H 7
REMARK 465 SER H 8
REMARK 465 SER H 9
REMARK 465 GLY H 10
REMARK 465 LEU H 11
REMARK 465 VAL H 12
REMARK 465 PRO H 13
REMARK 465 ARG H 14
REMARK 465 GLY H 15
REMARK 465 SER H 16
REMARK 465 HIS H 17
REMARK 465 MET H 18
REMARK 465 LEU H 19
REMARK 465 GLU H 20
REMARK 465 MET I -2
REMARK 465 GLY I -1
REMARK 465 SER I 0
REMARK 465 SER I 1
REMARK 465 HIS I 2
REMARK 465 HIS I 3
REMARK 465 HIS I 4
REMARK 465 HIS I 5
REMARK 465 HIS I 6
REMARK 465 HIS I 7
REMARK 465 SER I 8
REMARK 465 SER I 9
REMARK 465 GLY I 10
REMARK 465 LEU I 11
REMARK 465 VAL I 12
REMARK 465 PRO I 13
REMARK 465 ARG I 14
REMARK 465 GLY I 15
REMARK 465 SER I 16
REMARK 465 HIS I 17
REMARK 465 MET I 18
REMARK 465 LEU I 19
REMARK 465 GLU I 20
REMARK 465 MET J -2
REMARK 465 GLY J -1
REMARK 465 SER J 0
REMARK 465 SER J 1
REMARK 465 HIS J 2
REMARK 465 HIS J 3
REMARK 465 HIS J 4
REMARK 465 HIS J 5
REMARK 465 HIS J 6
REMARK 465 HIS J 7
REMARK 465 SER J 8
REMARK 465 SER J 9
REMARK 465 GLY J 10
REMARK 465 LEU J 11
REMARK 465 VAL J 12
REMARK 465 PRO J 13
REMARK 465 ARG J 14
REMARK 465 GLY J 15
REMARK 465 SER J 16
REMARK 465 HIS J 17
REMARK 465 MET J 18
REMARK 465 LEU J 19
REMARK 465 GLU J 20
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLN A 21 CG CD OE1 NE2
REMARK 470 LYS A 193 CG CD CE NZ
REMARK 470 GLU A 197 CG CD OE1 OE2
REMARK 470 GLU A 218 CG CD OE1 OE2
REMARK 470 GLN B 21 CG CD OE1 NE2
REMARK 470 LYS B 193 CG CD CE NZ
REMARK 470 GLU B 197 CG CD OE1 OE2
REMARK 470 GLU B 218 CG CD OE1 OE2
REMARK 470 GLN C 21 CG CD OE1 NE2
REMARK 470 GLN C 22 CG CD OE1 NE2
REMARK 470 GLU C 218 CG CD OE1 OE2
REMARK 470 GLN D 21 CG CD OE1 NE2
REMARK 470 GLN D 22 CG CD OE1 NE2
REMARK 470 SER D 192 OG
REMARK 470 LYS D 193 CG CD CE NZ
REMARK 470 GLU D 197 CG CD OE1 OE2
REMARK 470 LYS D 198 CG CD CE NZ
REMARK 470 LYS D 199 CG CD CE NZ
REMARK 470 GLU D 218 CG CD OE1 OE2
REMARK 470 GLN E 21 CG CD OE1 NE2
REMARK 470 GLN E 22 CG CD OE1 NE2
REMARK 470 LYS E 193 CG CD CE NZ
REMARK 470 GLU E 218 CG CD OE1 OE2
REMARK 470 GLN F 21 CG CD OE1 NE2
REMARK 470 GLN F 22 CG CD OE1 NE2
REMARK 470 LYS F 193 CG CD CE NZ
REMARK 470 GLU F 197 CG CD OE1 OE2
REMARK 470 GLN G 21 CG CD OE1 NE2
REMARK 470 GLN G 22 CG CD OE1 NE2
REMARK 470 LEU G 191 CG CD1 CD2
REMARK 470 LYS G 193 CG CD CE NZ
REMARK 470 VAL G 194 CG1 CG2
REMARK 470 GLU G 197 CG CD OE1 OE2
REMARK 470 GLU G 218 CG CD OE1 OE2
REMARK 470 GLN H 21 CG CD OE1 NE2
REMARK 470 GLN H 22 CG CD OE1 NE2
REMARK 470 LEU H 191 CG CD1 CD2
REMARK 470 LYS H 193 CG CD CE NZ
REMARK 470 VAL H 194 CG1 CG2
REMARK 470 GLU H 197 CG CD OE1 OE2
REMARK 470 GLU H 218 CG CD OE1 OE2
REMARK 470 GLN I 21 CG CD OE1 NE2
REMARK 470 GLN I 22 CG CD OE1 NE2
REMARK 470 LYS I 193 CG CD CE NZ
REMARK 470 GLU I 197 CG CD OE1 OE2
REMARK 470 GLU I 218 CG CD OE1 OE2
REMARK 470 GLN J 21 CG CD OE1 NE2
REMARK 470 GLN J 22 CG CD OE1 NE2
REMARK 470 LYS J 193 CG CD CE NZ
REMARK 470 GLU J 197 CG CD OE1 OE2
REMARK 470 GLU J 218 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 69 -155.55 -128.26
REMARK 500 VAL A 105 -61.99 75.90
REMARK 500 TYR A 117 86.64 -156.16
REMARK 500 SER A 150 -118.58 55.66
REMARK 500 SER A 264 -168.91 -123.66
REMARK 500 GLN A 287 167.70 65.38
REMARK 500 ASN B 69 -154.07 -129.21
REMARK 500 VAL B 105 -62.04 75.07
REMARK 500 TYR B 117 85.33 -156.55
REMARK 500 SER B 150 -118.61 55.86
REMARK 500 SER B 264 -168.50 -123.29
REMARK 500 GLN B 287 167.72 65.04
REMARK 500 ASN C 69 -155.67 -128.53
REMARK 500 VAL C 105 -60.45 75.42
REMARK 500 TYR C 117 84.42 -154.48
REMARK 500 SER C 150 -117.75 54.83
REMARK 500 GLN C 287 167.52 65.09
REMARK 500 ASN D 69 -155.33 -129.14
REMARK 500 VAL D 105 -61.20 73.52
REMARK 500 TYR D 117 86.43 -158.38
REMARK 500 SER D 150 -117.13 54.30
REMARK 500 GLN D 287 166.20 65.15
REMARK 500 ASN E 69 -154.26 -128.61
REMARK 500 VAL E 105 -62.37 75.50
REMARK 500 TYR E 117 85.80 -156.15
REMARK 500 SER E 150 -117.28 54.86
REMARK 500 SER E 264 -169.93 -123.41
REMARK 500 GLN E 287 167.38 64.39
REMARK 500 ASN F 69 -155.94 -128.91
REMARK 500 VAL F 105 -61.61 76.62
REMARK 500 TYR F 117 84.98 -154.72
REMARK 500 SER F 150 -118.15 54.73
REMARK 500 SER F 264 -169.29 -123.24
REMARK 500 GLN F 287 167.05 65.56
REMARK 500 ASN G 69 -157.11 -127.91
REMARK 500 VAL G 105 -63.27 76.48
REMARK 500 TYR G 117 84.50 -154.70
REMARK 500 SER G 150 -119.72 55.63
REMARK 500 SER G 264 -167.46 -123.36
REMARK 500 GLN G 287 167.71 65.40
REMARK 500 ASN H 69 -156.05 -127.90
REMARK 500 VAL H 105 -61.99 76.16
REMARK 500 TYR H 117 86.65 -155.76
REMARK 500 SER H 150 -118.91 55.79
REMARK 500 SER H 264 -168.95 -124.19
REMARK 500 GLN H 287 168.21 66.76
REMARK 500 ASN I 69 -154.41 -128.49
REMARK 500 VAL I 105 -61.45 75.81
REMARK 500 TYR I 117 85.48 -157.03
REMARK 500 SER I 150 -118.85 56.29
REMARK 500
REMARK 500 THIS ENTRY HAS 58 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 611 DISTANCE = 6.11 ANGSTROMS
REMARK 525 HOH A 612 DISTANCE = 6.70 ANGSTROMS
REMARK 525 HOH B 612 DISTANCE = 6.44 ANGSTROMS
REMARK 525 HOH C 638 DISTANCE = 6.19 ANGSTROMS
REMARK 525 HOH D 534 DISTANCE = 6.63 ANGSTROMS
REMARK 525 HOH D 535 DISTANCE = 6.72 ANGSTROMS
REMARK 525 HOH E 612 DISTANCE = 6.51 ANGSTROMS
REMARK 525 HOH F 603 DISTANCE = 6.67 ANGSTROMS
REMARK 525 HOH H 547 DISTANCE = 6.65 ANGSTROMS
REMARK 525 HOH I 599 DISTANCE = 5.88 ANGSTROMS
REMARK 525 HOH I 600 DISTANCE = 6.48 ANGSTROMS
REMARK 525 HOH J 574 DISTANCE = 6.75 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 234 OD1
REMARK 620 2 ASP A 234 OD2 48.4
REMARK 620 3 ASP A 235 OD1 79.5 89.3
REMARK 620 4 ASP A 235 OD2 73.4 115.3 50.0
REMARK 620 5 ASP A 262 OD1 80.6 105.6 136.3 87.0
REMARK 620 6 GLU B 257 OE2 114.2 77.8 142.5 164.5 81.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 257 OE2
REMARK 620 2 ASP B 234 OD1 114.2
REMARK 620 3 ASP B 234 OD2 76.9 50.0
REMARK 620 4 ASP B 235 OD1 145.3 77.7 89.5
REMARK 620 5 ASP B 235 OD2 163.1 72.0 116.1 49.8
REMARK 620 6 ASP B 262 OD1 80.1 80.5 105.9 134.7 85.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 234 OD1
REMARK 620 2 ASP C 234 OD2 48.2
REMARK 620 3 ASP C 235 OD1 76.8 86.1
REMARK 620 4 ASP C 235 OD2 74.2 115.6 50.3
REMARK 620 5 ASP C 262 OD1 82.2 106.9 137.0 88.1
REMARK 620 6 GLU E 257 OE2 115.2 78.4 141.2 164.9 81.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 257 OE1
REMARK 620 2 ASP E 234 OD1 114.7
REMARK 620 3 ASP E 234 OD2 78.7 49.2
REMARK 620 4 ASP E 235 OD1 142.7 78.1 86.6
REMARK 620 5 ASP E 235 OD2 165.6 73.4 114.4 48.4
REMARK 620 6 ASP E 262 OD1 82.1 80.8 108.2 135.2 87.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 234 OD1
REMARK 620 2 ASP D 234 OD2 49.6
REMARK 620 3 ASP D 235 OD1 77.8 83.1
REMARK 620 4 ASP D 235 OD2 72.8 113.5 51.2
REMARK 620 5 ASP D 262 OD1 79.3 109.0 135.9 86.1
REMARK 620 6 GLU G 257 OE2 115.2 79.6 139.9 165.8 84.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA G 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 257 OE2
REMARK 620 2 ASP G 234 OD1 114.6
REMARK 620 3 ASP G 234 OD2 78.9 48.4
REMARK 620 4 ASP G 235 OD1 142.7 78.8 87.6
REMARK 620 5 ASP G 235 OD2 161.8 76.6 118.0 50.7
REMARK 620 6 ASP G 262 OD1 80.4 81.0 106.3 136.8 87.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 234 OD1
REMARK 620 2 ASP F 234 OD2 48.1
REMARK 620 3 ASP F 235 OD1 79.4 87.3
REMARK 620 4 ASP F 235 OD2 73.9 114.9 50.6
REMARK 620 5 ASP F 262 OD1 78.3 105.6 134.7 85.4
REMARK 620 6 GLU H 257 OE2 110.7 77.9 146.0 162.3 79.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA H 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU F 257 OE2
REMARK 620 2 ASP H 234 OD1 115.1
REMARK 620 3 ASP H 234 OD2 79.2 49.6
REMARK 620 4 ASP H 235 OD1 143.0 79.9 88.2
REMARK 620 5 ASP H 235 OD2 162.3 75.0 117.0 50.2
REMARK 620 6 ASP H 262 OD1 81.6 80.8 108.4 135.4 86.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA I 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP I 234 OD1
REMARK 620 2 ASP I 234 OD2 50.1
REMARK 620 3 ASP I 235 OD1 78.3 86.6
REMARK 620 4 ASP I 235 OD2 73.1 116.3 52.1
REMARK 620 5 ASP I 262 OD1 79.6 106.7 136.7 86.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA J 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU I 257 OE2
REMARK 620 2 ASP J 234 OD1 112.8
REMARK 620 3 ASP J 234 OD2 78.7 49.1
REMARK 620 4 ASP J 235 OD1 144.4 80.1 87.7
REMARK 620 5 ASP J 235 OD2 162.3 75.9 116.8 49.9
REMARK 620 6 ASP J 262 OD1 80.8 80.8 109.3 134.8 85.7
REMARK 620 N 1 2 3 4 5
DBREF 7XRT A 21 288 UNP Q8A0E4 Q8A0E4_BACTN 21 288
DBREF 7XRT B 21 288 UNP Q8A0E4 Q8A0E4_BACTN 21 288
DBREF 7XRT C 21 288 UNP Q8A0E4 Q8A0E4_BACTN 21 288
DBREF 7XRT D 21 288 UNP Q8A0E4 Q8A0E4_BACTN 21 288
DBREF 7XRT E 21 288 UNP Q8A0E4 Q8A0E4_BACTN 21 288
DBREF 7XRT F 21 288 UNP Q8A0E4 Q8A0E4_BACTN 21 288
DBREF 7XRT G 21 288 UNP Q8A0E4 Q8A0E4_BACTN 21 288
DBREF 7XRT H 21 288 UNP Q8A0E4 Q8A0E4_BACTN 21 288
DBREF 7XRT I 21 288 UNP Q8A0E4 Q8A0E4_BACTN 21 288
DBREF 7XRT J 21 288 UNP Q8A0E4 Q8A0E4_BACTN 21 288
SEQADV 7XRT MET A -2 UNP Q8A0E4 INITIATING METHIONINE
SEQADV 7XRT GLY A -1 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER A 0 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER A 1 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS A 2 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS A 3 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS A 4 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS A 5 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS A 6 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS A 7 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER A 8 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER A 9 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT GLY A 10 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT LEU A 11 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT VAL A 12 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT PRO A 13 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT ARG A 14 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT GLY A 15 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER A 16 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS A 17 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT MET A 18 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT LEU A 19 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT GLU A 20 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT MET B -2 UNP Q8A0E4 INITIATING METHIONINE
SEQADV 7XRT GLY B -1 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER B 0 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER B 1 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS B 2 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS B 3 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS B 4 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS B 5 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS B 6 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS B 7 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER B 8 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER B 9 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT GLY B 10 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT LEU B 11 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT VAL B 12 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT PRO B 13 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT ARG B 14 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT GLY B 15 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER B 16 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS B 17 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT MET B 18 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT LEU B 19 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT GLU B 20 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT MET C -2 UNP Q8A0E4 INITIATING METHIONINE
SEQADV 7XRT GLY C -1 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER C 0 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER C 1 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS C 2 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS C 3 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS C 4 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS C 5 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS C 6 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS C 7 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER C 8 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER C 9 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT GLY C 10 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT LEU C 11 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT VAL C 12 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT PRO C 13 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT ARG C 14 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT GLY C 15 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER C 16 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS C 17 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT MET C 18 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT LEU C 19 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT GLU C 20 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT MET D -2 UNP Q8A0E4 INITIATING METHIONINE
SEQADV 7XRT GLY D -1 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER D 0 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER D 1 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS D 2 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS D 3 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS D 4 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS D 5 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS D 6 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS D 7 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER D 8 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER D 9 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT GLY D 10 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT LEU D 11 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT VAL D 12 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT PRO D 13 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT ARG D 14 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT GLY D 15 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER D 16 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS D 17 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT MET D 18 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT LEU D 19 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT GLU D 20 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT MET E -2 UNP Q8A0E4 INITIATING METHIONINE
SEQADV 7XRT GLY E -1 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER E 0 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER E 1 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS E 2 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS E 3 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS E 4 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS E 5 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS E 6 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS E 7 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER E 8 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER E 9 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT GLY E 10 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT LEU E 11 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT VAL E 12 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT PRO E 13 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT ARG E 14 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT GLY E 15 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER E 16 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS E 17 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT MET E 18 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT LEU E 19 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT GLU E 20 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT MET F -2 UNP Q8A0E4 INITIATING METHIONINE
SEQADV 7XRT GLY F -1 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER F 0 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER F 1 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS F 2 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS F 3 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS F 4 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS F 5 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS F 6 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS F 7 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER F 8 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER F 9 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT GLY F 10 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT LEU F 11 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT VAL F 12 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT PRO F 13 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT ARG F 14 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT GLY F 15 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER F 16 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS F 17 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT MET F 18 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT LEU F 19 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT GLU F 20 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT MET G -2 UNP Q8A0E4 INITIATING METHIONINE
SEQADV 7XRT GLY G -1 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER G 0 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER G 1 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS G 2 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS G 3 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS G 4 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS G 5 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS G 6 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS G 7 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER G 8 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER G 9 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT GLY G 10 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT LEU G 11 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT VAL G 12 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT PRO G 13 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT ARG G 14 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT GLY G 15 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER G 16 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS G 17 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT MET G 18 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT LEU G 19 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT GLU G 20 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT MET H -2 UNP Q8A0E4 INITIATING METHIONINE
SEQADV 7XRT GLY H -1 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER H 0 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER H 1 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS H 2 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS H 3 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS H 4 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS H 5 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS H 6 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS H 7 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER H 8 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER H 9 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT GLY H 10 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT LEU H 11 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT VAL H 12 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT PRO H 13 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT ARG H 14 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT GLY H 15 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER H 16 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS H 17 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT MET H 18 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT LEU H 19 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT GLU H 20 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT MET I -2 UNP Q8A0E4 INITIATING METHIONINE
SEQADV 7XRT GLY I -1 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER I 0 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER I 1 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS I 2 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS I 3 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS I 4 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS I 5 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS I 6 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS I 7 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER I 8 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER I 9 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT GLY I 10 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT LEU I 11 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT VAL I 12 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT PRO I 13 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT ARG I 14 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT GLY I 15 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER I 16 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS I 17 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT MET I 18 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT LEU I 19 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT GLU I 20 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT MET J -2 UNP Q8A0E4 INITIATING METHIONINE
SEQADV 7XRT GLY J -1 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER J 0 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER J 1 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS J 2 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS J 3 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS J 4 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS J 5 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS J 6 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS J 7 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER J 8 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER J 9 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT GLY J 10 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT LEU J 11 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT VAL J 12 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT PRO J 13 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT ARG J 14 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT GLY J 15 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT SER J 16 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT HIS J 17 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT MET J 18 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT LEU J 19 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRT GLU J 20 UNP Q8A0E4 EXPRESSION TAG
SEQRES 1 A 291 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 291 LEU VAL PRO ARG GLY SER HIS MET LEU GLU GLN GLN GLY
SEQRES 3 A 291 LYS VAL TYR GLU THR ARG THR VAL LYS SER LYS ILE LEU
SEQRES 4 A 291 GLY MET GLU ARG SER TYR SER ILE TYR LEU PRO ALA GLY
SEQRES 5 A 291 TYR ASP GLU GLY ASP GLY SER TYR PRO VAL LEU TYR LEU
SEQRES 6 A 291 LEU HIS GLY LEU GLY ASP ASN HIS THR GLY TRP VAL GLN
SEQRES 7 A 291 PHE GLY GLN VAL GLN TYR ILE ALA ASP LYS ALA ILE ALA
SEQRES 8 A 291 GLU GLY LYS SER ALA PRO MET ILE ILE VAL MET PRO ASP
SEQRES 9 A 291 ALA ASP THR VAL HIS LYS GLY TYR PHE ASN LEU LEU ASP
SEQRES 10 A 291 GLY THR TYR ASN TYR GLU ASP PHE PHE PHE GLN GLU LEU
SEQRES 11 A 291 ILE PRO HIS ILE GLU LYS THR TYR ARG VAL ARG ALA GLU
SEQRES 12 A 291 SER ARG TYR ARG ALA ILE SER GLY LEU SER MET GLY GLY
SEQRES 13 A 291 GLY GLY ALA LEU PHE TYR ALA LEU HIS TYR PRO GLU MET
SEQRES 14 A 291 PHE VAL ALA VAL ALA PRO LEU SER ALA VAL GLY GLY ALA
SEQRES 15 A 291 TRP THR PHE ASP GLN MET LYS ASN GLN SER ASP LEU SER
SEQRES 16 A 291 LYS VAL SER GLU GLU LYS LYS ALA GLU VAL LEU GLY GLN
SEQRES 17 A 291 MET ASP ILE GLN THR ILE LEU GLU LYS SER PRO LYS GLU
SEQRES 18 A 291 LYS LEU ASP ARG ILE LYS TRP ILE ARG TRP TYR ILE SER
SEQRES 19 A 291 CYS GLY ASP ASP ASP PHE LEU SER VAL THR ASN CYS LEU
SEQRES 20 A 291 LEU HIS ASN THR LEU LEU GLN HIS GLN VAL GLY HIS GLU
SEQRES 21 A 291 PHE ARG MET LYS ASP GLY SER HIS SER TRP THR TYR TRP
SEQRES 22 A 291 ARG MET GLU LEU PRO GLU VAL MET ARG PHE VAL SER ARG
SEQRES 23 A 291 ILE PHE THR GLN TYR
SEQRES 1 B 291 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 291 LEU VAL PRO ARG GLY SER HIS MET LEU GLU GLN GLN GLY
SEQRES 3 B 291 LYS VAL TYR GLU THR ARG THR VAL LYS SER LYS ILE LEU
SEQRES 4 B 291 GLY MET GLU ARG SER TYR SER ILE TYR LEU PRO ALA GLY
SEQRES 5 B 291 TYR ASP GLU GLY ASP GLY SER TYR PRO VAL LEU TYR LEU
SEQRES 6 B 291 LEU HIS GLY LEU GLY ASP ASN HIS THR GLY TRP VAL GLN
SEQRES 7 B 291 PHE GLY GLN VAL GLN TYR ILE ALA ASP LYS ALA ILE ALA
SEQRES 8 B 291 GLU GLY LYS SER ALA PRO MET ILE ILE VAL MET PRO ASP
SEQRES 9 B 291 ALA ASP THR VAL HIS LYS GLY TYR PHE ASN LEU LEU ASP
SEQRES 10 B 291 GLY THR TYR ASN TYR GLU ASP PHE PHE PHE GLN GLU LEU
SEQRES 11 B 291 ILE PRO HIS ILE GLU LYS THR TYR ARG VAL ARG ALA GLU
SEQRES 12 B 291 SER ARG TYR ARG ALA ILE SER GLY LEU SER MET GLY GLY
SEQRES 13 B 291 GLY GLY ALA LEU PHE TYR ALA LEU HIS TYR PRO GLU MET
SEQRES 14 B 291 PHE VAL ALA VAL ALA PRO LEU SER ALA VAL GLY GLY ALA
SEQRES 15 B 291 TRP THR PHE ASP GLN MET LYS ASN GLN SER ASP LEU SER
SEQRES 16 B 291 LYS VAL SER GLU GLU LYS LYS ALA GLU VAL LEU GLY GLN
SEQRES 17 B 291 MET ASP ILE GLN THR ILE LEU GLU LYS SER PRO LYS GLU
SEQRES 18 B 291 LYS LEU ASP ARG ILE LYS TRP ILE ARG TRP TYR ILE SER
SEQRES 19 B 291 CYS GLY ASP ASP ASP PHE LEU SER VAL THR ASN CYS LEU
SEQRES 20 B 291 LEU HIS ASN THR LEU LEU GLN HIS GLN VAL GLY HIS GLU
SEQRES 21 B 291 PHE ARG MET LYS ASP GLY SER HIS SER TRP THR TYR TRP
SEQRES 22 B 291 ARG MET GLU LEU PRO GLU VAL MET ARG PHE VAL SER ARG
SEQRES 23 B 291 ILE PHE THR GLN TYR
SEQRES 1 C 291 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 291 LEU VAL PRO ARG GLY SER HIS MET LEU GLU GLN GLN GLY
SEQRES 3 C 291 LYS VAL TYR GLU THR ARG THR VAL LYS SER LYS ILE LEU
SEQRES 4 C 291 GLY MET GLU ARG SER TYR SER ILE TYR LEU PRO ALA GLY
SEQRES 5 C 291 TYR ASP GLU GLY ASP GLY SER TYR PRO VAL LEU TYR LEU
SEQRES 6 C 291 LEU HIS GLY LEU GLY ASP ASN HIS THR GLY TRP VAL GLN
SEQRES 7 C 291 PHE GLY GLN VAL GLN TYR ILE ALA ASP LYS ALA ILE ALA
SEQRES 8 C 291 GLU GLY LYS SER ALA PRO MET ILE ILE VAL MET PRO ASP
SEQRES 9 C 291 ALA ASP THR VAL HIS LYS GLY TYR PHE ASN LEU LEU ASP
SEQRES 10 C 291 GLY THR TYR ASN TYR GLU ASP PHE PHE PHE GLN GLU LEU
SEQRES 11 C 291 ILE PRO HIS ILE GLU LYS THR TYR ARG VAL ARG ALA GLU
SEQRES 12 C 291 SER ARG TYR ARG ALA ILE SER GLY LEU SER MET GLY GLY
SEQRES 13 C 291 GLY GLY ALA LEU PHE TYR ALA LEU HIS TYR PRO GLU MET
SEQRES 14 C 291 PHE VAL ALA VAL ALA PRO LEU SER ALA VAL GLY GLY ALA
SEQRES 15 C 291 TRP THR PHE ASP GLN MET LYS ASN GLN SER ASP LEU SER
SEQRES 16 C 291 LYS VAL SER GLU GLU LYS LYS ALA GLU VAL LEU GLY GLN
SEQRES 17 C 291 MET ASP ILE GLN THR ILE LEU GLU LYS SER PRO LYS GLU
SEQRES 18 C 291 LYS LEU ASP ARG ILE LYS TRP ILE ARG TRP TYR ILE SER
SEQRES 19 C 291 CYS GLY ASP ASP ASP PHE LEU SER VAL THR ASN CYS LEU
SEQRES 20 C 291 LEU HIS ASN THR LEU LEU GLN HIS GLN VAL GLY HIS GLU
SEQRES 21 C 291 PHE ARG MET LYS ASP GLY SER HIS SER TRP THR TYR TRP
SEQRES 22 C 291 ARG MET GLU LEU PRO GLU VAL MET ARG PHE VAL SER ARG
SEQRES 23 C 291 ILE PHE THR GLN TYR
SEQRES 1 D 291 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 291 LEU VAL PRO ARG GLY SER HIS MET LEU GLU GLN GLN GLY
SEQRES 3 D 291 LYS VAL TYR GLU THR ARG THR VAL LYS SER LYS ILE LEU
SEQRES 4 D 291 GLY MET GLU ARG SER TYR SER ILE TYR LEU PRO ALA GLY
SEQRES 5 D 291 TYR ASP GLU GLY ASP GLY SER TYR PRO VAL LEU TYR LEU
SEQRES 6 D 291 LEU HIS GLY LEU GLY ASP ASN HIS THR GLY TRP VAL GLN
SEQRES 7 D 291 PHE GLY GLN VAL GLN TYR ILE ALA ASP LYS ALA ILE ALA
SEQRES 8 D 291 GLU GLY LYS SER ALA PRO MET ILE ILE VAL MET PRO ASP
SEQRES 9 D 291 ALA ASP THR VAL HIS LYS GLY TYR PHE ASN LEU LEU ASP
SEQRES 10 D 291 GLY THR TYR ASN TYR GLU ASP PHE PHE PHE GLN GLU LEU
SEQRES 11 D 291 ILE PRO HIS ILE GLU LYS THR TYR ARG VAL ARG ALA GLU
SEQRES 12 D 291 SER ARG TYR ARG ALA ILE SER GLY LEU SER MET GLY GLY
SEQRES 13 D 291 GLY GLY ALA LEU PHE TYR ALA LEU HIS TYR PRO GLU MET
SEQRES 14 D 291 PHE VAL ALA VAL ALA PRO LEU SER ALA VAL GLY GLY ALA
SEQRES 15 D 291 TRP THR PHE ASP GLN MET LYS ASN GLN SER ASP LEU SER
SEQRES 16 D 291 LYS VAL SER GLU GLU LYS LYS ALA GLU VAL LEU GLY GLN
SEQRES 17 D 291 MET ASP ILE GLN THR ILE LEU GLU LYS SER PRO LYS GLU
SEQRES 18 D 291 LYS LEU ASP ARG ILE LYS TRP ILE ARG TRP TYR ILE SER
SEQRES 19 D 291 CYS GLY ASP ASP ASP PHE LEU SER VAL THR ASN CYS LEU
SEQRES 20 D 291 LEU HIS ASN THR LEU LEU GLN HIS GLN VAL GLY HIS GLU
SEQRES 21 D 291 PHE ARG MET LYS ASP GLY SER HIS SER TRP THR TYR TRP
SEQRES 22 D 291 ARG MET GLU LEU PRO GLU VAL MET ARG PHE VAL SER ARG
SEQRES 23 D 291 ILE PHE THR GLN TYR
SEQRES 1 E 291 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 E 291 LEU VAL PRO ARG GLY SER HIS MET LEU GLU GLN GLN GLY
SEQRES 3 E 291 LYS VAL TYR GLU THR ARG THR VAL LYS SER LYS ILE LEU
SEQRES 4 E 291 GLY MET GLU ARG SER TYR SER ILE TYR LEU PRO ALA GLY
SEQRES 5 E 291 TYR ASP GLU GLY ASP GLY SER TYR PRO VAL LEU TYR LEU
SEQRES 6 E 291 LEU HIS GLY LEU GLY ASP ASN HIS THR GLY TRP VAL GLN
SEQRES 7 E 291 PHE GLY GLN VAL GLN TYR ILE ALA ASP LYS ALA ILE ALA
SEQRES 8 E 291 GLU GLY LYS SER ALA PRO MET ILE ILE VAL MET PRO ASP
SEQRES 9 E 291 ALA ASP THR VAL HIS LYS GLY TYR PHE ASN LEU LEU ASP
SEQRES 10 E 291 GLY THR TYR ASN TYR GLU ASP PHE PHE PHE GLN GLU LEU
SEQRES 11 E 291 ILE PRO HIS ILE GLU LYS THR TYR ARG VAL ARG ALA GLU
SEQRES 12 E 291 SER ARG TYR ARG ALA ILE SER GLY LEU SER MET GLY GLY
SEQRES 13 E 291 GLY GLY ALA LEU PHE TYR ALA LEU HIS TYR PRO GLU MET
SEQRES 14 E 291 PHE VAL ALA VAL ALA PRO LEU SER ALA VAL GLY GLY ALA
SEQRES 15 E 291 TRP THR PHE ASP GLN MET LYS ASN GLN SER ASP LEU SER
SEQRES 16 E 291 LYS VAL SER GLU GLU LYS LYS ALA GLU VAL LEU GLY GLN
SEQRES 17 E 291 MET ASP ILE GLN THR ILE LEU GLU LYS SER PRO LYS GLU
SEQRES 18 E 291 LYS LEU ASP ARG ILE LYS TRP ILE ARG TRP TYR ILE SER
SEQRES 19 E 291 CYS GLY ASP ASP ASP PHE LEU SER VAL THR ASN CYS LEU
SEQRES 20 E 291 LEU HIS ASN THR LEU LEU GLN HIS GLN VAL GLY HIS GLU
SEQRES 21 E 291 PHE ARG MET LYS ASP GLY SER HIS SER TRP THR TYR TRP
SEQRES 22 E 291 ARG MET GLU LEU PRO GLU VAL MET ARG PHE VAL SER ARG
SEQRES 23 E 291 ILE PHE THR GLN TYR
SEQRES 1 F 291 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 F 291 LEU VAL PRO ARG GLY SER HIS MET LEU GLU GLN GLN GLY
SEQRES 3 F 291 LYS VAL TYR GLU THR ARG THR VAL LYS SER LYS ILE LEU
SEQRES 4 F 291 GLY MET GLU ARG SER TYR SER ILE TYR LEU PRO ALA GLY
SEQRES 5 F 291 TYR ASP GLU GLY ASP GLY SER TYR PRO VAL LEU TYR LEU
SEQRES 6 F 291 LEU HIS GLY LEU GLY ASP ASN HIS THR GLY TRP VAL GLN
SEQRES 7 F 291 PHE GLY GLN VAL GLN TYR ILE ALA ASP LYS ALA ILE ALA
SEQRES 8 F 291 GLU GLY LYS SER ALA PRO MET ILE ILE VAL MET PRO ASP
SEQRES 9 F 291 ALA ASP THR VAL HIS LYS GLY TYR PHE ASN LEU LEU ASP
SEQRES 10 F 291 GLY THR TYR ASN TYR GLU ASP PHE PHE PHE GLN GLU LEU
SEQRES 11 F 291 ILE PRO HIS ILE GLU LYS THR TYR ARG VAL ARG ALA GLU
SEQRES 12 F 291 SER ARG TYR ARG ALA ILE SER GLY LEU SER MET GLY GLY
SEQRES 13 F 291 GLY GLY ALA LEU PHE TYR ALA LEU HIS TYR PRO GLU MET
SEQRES 14 F 291 PHE VAL ALA VAL ALA PRO LEU SER ALA VAL GLY GLY ALA
SEQRES 15 F 291 TRP THR PHE ASP GLN MET LYS ASN GLN SER ASP LEU SER
SEQRES 16 F 291 LYS VAL SER GLU GLU LYS LYS ALA GLU VAL LEU GLY GLN
SEQRES 17 F 291 MET ASP ILE GLN THR ILE LEU GLU LYS SER PRO LYS GLU
SEQRES 18 F 291 LYS LEU ASP ARG ILE LYS TRP ILE ARG TRP TYR ILE SER
SEQRES 19 F 291 CYS GLY ASP ASP ASP PHE LEU SER VAL THR ASN CYS LEU
SEQRES 20 F 291 LEU HIS ASN THR LEU LEU GLN HIS GLN VAL GLY HIS GLU
SEQRES 21 F 291 PHE ARG MET LYS ASP GLY SER HIS SER TRP THR TYR TRP
SEQRES 22 F 291 ARG MET GLU LEU PRO GLU VAL MET ARG PHE VAL SER ARG
SEQRES 23 F 291 ILE PHE THR GLN TYR
SEQRES 1 G 291 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 G 291 LEU VAL PRO ARG GLY SER HIS MET LEU GLU GLN GLN GLY
SEQRES 3 G 291 LYS VAL TYR GLU THR ARG THR VAL LYS SER LYS ILE LEU
SEQRES 4 G 291 GLY MET GLU ARG SER TYR SER ILE TYR LEU PRO ALA GLY
SEQRES 5 G 291 TYR ASP GLU GLY ASP GLY SER TYR PRO VAL LEU TYR LEU
SEQRES 6 G 291 LEU HIS GLY LEU GLY ASP ASN HIS THR GLY TRP VAL GLN
SEQRES 7 G 291 PHE GLY GLN VAL GLN TYR ILE ALA ASP LYS ALA ILE ALA
SEQRES 8 G 291 GLU GLY LYS SER ALA PRO MET ILE ILE VAL MET PRO ASP
SEQRES 9 G 291 ALA ASP THR VAL HIS LYS GLY TYR PHE ASN LEU LEU ASP
SEQRES 10 G 291 GLY THR TYR ASN TYR GLU ASP PHE PHE PHE GLN GLU LEU
SEQRES 11 G 291 ILE PRO HIS ILE GLU LYS THR TYR ARG VAL ARG ALA GLU
SEQRES 12 G 291 SER ARG TYR ARG ALA ILE SER GLY LEU SER MET GLY GLY
SEQRES 13 G 291 GLY GLY ALA LEU PHE TYR ALA LEU HIS TYR PRO GLU MET
SEQRES 14 G 291 PHE VAL ALA VAL ALA PRO LEU SER ALA VAL GLY GLY ALA
SEQRES 15 G 291 TRP THR PHE ASP GLN MET LYS ASN GLN SER ASP LEU SER
SEQRES 16 G 291 LYS VAL SER GLU GLU LYS LYS ALA GLU VAL LEU GLY GLN
SEQRES 17 G 291 MET ASP ILE GLN THR ILE LEU GLU LYS SER PRO LYS GLU
SEQRES 18 G 291 LYS LEU ASP ARG ILE LYS TRP ILE ARG TRP TYR ILE SER
SEQRES 19 G 291 CYS GLY ASP ASP ASP PHE LEU SER VAL THR ASN CYS LEU
SEQRES 20 G 291 LEU HIS ASN THR LEU LEU GLN HIS GLN VAL GLY HIS GLU
SEQRES 21 G 291 PHE ARG MET LYS ASP GLY SER HIS SER TRP THR TYR TRP
SEQRES 22 G 291 ARG MET GLU LEU PRO GLU VAL MET ARG PHE VAL SER ARG
SEQRES 23 G 291 ILE PHE THR GLN TYR
SEQRES 1 H 291 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 H 291 LEU VAL PRO ARG GLY SER HIS MET LEU GLU GLN GLN GLY
SEQRES 3 H 291 LYS VAL TYR GLU THR ARG THR VAL LYS SER LYS ILE LEU
SEQRES 4 H 291 GLY MET GLU ARG SER TYR SER ILE TYR LEU PRO ALA GLY
SEQRES 5 H 291 TYR ASP GLU GLY ASP GLY SER TYR PRO VAL LEU TYR LEU
SEQRES 6 H 291 LEU HIS GLY LEU GLY ASP ASN HIS THR GLY TRP VAL GLN
SEQRES 7 H 291 PHE GLY GLN VAL GLN TYR ILE ALA ASP LYS ALA ILE ALA
SEQRES 8 H 291 GLU GLY LYS SER ALA PRO MET ILE ILE VAL MET PRO ASP
SEQRES 9 H 291 ALA ASP THR VAL HIS LYS GLY TYR PHE ASN LEU LEU ASP
SEQRES 10 H 291 GLY THR TYR ASN TYR GLU ASP PHE PHE PHE GLN GLU LEU
SEQRES 11 H 291 ILE PRO HIS ILE GLU LYS THR TYR ARG VAL ARG ALA GLU
SEQRES 12 H 291 SER ARG TYR ARG ALA ILE SER GLY LEU SER MET GLY GLY
SEQRES 13 H 291 GLY GLY ALA LEU PHE TYR ALA LEU HIS TYR PRO GLU MET
SEQRES 14 H 291 PHE VAL ALA VAL ALA PRO LEU SER ALA VAL GLY GLY ALA
SEQRES 15 H 291 TRP THR PHE ASP GLN MET LYS ASN GLN SER ASP LEU SER
SEQRES 16 H 291 LYS VAL SER GLU GLU LYS LYS ALA GLU VAL LEU GLY GLN
SEQRES 17 H 291 MET ASP ILE GLN THR ILE LEU GLU LYS SER PRO LYS GLU
SEQRES 18 H 291 LYS LEU ASP ARG ILE LYS TRP ILE ARG TRP TYR ILE SER
SEQRES 19 H 291 CYS GLY ASP ASP ASP PHE LEU SER VAL THR ASN CYS LEU
SEQRES 20 H 291 LEU HIS ASN THR LEU LEU GLN HIS GLN VAL GLY HIS GLU
SEQRES 21 H 291 PHE ARG MET LYS ASP GLY SER HIS SER TRP THR TYR TRP
SEQRES 22 H 291 ARG MET GLU LEU PRO GLU VAL MET ARG PHE VAL SER ARG
SEQRES 23 H 291 ILE PHE THR GLN TYR
SEQRES 1 I 291 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 I 291 LEU VAL PRO ARG GLY SER HIS MET LEU GLU GLN GLN GLY
SEQRES 3 I 291 LYS VAL TYR GLU THR ARG THR VAL LYS SER LYS ILE LEU
SEQRES 4 I 291 GLY MET GLU ARG SER TYR SER ILE TYR LEU PRO ALA GLY
SEQRES 5 I 291 TYR ASP GLU GLY ASP GLY SER TYR PRO VAL LEU TYR LEU
SEQRES 6 I 291 LEU HIS GLY LEU GLY ASP ASN HIS THR GLY TRP VAL GLN
SEQRES 7 I 291 PHE GLY GLN VAL GLN TYR ILE ALA ASP LYS ALA ILE ALA
SEQRES 8 I 291 GLU GLY LYS SER ALA PRO MET ILE ILE VAL MET PRO ASP
SEQRES 9 I 291 ALA ASP THR VAL HIS LYS GLY TYR PHE ASN LEU LEU ASP
SEQRES 10 I 291 GLY THR TYR ASN TYR GLU ASP PHE PHE PHE GLN GLU LEU
SEQRES 11 I 291 ILE PRO HIS ILE GLU LYS THR TYR ARG VAL ARG ALA GLU
SEQRES 12 I 291 SER ARG TYR ARG ALA ILE SER GLY LEU SER MET GLY GLY
SEQRES 13 I 291 GLY GLY ALA LEU PHE TYR ALA LEU HIS TYR PRO GLU MET
SEQRES 14 I 291 PHE VAL ALA VAL ALA PRO LEU SER ALA VAL GLY GLY ALA
SEQRES 15 I 291 TRP THR PHE ASP GLN MET LYS ASN GLN SER ASP LEU SER
SEQRES 16 I 291 LYS VAL SER GLU GLU LYS LYS ALA GLU VAL LEU GLY GLN
SEQRES 17 I 291 MET ASP ILE GLN THR ILE LEU GLU LYS SER PRO LYS GLU
SEQRES 18 I 291 LYS LEU ASP ARG ILE LYS TRP ILE ARG TRP TYR ILE SER
SEQRES 19 I 291 CYS GLY ASP ASP ASP PHE LEU SER VAL THR ASN CYS LEU
SEQRES 20 I 291 LEU HIS ASN THR LEU LEU GLN HIS GLN VAL GLY HIS GLU
SEQRES 21 I 291 PHE ARG MET LYS ASP GLY SER HIS SER TRP THR TYR TRP
SEQRES 22 I 291 ARG MET GLU LEU PRO GLU VAL MET ARG PHE VAL SER ARG
SEQRES 23 I 291 ILE PHE THR GLN TYR
SEQRES 1 J 291 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 J 291 LEU VAL PRO ARG GLY SER HIS MET LEU GLU GLN GLN GLY
SEQRES 3 J 291 LYS VAL TYR GLU THR ARG THR VAL LYS SER LYS ILE LEU
SEQRES 4 J 291 GLY MET GLU ARG SER TYR SER ILE TYR LEU PRO ALA GLY
SEQRES 5 J 291 TYR ASP GLU GLY ASP GLY SER TYR PRO VAL LEU TYR LEU
SEQRES 6 J 291 LEU HIS GLY LEU GLY ASP ASN HIS THR GLY TRP VAL GLN
SEQRES 7 J 291 PHE GLY GLN VAL GLN TYR ILE ALA ASP LYS ALA ILE ALA
SEQRES 8 J 291 GLU GLY LYS SER ALA PRO MET ILE ILE VAL MET PRO ASP
SEQRES 9 J 291 ALA ASP THR VAL HIS LYS GLY TYR PHE ASN LEU LEU ASP
SEQRES 10 J 291 GLY THR TYR ASN TYR GLU ASP PHE PHE PHE GLN GLU LEU
SEQRES 11 J 291 ILE PRO HIS ILE GLU LYS THR TYR ARG VAL ARG ALA GLU
SEQRES 12 J 291 SER ARG TYR ARG ALA ILE SER GLY LEU SER MET GLY GLY
SEQRES 13 J 291 GLY GLY ALA LEU PHE TYR ALA LEU HIS TYR PRO GLU MET
SEQRES 14 J 291 PHE VAL ALA VAL ALA PRO LEU SER ALA VAL GLY GLY ALA
SEQRES 15 J 291 TRP THR PHE ASP GLN MET LYS ASN GLN SER ASP LEU SER
SEQRES 16 J 291 LYS VAL SER GLU GLU LYS LYS ALA GLU VAL LEU GLY GLN
SEQRES 17 J 291 MET ASP ILE GLN THR ILE LEU GLU LYS SER PRO LYS GLU
SEQRES 18 J 291 LYS LEU ASP ARG ILE LYS TRP ILE ARG TRP TYR ILE SER
SEQRES 19 J 291 CYS GLY ASP ASP ASP PHE LEU SER VAL THR ASN CYS LEU
SEQRES 20 J 291 LEU HIS ASN THR LEU LEU GLN HIS GLN VAL GLY HIS GLU
SEQRES 21 J 291 PHE ARG MET LYS ASP GLY SER HIS SER TRP THR TYR TRP
SEQRES 22 J 291 ARG MET GLU LEU PRO GLU VAL MET ARG PHE VAL SER ARG
SEQRES 23 J 291 ILE PHE THR GLN TYR
HET CA A 301 1
HET MPD A 302 8
HET CA B 301 1
HET CA C 301 1
HET CA D 301 1
HET MPD D 302 8
HET CA E 301 1
HET MPD E 302 8
HET CA F 301 1
HET MPD F 302 8
HET CA G 301 1
HET MPD G 302 8
HET MPD G 303 8
HET CA H 301 1
HET MPD H 302 8
HET CA I 301 1
HET MPD I 302 8
HET CA J 301 1
HET MPD J 302 8
HETNAM CA CALCIUM ION
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
FORMUL 11 CA 10(CA 2+)
FORMUL 12 MPD 9(C6 H14 O2)
FORMUL 30 HOH *1881(H2 O)
HELIX 1 AA1 THR A 71 PHE A 76 1 6
HELIX 2 AA2 GLN A 78 GLU A 89 1 12
HELIX 3 AA3 ASN A 118 GLU A 126 1 9
HELIX 4 AA4 GLU A 126 TYR A 135 1 10
HELIX 5 AA5 GLU A 140 ARG A 142 5 3
HELIX 6 AA6 SER A 150 TYR A 163 1 14
HELIX 7 AA7 PRO A 164 PHE A 167 5 4
HELIX 8 AA8 GLY A 177 GLN A 188 1 12
HELIX 9 AA9 ASP A 190 VAL A 194 5 5
HELIX 10 AB1 SER A 195 MET A 206 1 12
HELIX 11 AB2 ASP A 207 SER A 215 1 9
HELIX 12 AB3 PRO A 216 ILE A 226 1 11
HELIX 13 AB4 LEU A 238 HIS A 252 1 15
HELIX 14 AB5 SER A 266 GLN A 287 1 22
HELIX 15 AB6 THR B 71 PHE B 76 1 6
HELIX 16 AB7 GLN B 78 GLU B 89 1 12
HELIX 17 AB8 ASN B 118 GLU B 126 1 9
HELIX 18 AB9 GLU B 126 TYR B 135 1 10
HELIX 19 AC1 GLU B 140 ARG B 142 5 3
HELIX 20 AC2 SER B 150 TYR B 163 1 14
HELIX 21 AC3 PRO B 164 PHE B 167 5 4
HELIX 22 AC4 GLY B 177 ASN B 187 1 11
HELIX 23 AC5 GLN B 188 SER B 189 5 2
HELIX 24 AC6 ASP B 190 VAL B 194 5 5
HELIX 25 AC7 SER B 195 MET B 206 1 12
HELIX 26 AC8 ASP B 207 SER B 215 1 9
HELIX 27 AC9 PRO B 216 ILE B 226 1 11
HELIX 28 AD1 LEU B 238 HIS B 252 1 15
HELIX 29 AD2 SER B 266 GLN B 287 1 22
HELIX 30 AD3 THR C 71 PHE C 76 1 6
HELIX 31 AD4 GLN C 78 GLU C 89 1 12
HELIX 32 AD5 ASN C 118 GLU C 126 1 9
HELIX 33 AD6 GLU C 126 TYR C 135 1 10
HELIX 34 AD7 GLU C 140 ARG C 142 5 3
HELIX 35 AD8 SER C 150 TYR C 163 1 14
HELIX 36 AD9 PRO C 164 PHE C 167 5 4
HELIX 37 AE1 GLY C 177 SER C 189 1 13
HELIX 38 AE2 ASP C 190 VAL C 194 5 5
HELIX 39 AE3 SER C 195 MET C 206 1 12
HELIX 40 AE4 ASP C 207 SER C 215 1 9
HELIX 41 AE5 PRO C 216 ILE C 226 1 11
HELIX 42 AE6 LEU C 238 HIS C 252 1 15
HELIX 43 AE7 SER C 266 GLN C 287 1 22
HELIX 44 AE8 THR D 71 PHE D 76 1 6
HELIX 45 AE9 GLN D 78 GLU D 89 1 12
HELIX 46 AF1 ASN D 118 GLU D 126 1 9
HELIX 47 AF2 GLU D 126 TYR D 135 1 10
HELIX 48 AF3 GLU D 140 ARG D 142 5 3
HELIX 49 AF4 SER D 150 TYR D 163 1 14
HELIX 50 AF5 PRO D 164 PHE D 167 5 4
HELIX 51 AF6 GLY D 177 SER D 189 1 13
HELIX 52 AF7 ASP D 190 VAL D 194 5 5
HELIX 53 AF8 SER D 195 MET D 206 1 12
HELIX 54 AF9 ASP D 207 SER D 215 1 9
HELIX 55 AG1 PRO D 216 ILE D 226 1 11
HELIX 56 AG2 LEU D 238 HIS D 252 1 15
HELIX 57 AG3 SER D 266 GLN D 287 1 22
HELIX 58 AG4 THR E 71 PHE E 76 1 6
HELIX 59 AG5 GLN E 78 GLU E 89 1 12
HELIX 60 AG6 ASN E 118 GLU E 126 1 9
HELIX 61 AG7 GLU E 126 TYR E 135 1 10
HELIX 62 AG8 GLU E 140 ARG E 142 5 3
HELIX 63 AG9 SER E 150 TYR E 163 1 14
HELIX 64 AH1 PRO E 164 PHE E 167 5 4
HELIX 65 AH2 GLY E 177 GLN E 188 1 12
HELIX 66 AH3 ASP E 190 VAL E 194 5 5
HELIX 67 AH4 SER E 195 MET E 206 1 12
HELIX 68 AH5 ASP E 207 SER E 215 1 9
HELIX 69 AH6 PRO E 216 ILE E 226 1 11
HELIX 70 AH7 LEU E 238 HIS E 252 1 15
HELIX 71 AH8 SER E 266 GLN E 287 1 22
HELIX 72 AH9 THR F 71 PHE F 76 1 6
HELIX 73 AI1 GLN F 78 GLU F 89 1 12
HELIX 74 AI2 ASN F 118 GLU F 126 1 9
HELIX 75 AI3 GLU F 126 TYR F 135 1 10
HELIX 76 AI4 GLU F 140 ARG F 142 5 3
HELIX 77 AI5 SER F 150 TYR F 163 1 14
HELIX 78 AI6 PRO F 164 PHE F 167 5 4
HELIX 79 AI7 GLY F 177 ASN F 187 1 11
HELIX 80 AI8 GLN F 188 SER F 189 5 2
HELIX 81 AI9 ASP F 190 VAL F 194 5 5
HELIX 82 AJ1 SER F 195 MET F 206 1 12
HELIX 83 AJ2 ASP F 207 SER F 215 1 9
HELIX 84 AJ3 PRO F 216 ILE F 226 1 11
HELIX 85 AJ4 LEU F 238 HIS F 252 1 15
HELIX 86 AJ5 SER F 266 GLN F 287 1 22
HELIX 87 AJ6 THR G 71 PHE G 76 1 6
HELIX 88 AJ7 GLN G 78 GLU G 89 1 12
HELIX 89 AJ8 ASN G 118 GLU G 126 1 9
HELIX 90 AJ9 GLU G 126 TYR G 135 1 10
HELIX 91 AK1 GLU G 140 ARG G 142 5 3
HELIX 92 AK2 SER G 150 TYR G 163 1 14
HELIX 93 AK3 PRO G 164 PHE G 167 5 4
HELIX 94 AK4 GLY G 177 SER G 189 1 13
HELIX 95 AK5 ASP G 190 VAL G 194 5 5
HELIX 96 AK6 SER G 195 MET G 206 1 12
HELIX 97 AK7 ASP G 207 SER G 215 1 9
HELIX 98 AK8 PRO G 216 ILE G 226 1 11
HELIX 99 AK9 LEU G 238 HIS G 252 1 15
HELIX 100 AL1 SER G 266 GLN G 287 1 22
HELIX 101 AL2 THR H 71 PHE H 76 1 6
HELIX 102 AL3 GLN H 78 GLU H 89 1 12
HELIX 103 AL4 ASN H 118 GLU H 126 1 9
HELIX 104 AL5 GLU H 126 TYR H 135 1 10
HELIX 105 AL6 GLU H 140 ARG H 142 5 3
HELIX 106 AL7 SER H 150 TYR H 163 1 14
HELIX 107 AL8 PRO H 164 PHE H 167 5 4
HELIX 108 AL9 GLY H 177 GLN H 188 1 12
HELIX 109 AM1 ASP H 190 VAL H 194 5 5
HELIX 110 AM2 SER H 195 MET H 206 1 12
HELIX 111 AM3 ASP H 207 SER H 215 1 9
HELIX 112 AM4 PRO H 216 ILE H 226 1 11
HELIX 113 AM5 LEU H 238 HIS H 252 1 15
HELIX 114 AM6 SER H 266 GLN H 287 1 22
HELIX 115 AM7 THR I 71 PHE I 76 1 6
HELIX 116 AM8 GLN I 78 GLU I 89 1 12
HELIX 117 AM9 ASN I 118 GLU I 126 1 9
HELIX 118 AN1 GLU I 126 TYR I 135 1 10
HELIX 119 AN2 GLU I 140 ARG I 142 5 3
HELIX 120 AN3 SER I 150 TYR I 163 1 14
HELIX 121 AN4 PRO I 164 PHE I 167 5 4
HELIX 122 AN5 GLY I 177 GLN I 188 1 12
HELIX 123 AN6 ASP I 190 VAL I 194 5 5
HELIX 124 AN7 SER I 195 MET I 206 1 12
HELIX 125 AN8 ASP I 207 SER I 215 1 9
HELIX 126 AN9 PRO I 216 ILE I 226 1 11
HELIX 127 AO1 LEU I 238 HIS I 252 1 15
HELIX 128 AO2 SER I 266 GLN I 287 1 22
HELIX 129 AO3 THR J 71 PHE J 76 1 6
HELIX 130 AO4 GLN J 78 GLU J 89 1 12
HELIX 131 AO5 ASN J 118 GLU J 126 1 9
HELIX 132 AO6 GLU J 126 TYR J 135 1 10
HELIX 133 AO7 GLU J 140 ARG J 142 5 3
HELIX 134 AO8 SER J 150 TYR J 163 1 14
HELIX 135 AO9 PRO J 164 PHE J 167 5 4
HELIX 136 AP1 GLY J 177 GLN J 188 1 12
HELIX 137 AP2 ASP J 190 VAL J 194 5 5
HELIX 138 AP3 SER J 195 MET J 206 1 12
HELIX 139 AP4 ASP J 207 SER J 215 1 9
HELIX 140 AP5 PRO J 216 ILE J 226 1 11
HELIX 141 AP6 LEU J 238 HIS J 252 1 15
HELIX 142 AP7 SER J 266 GLN J 287 1 22
SHEET 1 AA1 3 LYS A 24 TYR A 26 0
SHEET 2 AA1 3 MET A 38 LEU A 46 -1 O LEU A 46 N LYS A 24
SHEET 3 AA1 3 THR A 30 SER A 33 -1 N VAL A 31 O ARG A 40
SHEET 1 AA2 8 LYS A 24 TYR A 26 0
SHEET 2 AA2 8 MET A 38 LEU A 46 -1 O LEU A 46 N LYS A 24
SHEET 3 AA2 8 ILE A 96 PRO A 100 -1 O MET A 99 N SER A 43
SHEET 4 AA2 8 VAL A 59 LEU A 63 1 N LEU A 62 O VAL A 98
SHEET 5 AA2 8 ARG A 144 LEU A 149 1 O ALA A 145 N TYR A 61
SHEET 6 AA2 8 ALA A 169 LEU A 173 1 O LEU A 173 N GLY A 148
SHEET 7 AA2 8 ARG A 227 GLY A 233 1 O TYR A 229 N VAL A 170
SHEET 8 AA2 8 GLU A 257 LYS A 261 1 O GLU A 257 N TRP A 228
SHEET 1 AA3 3 LYS B 24 TYR B 26 0
SHEET 2 AA3 3 MET B 38 LEU B 46 -1 O LEU B 46 N LYS B 24
SHEET 3 AA3 3 THR B 30 SER B 33 -1 N VAL B 31 O ARG B 40
SHEET 1 AA4 8 LYS B 24 TYR B 26 0
SHEET 2 AA4 8 MET B 38 LEU B 46 -1 O LEU B 46 N LYS B 24
SHEET 3 AA4 8 ILE B 96 PRO B 100 -1 O MET B 99 N SER B 43
SHEET 4 AA4 8 VAL B 59 LEU B 63 1 N LEU B 62 O VAL B 98
SHEET 5 AA4 8 ARG B 144 LEU B 149 1 O SER B 147 N TYR B 61
SHEET 6 AA4 8 ALA B 169 LEU B 173 1 O LEU B 173 N GLY B 148
SHEET 7 AA4 8 ARG B 227 GLY B 233 1 O TYR B 229 N VAL B 170
SHEET 8 AA4 8 GLU B 257 LYS B 261 1 O ARG B 259 N ILE B 230
SHEET 1 AA5 3 LYS C 24 TYR C 26 0
SHEET 2 AA5 3 MET C 38 LEU C 46 -1 O LEU C 46 N LYS C 24
SHEET 3 AA5 3 THR C 30 SER C 33 -1 N VAL C 31 O ARG C 40
SHEET 1 AA6 8 LYS C 24 TYR C 26 0
SHEET 2 AA6 8 MET C 38 LEU C 46 -1 O LEU C 46 N LYS C 24
SHEET 3 AA6 8 ILE C 96 PRO C 100 -1 O MET C 99 N SER C 43
SHEET 4 AA6 8 VAL C 59 LEU C 63 1 N LEU C 62 O VAL C 98
SHEET 5 AA6 8 ARG C 144 LEU C 149 1 O SER C 147 N TYR C 61
SHEET 6 AA6 8 ALA C 169 LEU C 173 1 O LEU C 173 N GLY C 148
SHEET 7 AA6 8 ARG C 227 GLY C 233 1 O TYR C 229 N VAL C 170
SHEET 8 AA6 8 GLU C 257 LYS C 261 1 O GLU C 257 N ILE C 230
SHEET 1 AA7 3 LYS D 24 TYR D 26 0
SHEET 2 AA7 3 MET D 38 LEU D 46 -1 O LEU D 46 N LYS D 24
SHEET 3 AA7 3 THR D 30 SER D 33 -1 N VAL D 31 O ARG D 40
SHEET 1 AA8 8 LYS D 24 TYR D 26 0
SHEET 2 AA8 8 MET D 38 LEU D 46 -1 O LEU D 46 N LYS D 24
SHEET 3 AA8 8 ILE D 96 PRO D 100 -1 O MET D 99 N SER D 43
SHEET 4 AA8 8 VAL D 59 LEU D 63 1 N LEU D 60 O ILE D 96
SHEET 5 AA8 8 ARG D 144 LEU D 149 1 O SER D 147 N TYR D 61
SHEET 6 AA8 8 ALA D 169 LEU D 173 1 O LEU D 173 N GLY D 148
SHEET 7 AA8 8 ARG D 227 GLY D 233 1 O TYR D 229 N VAL D 170
SHEET 8 AA8 8 GLU D 257 LYS D 261 1 O GLU D 257 N ILE D 230
SHEET 1 AA9 3 LYS E 24 TYR E 26 0
SHEET 2 AA9 3 MET E 38 LEU E 46 -1 O LEU E 46 N LYS E 24
SHEET 3 AA9 3 THR E 30 SER E 33 -1 N SER E 33 O MET E 38
SHEET 1 AB1 8 LYS E 24 TYR E 26 0
SHEET 2 AB1 8 MET E 38 LEU E 46 -1 O LEU E 46 N LYS E 24
SHEET 3 AB1 8 ILE E 96 PRO E 100 -1 O MET E 99 N SER E 43
SHEET 4 AB1 8 VAL E 59 LEU E 63 1 N LEU E 62 O VAL E 98
SHEET 5 AB1 8 ARG E 144 LEU E 149 1 O SER E 147 N TYR E 61
SHEET 6 AB1 8 ALA E 169 LEU E 173 1 O LEU E 173 N GLY E 148
SHEET 7 AB1 8 ARG E 227 GLY E 233 1 O TYR E 229 N VAL E 170
SHEET 8 AB1 8 GLU E 257 LYS E 261 1 O GLU E 257 N TRP E 228
SHEET 1 AB2 3 LYS F 24 TYR F 26 0
SHEET 2 AB2 3 MET F 38 LEU F 46 -1 O LEU F 46 N LYS F 24
SHEET 3 AB2 3 THR F 30 SER F 33 -1 N VAL F 31 O ARG F 40
SHEET 1 AB3 8 LYS F 24 TYR F 26 0
SHEET 2 AB3 8 MET F 38 LEU F 46 -1 O LEU F 46 N LYS F 24
SHEET 3 AB3 8 ILE F 96 PRO F 100 -1 O MET F 99 N SER F 43
SHEET 4 AB3 8 VAL F 59 LEU F 63 1 N LEU F 62 O VAL F 98
SHEET 5 AB3 8 ARG F 144 LEU F 149 1 O SER F 147 N TYR F 61
SHEET 6 AB3 8 ALA F 169 LEU F 173 1 O LEU F 173 N GLY F 148
SHEET 7 AB3 8 ARG F 227 GLY F 233 1 O TYR F 229 N VAL F 170
SHEET 8 AB3 8 GLU F 257 LYS F 261 1 O ARG F 259 N ILE F 230
SHEET 1 AB4 3 LYS G 24 TYR G 26 0
SHEET 2 AB4 3 MET G 38 LEU G 46 -1 O LEU G 46 N LYS G 24
SHEET 3 AB4 3 THR G 30 SER G 33 -1 N SER G 33 O MET G 38
SHEET 1 AB5 8 LYS G 24 TYR G 26 0
SHEET 2 AB5 8 MET G 38 LEU G 46 -1 O LEU G 46 N LYS G 24
SHEET 3 AB5 8 ILE G 96 PRO G 100 -1 O MET G 99 N SER G 43
SHEET 4 AB5 8 VAL G 59 LEU G 63 1 N LEU G 62 O VAL G 98
SHEET 5 AB5 8 ARG G 144 LEU G 149 1 O SER G 147 N TYR G 61
SHEET 6 AB5 8 ALA G 169 LEU G 173 1 O LEU G 173 N GLY G 148
SHEET 7 AB5 8 ARG G 227 GLY G 233 1 O TYR G 229 N VAL G 170
SHEET 8 AB5 8 GLU G 257 LYS G 261 1 O GLU G 257 N ILE G 230
SHEET 1 AB6 3 LYS H 24 TYR H 26 0
SHEET 2 AB6 3 MET H 38 LEU H 46 -1 O LEU H 46 N LYS H 24
SHEET 3 AB6 3 THR H 30 SER H 33 -1 N VAL H 31 O ARG H 40
SHEET 1 AB7 8 LYS H 24 TYR H 26 0
SHEET 2 AB7 8 MET H 38 LEU H 46 -1 O LEU H 46 N LYS H 24
SHEET 3 AB7 8 ILE H 96 PRO H 100 -1 O MET H 99 N SER H 43
SHEET 4 AB7 8 VAL H 59 LEU H 63 1 N LEU H 62 O VAL H 98
SHEET 5 AB7 8 ARG H 144 LEU H 149 1 O ALA H 145 N TYR H 61
SHEET 6 AB7 8 ALA H 169 LEU H 173 1 O LEU H 173 N GLY H 148
SHEET 7 AB7 8 ARG H 227 GLY H 233 1 O TYR H 229 N VAL H 170
SHEET 8 AB7 8 GLU H 257 LYS H 261 1 O GLU H 257 N TRP H 228
SHEET 1 AB8 3 LYS I 24 TYR I 26 0
SHEET 2 AB8 3 MET I 38 LEU I 46 -1 O LEU I 46 N LYS I 24
SHEET 3 AB8 3 THR I 30 SER I 33 -1 N VAL I 31 O ARG I 40
SHEET 1 AB9 8 LYS I 24 TYR I 26 0
SHEET 2 AB9 8 MET I 38 LEU I 46 -1 O LEU I 46 N LYS I 24
SHEET 3 AB9 8 ILE I 96 PRO I 100 -1 O MET I 99 N SER I 43
SHEET 4 AB9 8 VAL I 59 LEU I 63 1 N LEU I 62 O VAL I 98
SHEET 5 AB9 8 ARG I 144 LEU I 149 1 O ALA I 145 N TYR I 61
SHEET 6 AB9 8 ALA I 169 LEU I 173 1 O LEU I 173 N GLY I 148
SHEET 7 AB9 8 ARG I 227 GLY I 233 1 O TYR I 229 N VAL I 170
SHEET 8 AB9 8 GLU I 257 LYS I 261 1 O GLU I 257 N TRP I 228
SHEET 1 AC1 3 LYS J 24 TYR J 26 0
SHEET 2 AC1 3 MET J 38 LEU J 46 -1 O LEU J 46 N LYS J 24
SHEET 3 AC1 3 THR J 30 SER J 33 -1 N VAL J 31 O ARG J 40
SHEET 1 AC2 8 LYS J 24 TYR J 26 0
SHEET 2 AC2 8 MET J 38 LEU J 46 -1 O LEU J 46 N LYS J 24
SHEET 3 AC2 8 ILE J 96 PRO J 100 -1 O MET J 99 N SER J 43
SHEET 4 AC2 8 VAL J 59 LEU J 63 1 N LEU J 62 O VAL J 98
SHEET 5 AC2 8 ARG J 144 LEU J 149 1 O SER J 147 N TYR J 61
SHEET 6 AC2 8 ALA J 169 LEU J 173 1 O LEU J 173 N GLY J 148
SHEET 7 AC2 8 ARG J 227 GLY J 233 1 O TYR J 229 N VAL J 170
SHEET 8 AC2 8 GLU J 257 LYS J 261 1 O GLU J 257 N TRP J 228
LINK OD1 ASP A 234 CA CA A 301 1555 1555 2.71
LINK OD2 ASP A 234 CA CA A 301 1555 1555 2.68
LINK OD1 ASP A 235 CA CA A 301 1555 1555 2.66
LINK OD2 ASP A 235 CA CA A 301 1555 1555 2.56
LINK OE2 GLU A 257 CA CA B 301 1555 1555 2.62
LINK OD1 ASP A 262 CA CA A 301 1555 1555 2.25
LINK CA CA A 301 OE2 GLU B 257 1555 1555 2.57
LINK OD1 ASP B 234 CA CA B 301 1555 1555 2.64
LINK OD2 ASP B 234 CA CA B 301 1555 1555 2.54
LINK OD1 ASP B 235 CA CA B 301 1555 1555 2.56
LINK OD2 ASP B 235 CA CA B 301 1555 1555 2.64
LINK OD1 ASP B 262 CA CA B 301 1555 1555 2.32
LINK OD1 ASP C 234 CA CA C 301 1555 1555 2.65
LINK OD2 ASP C 234 CA CA C 301 1555 1555 2.69
LINK OD1 ASP C 235 CA CA C 301 1555 1555 2.59
LINK OD2 ASP C 235 CA CA C 301 1555 1555 2.55
LINK OE1 GLU C 257 CA CA E 301 1555 1555 2.54
LINK OD1 ASP C 262 CA CA C 301 1555 1555 2.38
LINK CA CA C 301 OE2 GLU E 257 1555 1555 2.46
LINK OD1 ASP D 234 CA CA D 301 1555 1555 2.67
LINK OD2 ASP D 234 CA CA D 301 1555 1555 2.54
LINK OD1 ASP D 235 CA CA D 301 1555 1555 2.67
LINK OD2 ASP D 235 CA CA D 301 1555 1555 2.35
LINK OE2 GLU D 257 CA CA G 301 1555 1555 2.58
LINK OD1 ASP D 262 CA CA D 301 1555 1555 2.42
LINK CA CA D 301 OE2 GLU G 257 1555 1555 2.44
LINK OD1 ASP E 234 CA CA E 301 1555 1555 2.63
LINK OD2 ASP E 234 CA CA E 301 1555 1555 2.65
LINK OD1 ASP E 235 CA CA E 301 1555 1555 2.77
LINK OD2 ASP E 235 CA CA E 301 1555 1555 2.58
LINK OD1 ASP E 262 CA CA E 301 1555 1555 2.36
LINK OD1 ASP F 234 CA CA F 301 1555 1555 2.68
LINK OD2 ASP F 234 CA CA F 301 1555 1555 2.66
LINK OD1 ASP F 235 CA CA F 301 1555 1555 2.59
LINK OD2 ASP F 235 CA CA F 301 1555 1555 2.53
LINK OE2 GLU F 257 CA CA H 301 1555 1555 2.55
LINK OD1 ASP F 262 CA CA F 301 1555 1555 2.47
LINK CA CA F 301 OE2 GLU H 257 1555 1555 2.49
LINK OD1 ASP G 234 CA CA G 301 1555 1555 2.65
LINK OD2 ASP G 234 CA CA G 301 1555 1555 2.69
LINK OD1 ASP G 235 CA CA G 301 1555 1555 2.65
LINK OD2 ASP G 235 CA CA G 301 1555 1555 2.44
LINK OD1 ASP G 262 CA CA G 301 1555 1555 2.44
LINK OD1 ASP H 234 CA CA H 301 1555 1555 2.67
LINK OD2 ASP H 234 CA CA H 301 1555 1555 2.57
LINK OD1 ASP H 235 CA CA H 301 1555 1555 2.67
LINK OD2 ASP H 235 CA CA H 301 1555 1555 2.49
LINK OD1 ASP H 262 CA CA H 301 1555 1555 2.32
LINK OD1 ASP I 234 CA CA I 301 1555 1555 2.62
LINK OD2 ASP I 234 CA CA I 301 1555 1555 2.53
LINK OD1 ASP I 235 CA CA I 301 1555 1555 2.48
LINK OD2 ASP I 235 CA CA I 301 1555 1555 2.54
LINK OE2 GLU I 257 CA CA J 301 1555 1555 2.51
LINK OD1 ASP I 262 CA CA I 301 1555 1555 2.44
LINK OD1 ASP J 234 CA CA J 301 1555 1555 2.61
LINK OD2 ASP J 234 CA CA J 301 1555 1555 2.67
LINK OD1 ASP J 235 CA CA J 301 1555 1555 2.64
LINK OD2 ASP J 235 CA CA J 301 1555 1555 2.55
LINK OD1 ASP J 262 CA CA J 301 1555 1555 2.36
CRYST1 113.385 160.164 192.056 90.00 90.00 90.00 P 21 21 21 40
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 0.008820 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006244 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005207 0.00000
TER 2154 TYR A 288
TER 4312 TYR B 288
TER 6470 TYR C 288
TER 8611 TYR D 288
TER 10765 TYR E 288
TER 12919 TYR F 288
TER 15064 TYR G 288
TER 17209 TYR H 288
TER 19359 TYR I 288
TER 21509 TYR J 288
MASTER 723 0 19 142 110 0 0 623458 10 151 230
END |