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HEADER HYDROLASE 11-MAY-22 7XRV
TITLE BACTEROIDES THETAIOTAOMICRON FERULIC ACID ESTERASE - S150A (BT_4077-
TITLE 2 S150A) COMPLEX WITH TRANS-METHYLFERULATE
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;
COMPND 5 MUTATION: 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, COMPLEX, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.M.DU,Y.L.WANG,F.J.XIN
REVDAT 1 22-NOV-23 7XRV 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. 2.71 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) : 2.71
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 109.86
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 101107
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.970
REMARK 3 FREE R VALUE TEST SET COUNT : 1987
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1109.8590 - 6.5385 0.98 7343 145 0.1387 0.1640
REMARK 3 2 6.5385 - 5.1898 1.00 7221 145 0.1499 0.1919
REMARK 3 3 5.1898 - 4.5338 1.00 7177 144 0.1169 0.1603
REMARK 3 4 4.5338 - 4.1192 1.00 7133 144 0.1286 0.1541
REMARK 3 5 4.1192 - 3.8240 0.97 6904 140 0.1980 0.2628
REMARK 3 6 3.8240 - 3.5985 0.98 6962 142 0.2223 0.2728
REMARK 3 7 3.5985 - 3.4183 0.99 6995 142 0.2275 0.2915
REMARK 3 8 3.4183 - 3.2695 1.00 7103 134 0.2070 0.2940
REMARK 3 9 3.2695 - 3.1436 1.00 7069 147 0.1919 0.2286
REMARK 3 10 3.1436 - 3.0351 1.00 7035 135 0.2116 0.2892
REMARK 3 11 3.0351 - 2.9402 1.00 7071 144 0.2340 0.2988
REMARK 3 12 2.9402 - 2.8561 1.00 7037 145 0.2281 0.3049
REMARK 3 13 2.8561 - 2.7810 1.00 7051 138 0.2238 0.2939
REMARK 3 14 2.7810 - 2.7131 1.00 7019 142 0.2343 0.2980
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) : 0.350
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.020
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.73
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 7XRV 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_1300029475.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-JUL-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL02U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97918
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 S 9M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.4
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 101667
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.710
REMARK 200 RESOLUTION RANGE LOW (A) : 109.860
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 9.500
REMARK 200 R MERGE (I) : 0.22700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.71
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.20
REMARK 200 R MERGE FOR SHELL (I) : 1.06800
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: PHASES
REMARK 200 STARTING MODEL: 7XRT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.16 M SUCCINIC ACID (PH 7.0), 16%
REMARK 280 (W/V) PEG3350, 0.2 M SODIUM IODIDE, 0.012 M SPERMINE
REMARK 280 TETRAHYDROCHLORIDE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293.15K
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 73.42700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 82.77400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 76.77400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 82.77400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 73.42700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 76.77400
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: 20630 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 98540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -159.0 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 LYS A 193 CG CD CE NZ
REMARK 470 GLU A 197 CG CD OE1 OE2
REMARK 470 LYS B 193 CG CD CE NZ
REMARK 470 GLU B 197 CG CD OE1 OE2
REMARK 470 GLN C 21 CG CD OE1 NE2
REMARK 470 GLN C 22 CG CD OE1 NE2
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 GLU D 197 CG CD OE1 OE2
REMARK 470 LYS D 198 CG CD CE NZ
REMARK 470 GLN E 22 CG CD OE1 NE2
REMARK 470 LYS E 193 CG CD CE NZ
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 LYS G 193 CG CD CE NZ
REMARK 470 GLU G 197 CG CD OE1 OE2
REMARK 470 GLN H 21 CG CD OE1 NE2
REMARK 470 GLN H 22 CG CD OE1 NE2
REMARK 470 LYS H 193 CG CD CE NZ
REMARK 470 GLU H 197 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 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 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 THR B 30 CA CB OG1 CG2
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 -151.07 -132.09
REMARK 500 VAL A 105 -58.05 72.62
REMARK 500 TYR A 117 88.08 -161.94
REMARK 500 ALA A 150 -114.22 56.95
REMARK 500 GLN A 287 168.38 68.78
REMARK 500 ASN B 69 -148.95 -132.82
REMARK 500 VAL B 105 -62.27 72.53
REMARK 500 TYR B 117 87.28 -160.62
REMARK 500 ALA B 150 -115.60 57.82
REMARK 500 SER B 264 -167.91 -129.98
REMARK 500 GLN B 287 162.89 68.67
REMARK 500 ASN C 69 -149.27 -134.36
REMARK 500 VAL C 105 -60.10 73.06
REMARK 500 TYR C 117 85.19 -157.01
REMARK 500 ALA C 150 -111.52 56.01
REMARK 500 SER C 264 -168.71 -127.85
REMARK 500 GLN C 287 166.37 70.11
REMARK 500 ASN D 69 -153.33 -128.74
REMARK 500 VAL D 105 -61.53 73.25
REMARK 500 TYR D 117 84.53 -158.04
REMARK 500 ALA D 150 -111.76 55.58
REMARK 500 SER D 264 -168.27 -124.49
REMARK 500 GLN D 287 166.77 69.94
REMARK 500 ASN E 69 -149.56 -133.66
REMARK 500 VAL E 105 -60.84 72.69
REMARK 500 TYR E 117 85.59 -157.80
REMARK 500 ALA E 150 -110.81 56.11
REMARK 500 SER E 264 -169.07 -126.87
REMARK 500 GLN E 287 167.82 70.35
REMARK 500 ASN F 69 -150.43 -129.75
REMARK 500 VAL F 105 -62.55 72.57
REMARK 500 TYR F 117 83.04 -157.62
REMARK 500 ALA F 150 -113.77 56.07
REMARK 500 SER F 264 -166.00 -129.26
REMARK 500 GLN F 287 166.75 69.96
REMARK 500 ASN G 69 -150.04 -130.16
REMARK 500 VAL G 105 -62.81 71.64
REMARK 500 TYR G 117 85.81 -159.53
REMARK 500 ALA G 150 -114.84 55.92
REMARK 500 SER G 264 -168.17 -128.05
REMARK 500 GLN G 287 165.76 70.57
REMARK 500 ASN H 69 -149.02 -133.04
REMARK 500 VAL H 105 -59.83 73.84
REMARK 500 TYR H 117 83.23 -158.74
REMARK 500 ALA H 150 -114.56 56.76
REMARK 500 SER H 264 -169.19 -127.73
REMARK 500 GLN H 287 168.55 69.89
REMARK 500 ASN I 69 -150.25 -133.17
REMARK 500 VAL I 105 -62.77 72.65
REMARK 500 TYR I 117 84.62 -157.32
REMARK 500
REMARK 500 THIS ENTRY HAS 58 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 CA A 301
REMARK 615 CA B 301
REMARK 615 CA C 301
REMARK 615 CA D 301
REMARK 615 CA E 301
REMARK 615 CA F 301
REMARK 615 CA G 301
REMARK 615 CA H 301
REMARK 615 CA I 301
REMARK 615 CA I 303
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 235 OD1
REMARK 620 2 ASP A 235 OD2 47.2
REMARK 620 3 ASP A 262 OD1 126.6 91.1
REMARK 620 4 GLU B 257 OE1 88.7 134.6 130.9
REMARK 620 5 GLU B 257 OE2 102.1 132.2 81.5 55.9
REMARK 620 N 1 2 3 4
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 OE1
REMARK 620 2 GLU A 257 OE2 55.5
REMARK 620 3 ASP B 234 OD1 152.5 97.0
REMARK 620 4 ASP B 234 OD2 118.2 77.6 45.0
REMARK 620 5 ASP B 235 OD1 116.3 152.0 87.0 86.1
REMARK 620 6 ASP B 235 OD2 125.6 150.4 78.4 115.2 57.5
REMARK 620 7 ASP B 262 OD1 98.8 72.4 70.9 103.1 134.2 78.6
REMARK 620 N 1 2 3 4 5 6
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 235 OD2
REMARK 620 2 GLU E 257 OE1 97.9
REMARK 620 N 1
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 GLU C 257 OE2 54.2
REMARK 620 3 ASP E 234 OD2 83.1 130.1
REMARK 620 4 ASP E 235 OD1 173.9 130.8 94.1
REMARK 620 5 ASP E 235 OD2 118.9 116.6 105.5 56.6
REMARK 620 N 1 2 3 4
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 41.6
REMARK 620 3 ASP D 235 OD1 86.8 86.0
REMARK 620 4 ASP D 235 OD2 79.0 112.6 56.5
REMARK 620 5 ASP D 262 OD1 66.3 98.0 129.6 76.3
REMARK 620 6 GLU G 257 OE1 147.1 112.3 115.1 133.2 109.6
REMARK 620 7 GLU G 257 OE2 92.3 76.1 153.6 148.9 73.0 56.9
REMARK 620 N 1 2 3 4 5 6
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 OE1
REMARK 620 2 GLU D 257 OE2 45.4
REMARK 620 3 ASP G 234 OD1 139.4 94.1
REMARK 620 4 ASP G 235 OD1 101.6 101.4 82.6
REMARK 620 5 ASP G 262 OD1 109.7 103.1 76.4 148.5
REMARK 620 N 1 2 3 4
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 54.5
REMARK 620 3 ASP F 235 OD1 100.9 87.8
REMARK 620 4 ASP F 235 OD2 106.7 130.0 47.1
REMARK 620 5 ASP F 262 OD1 88.3 122.7 146.5 99.4
REMARK 620 6 GLU H 257 OE1 156.6 103.4 84.3 93.7 99.9
REMARK 620 7 GLU H 257 OE2 105.2 74.4 130.0 147.8 76.6 56.6
REMARK 620 N 1 2 3 4 5 6
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 OE1
REMARK 620 2 GLU F 257 OE2 55.8
REMARK 620 3 ASP H 234 OD1 165.1 111.2
REMARK 620 4 ASP H 234 OD2 115.8 82.8 51.4
REMARK 620 5 ASP H 235 OD1 96.7 141.6 90.7 87.7
REMARK 620 6 ASP H 235 OD2 105.6 152.1 89.2 125.0 51.8
REMARK 620 7 ASP H 262 OD1 104.0 77.9 78.0 113.1 139.2 88.5
REMARK 620 N 1 2 3 4 5 6
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 235 OD1
REMARK 620 2 ASP I 235 OD2 50.0
REMARK 620 3 ASP I 262 OD1 133.2 99.8
REMARK 620 4 GLU J 257 OE1 85.4 126.0 134.2
REMARK 620 5 GLU J 257 OE2 101.6 144.1 85.1 59.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA I 303 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU I 257 OE1
REMARK 620 2 GLU I 257 OE2 51.6
REMARK 620 3 ASP J 235 OD2 111.5 95.2
REMARK 620 4 ASP J 262 OD1 115.5 66.1 87.4
REMARK 620 N 1 2 3
DBREF 7XRV A 21 288 UNP Q8A0E4 Q8A0E4_BACTN 21 288
DBREF 7XRV B 21 288 UNP Q8A0E4 Q8A0E4_BACTN 21 288
DBREF 7XRV C 21 288 UNP Q8A0E4 Q8A0E4_BACTN 21 288
DBREF 7XRV D 21 288 UNP Q8A0E4 Q8A0E4_BACTN 21 288
DBREF 7XRV E 21 288 UNP Q8A0E4 Q8A0E4_BACTN 21 288
DBREF 7XRV F 21 288 UNP Q8A0E4 Q8A0E4_BACTN 21 288
DBREF 7XRV G 21 288 UNP Q8A0E4 Q8A0E4_BACTN 21 288
DBREF 7XRV H 21 288 UNP Q8A0E4 Q8A0E4_BACTN 21 288
DBREF 7XRV I 21 288 UNP Q8A0E4 Q8A0E4_BACTN 21 288
DBREF 7XRV J 21 288 UNP Q8A0E4 Q8A0E4_BACTN 21 288
SEQADV 7XRV MET A -2 UNP Q8A0E4 INITIATING METHIONINE
SEQADV 7XRV GLY A -1 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER A 0 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER A 1 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS A 2 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS A 3 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS A 4 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS A 5 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS A 6 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS A 7 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER A 8 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER A 9 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV GLY A 10 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV LEU A 11 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV VAL A 12 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV PRO A 13 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV ARG A 14 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV GLY A 15 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER A 16 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS A 17 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV MET A 18 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV LEU A 19 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV GLU A 20 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV ALA A 150 UNP Q8A0E4 SER 150 ENGINEERED MUTATION
SEQADV 7XRV MET B -2 UNP Q8A0E4 INITIATING METHIONINE
SEQADV 7XRV GLY B -1 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER B 0 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER B 1 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS B 2 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS B 3 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS B 4 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS B 5 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS B 6 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS B 7 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER B 8 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER B 9 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV GLY B 10 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV LEU B 11 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV VAL B 12 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV PRO B 13 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV ARG B 14 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV GLY B 15 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER B 16 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS B 17 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV MET B 18 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV LEU B 19 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV GLU B 20 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV ALA B 150 UNP Q8A0E4 SER 150 ENGINEERED MUTATION
SEQADV 7XRV MET C -2 UNP Q8A0E4 INITIATING METHIONINE
SEQADV 7XRV GLY C -1 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER C 0 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER C 1 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS C 2 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS C 3 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS C 4 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS C 5 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS C 6 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS C 7 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER C 8 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER C 9 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV GLY C 10 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV LEU C 11 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV VAL C 12 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV PRO C 13 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV ARG C 14 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV GLY C 15 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER C 16 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS C 17 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV MET C 18 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV LEU C 19 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV GLU C 20 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV ALA C 150 UNP Q8A0E4 SER 150 ENGINEERED MUTATION
SEQADV 7XRV MET D -2 UNP Q8A0E4 INITIATING METHIONINE
SEQADV 7XRV GLY D -1 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER D 0 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER D 1 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS D 2 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS D 3 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS D 4 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS D 5 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS D 6 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS D 7 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER D 8 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER D 9 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV GLY D 10 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV LEU D 11 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV VAL D 12 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV PRO D 13 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV ARG D 14 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV GLY D 15 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER D 16 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS D 17 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV MET D 18 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV LEU D 19 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV GLU D 20 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV ALA D 150 UNP Q8A0E4 SER 150 ENGINEERED MUTATION
SEQADV 7XRV MET E -2 UNP Q8A0E4 INITIATING METHIONINE
SEQADV 7XRV GLY E -1 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER E 0 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER E 1 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS E 2 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS E 3 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS E 4 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS E 5 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS E 6 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS E 7 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER E 8 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER E 9 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV GLY E 10 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV LEU E 11 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV VAL E 12 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV PRO E 13 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV ARG E 14 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV GLY E 15 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER E 16 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS E 17 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV MET E 18 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV LEU E 19 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV GLU E 20 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV ALA E 150 UNP Q8A0E4 SER 150 ENGINEERED MUTATION
SEQADV 7XRV MET F -2 UNP Q8A0E4 INITIATING METHIONINE
SEQADV 7XRV GLY F -1 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER F 0 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER F 1 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS F 2 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS F 3 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS F 4 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS F 5 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS F 6 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS F 7 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER F 8 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER F 9 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV GLY F 10 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV LEU F 11 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV VAL F 12 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV PRO F 13 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV ARG F 14 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV GLY F 15 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER F 16 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS F 17 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV MET F 18 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV LEU F 19 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV GLU F 20 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV ALA F 150 UNP Q8A0E4 SER 150 ENGINEERED MUTATION
SEQADV 7XRV MET G -2 UNP Q8A0E4 INITIATING METHIONINE
SEQADV 7XRV GLY G -1 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER G 0 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER G 1 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS G 2 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS G 3 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS G 4 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS G 5 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS G 6 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS G 7 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER G 8 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER G 9 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV GLY G 10 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV LEU G 11 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV VAL G 12 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV PRO G 13 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV ARG G 14 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV GLY G 15 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER G 16 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS G 17 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV MET G 18 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV LEU G 19 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV GLU G 20 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV ALA G 150 UNP Q8A0E4 SER 150 ENGINEERED MUTATION
SEQADV 7XRV MET H -2 UNP Q8A0E4 INITIATING METHIONINE
SEQADV 7XRV GLY H -1 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER H 0 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER H 1 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS H 2 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS H 3 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS H 4 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS H 5 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS H 6 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS H 7 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER H 8 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER H 9 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV GLY H 10 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV LEU H 11 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV VAL H 12 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV PRO H 13 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV ARG H 14 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV GLY H 15 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER H 16 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS H 17 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV MET H 18 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV LEU H 19 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV GLU H 20 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV ALA H 150 UNP Q8A0E4 SER 150 ENGINEERED MUTATION
SEQADV 7XRV MET I -2 UNP Q8A0E4 INITIATING METHIONINE
SEQADV 7XRV GLY I -1 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER I 0 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER I 1 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS I 2 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS I 3 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS I 4 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS I 5 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS I 6 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS I 7 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER I 8 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER I 9 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV GLY I 10 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV LEU I 11 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV VAL I 12 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV PRO I 13 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV ARG I 14 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV GLY I 15 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER I 16 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS I 17 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV MET I 18 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV LEU I 19 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV GLU I 20 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV ALA I 150 UNP Q8A0E4 SER 150 ENGINEERED MUTATION
SEQADV 7XRV MET J -2 UNP Q8A0E4 INITIATING METHIONINE
SEQADV 7XRV GLY J -1 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER J 0 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER J 1 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS J 2 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS J 3 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS J 4 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS J 5 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS J 6 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS J 7 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER J 8 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER J 9 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV GLY J 10 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV LEU J 11 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV VAL J 12 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV PRO J 13 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV ARG J 14 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV GLY J 15 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV SER J 16 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV HIS J 17 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV MET J 18 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV LEU J 19 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV GLU J 20 UNP Q8A0E4 EXPRESSION TAG
SEQADV 7XRV ALA J 150 UNP Q8A0E4 SER 150 ENGINEERED MUTATION
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 ALA 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 ALA 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 ALA 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 ALA 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 ALA 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 ALA 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 ALA 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 ALA 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 ALA 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 ALA 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 SZQ A 302 15
HET CA B 301 1
HET SZQ B 302 15
HET CA C 301 1
HET CA D 301 1
HET CA E 301 1
HET SZQ E 302 15
HET CA F 301 1
HET SZQ F 302 15
HET CA G 301 1
HET SZQ G 302 15
HET CA H 301 1
HET SZQ H 302 15
HET CA I 301 1
HET SZQ I 302 15
HET CA I 303 1
HETNAM CA CALCIUM ION
HETNAM SZQ TRANS-METHYLFERULATE
HETSYN SZQ METHYL (~{E})-3-(3-METHOXY-4-OXIDANYL-PHENYL)PROP-2-
HETSYN 2 SZQ ENOATE
FORMUL 11 CA 10(CA 2+)
FORMUL 12 SZQ 7(C11 H12 O4)
FORMUL 28 HOH *462(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 ALA A 150 TYR A 163 1 14
HELIX 7 AA7 PRO A 164 PHE A 167 5 4
HELIX 8 AA8 GLY A 177 SER A 189 1 13
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 ALA B 150 TYR B 163 1 14
HELIX 21 AC3 PRO B 164 PHE B 167 5 4
HELIX 22 AC4 GLY B 177 SER B 189 1 13
HELIX 23 AC5 ASP B 190 VAL B 194 5 5
HELIX 24 AC6 SER B 195 MET B 206 1 12
HELIX 25 AC7 ASP B 207 SER B 215 1 9
HELIX 26 AC8 PRO B 216 ILE B 226 1 11
HELIX 27 AC9 LEU B 238 HIS B 252 1 15
HELIX 28 AD1 SER B 266 GLN B 287 1 22
HELIX 29 AD2 THR C 71 PHE C 76 1 6
HELIX 30 AD3 GLN C 78 GLU C 89 1 12
HELIX 31 AD4 ASN C 118 GLU C 126 1 9
HELIX 32 AD5 GLU C 126 TYR C 135 1 10
HELIX 33 AD6 GLU C 140 ARG C 142 5 3
HELIX 34 AD7 ALA C 150 TYR C 163 1 14
HELIX 35 AD8 PRO C 164 PHE C 167 5 4
HELIX 36 AD9 GLY C 177 SER C 189 1 13
HELIX 37 AE1 ASP C 190 VAL C 194 5 5
HELIX 38 AE2 SER C 195 MET C 206 1 12
HELIX 39 AE3 ASP C 207 SER C 215 1 9
HELIX 40 AE4 PRO C 216 ILE C 226 1 11
HELIX 41 AE5 LEU C 238 HIS C 252 1 15
HELIX 42 AE6 SER C 266 GLN C 287 1 22
HELIX 43 AE7 THR D 71 PHE D 76 1 6
HELIX 44 AE8 GLN D 78 GLU D 89 1 12
HELIX 45 AE9 ASN D 118 GLU D 126 1 9
HELIX 46 AF1 GLU D 126 TYR D 135 1 10
HELIX 47 AF2 GLU D 140 ARG D 142 5 3
HELIX 48 AF3 ALA D 150 TYR D 163 1 14
HELIX 49 AF4 PRO D 164 PHE D 167 5 4
HELIX 50 AF5 GLY D 177 GLN D 188 1 12
HELIX 51 AF6 ASP D 190 VAL D 194 5 5
HELIX 52 AF7 SER D 195 MET D 206 1 12
HELIX 53 AF8 ASP D 207 SER D 215 1 9
HELIX 54 AF9 PRO D 216 ILE D 226 1 11
HELIX 55 AG1 LEU D 238 HIS D 252 1 15
HELIX 56 AG2 SER D 266 GLN D 287 1 22
HELIX 57 AG3 THR E 71 PHE E 76 1 6
HELIX 58 AG4 GLN E 78 GLU E 89 1 12
HELIX 59 AG5 ASN E 118 GLU E 126 1 9
HELIX 60 AG6 GLU E 126 TYR E 135 1 10
HELIX 61 AG7 GLU E 140 ARG E 142 5 3
HELIX 62 AG8 ALA E 150 TYR E 163 1 14
HELIX 63 AG9 PRO E 164 PHE E 167 5 4
HELIX 64 AH1 GLY E 177 GLN E 188 1 12
HELIX 65 AH2 ASP E 190 VAL E 194 5 5
HELIX 66 AH3 SER E 195 MET E 206 1 12
HELIX 67 AH4 ASP E 207 SER E 215 1 9
HELIX 68 AH5 PRO E 216 ILE E 226 1 11
HELIX 69 AH6 LEU E 238 HIS E 252 1 15
HELIX 70 AH7 SER E 266 GLN E 287 1 22
HELIX 71 AH8 THR F 71 PHE F 76 1 6
HELIX 72 AH9 GLN F 78 GLU F 89 1 12
HELIX 73 AI1 ASN F 118 GLU F 126 1 9
HELIX 74 AI2 GLU F 126 TYR F 135 1 10
HELIX 75 AI3 GLU F 140 ARG F 142 5 3
HELIX 76 AI4 ALA F 150 TYR F 163 1 14
HELIX 77 AI5 PRO F 164 PHE F 167 5 4
HELIX 78 AI6 GLY F 177 SER F 189 1 13
HELIX 79 AI7 ASP F 190 VAL F 194 5 5
HELIX 80 AI8 SER F 195 MET F 206 1 12
HELIX 81 AI9 ASP F 207 SER F 215 1 9
HELIX 82 AJ1 PRO F 216 ILE F 226 1 11
HELIX 83 AJ2 LEU F 238 HIS F 252 1 15
HELIX 84 AJ3 SER F 266 GLN F 287 1 22
HELIX 85 AJ4 THR G 71 PHE G 76 1 6
HELIX 86 AJ5 GLN G 78 GLU G 89 1 12
HELIX 87 AJ6 ASN G 118 GLU G 126 1 9
HELIX 88 AJ7 GLU G 126 TYR G 135 1 10
HELIX 89 AJ8 GLU G 140 ARG G 142 5 3
HELIX 90 AJ9 ALA G 150 TYR G 163 1 14
HELIX 91 AK1 PRO G 164 PHE G 167 5 4
HELIX 92 AK2 GLY G 177 SER G 189 1 13
HELIX 93 AK3 ASP G 190 VAL G 194 5 5
HELIX 94 AK4 SER G 195 MET G 206 1 12
HELIX 95 AK5 ASP G 207 SER G 215 1 9
HELIX 96 AK6 PRO G 216 ILE G 226 1 11
HELIX 97 AK7 LEU G 238 HIS G 252 1 15
HELIX 98 AK8 SER G 266 GLN G 287 1 22
HELIX 99 AK9 THR H 71 PHE H 76 1 6
HELIX 100 AL1 GLN H 78 GLU H 89 1 12
HELIX 101 AL2 ASN H 118 GLU H 126 1 9
HELIX 102 AL3 GLU H 126 TYR H 135 1 10
HELIX 103 AL4 GLU H 140 ARG H 142 5 3
HELIX 104 AL5 ALA H 150 TYR H 163 1 14
HELIX 105 AL6 PRO H 164 PHE H 167 5 4
HELIX 106 AL7 GLY H 177 GLN H 188 1 12
HELIX 107 AL8 ASP H 190 VAL H 194 5 5
HELIX 108 AL9 SER H 195 MET H 206 1 12
HELIX 109 AM1 ASP H 207 SER H 215 1 9
HELIX 110 AM2 PRO H 216 ILE H 226 1 11
HELIX 111 AM3 LEU H 238 HIS H 252 1 15
HELIX 112 AM4 SER H 266 GLN H 287 1 22
HELIX 113 AM5 THR I 71 PHE I 76 1 6
HELIX 114 AM6 GLN I 78 GLU I 89 1 12
HELIX 115 AM7 ASN I 118 GLU I 126 1 9
HELIX 116 AM8 GLU I 126 TYR I 135 1 10
HELIX 117 AM9 GLU I 140 ARG I 142 5 3
HELIX 118 AN1 ALA I 150 TYR I 163 1 14
HELIX 119 AN2 PRO I 164 PHE I 167 5 4
HELIX 120 AN3 GLY I 177 GLN I 188 1 12
HELIX 121 AN4 ASP I 190 VAL I 194 5 5
HELIX 122 AN5 SER I 195 MET I 206 1 12
HELIX 123 AN6 ASP I 207 SER I 215 1 9
HELIX 124 AN7 PRO I 216 ILE I 226 1 11
HELIX 125 AN8 LEU I 238 HIS I 252 1 15
HELIX 126 AN9 SER I 266 GLN I 287 1 22
HELIX 127 AO1 THR J 71 PHE J 76 1 6
HELIX 128 AO2 GLN J 78 GLU J 89 1 12
HELIX 129 AO3 ASN J 118 GLU J 126 1 9
HELIX 130 AO4 GLU J 126 TYR J 135 1 10
HELIX 131 AO5 GLU J 140 ARG J 142 5 3
HELIX 132 AO6 ALA J 150 TYR J 163 1 14
HELIX 133 AO7 PRO J 164 PHE J 167 5 4
HELIX 134 AO8 GLY J 177 GLN J 188 1 12
HELIX 135 AO9 ASP J 190 VAL J 194 5 5
HELIX 136 AP1 SER J 195 MET J 206 1 12
HELIX 137 AP2 ASP J 207 SER J 215 1 9
HELIX 138 AP3 PRO J 216 ILE J 226 1 11
HELIX 139 AP4 LEU J 238 HIS J 252 1 15
HELIX 140 AP5 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 SER A 33 O MET A 38
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 SER A 147 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 SER B 33 O MET B 38
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 ILE B 97 N TYR B 45
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 ALA B 145 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 GLU B 257 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 SER C 33 O MET C 38
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 ALA C 145 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 LEU D 63
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 ARG D 227 N VAL D 170
SHEET 8 AA8 8 GLU D 257 LYS D 261 1 O ARG D 259 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 VAL E 31 O ARG E 40
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 60 O ILE E 96
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 ARG E 259 N ILE E 230
SHEET 1 AB2 8 LYS F 24 SER F 33 0
SHEET 2 AB2 8 MET F 38 LEU F 46 -1 O LEU F 46 N LYS F 24
SHEET 3 AB2 8 ILE F 96 PRO F 100 -1 O MET F 99 N SER F 43
SHEET 4 AB2 8 VAL F 59 LEU F 63 1 N LEU F 62 O VAL F 98
SHEET 5 AB2 8 ARG F 144 LEU F 149 1 O ALA F 145 N TYR F 61
SHEET 6 AB2 8 ALA F 169 LEU F 173 1 O LEU F 173 N GLY F 148
SHEET 7 AB2 8 ARG F 227 GLY F 233 1 O ARG F 227 N VAL F 170
SHEET 8 AB2 8 GLU F 257 LYS F 261 1 O ARG F 259 N ILE F 230
SHEET 1 AB3 3 LYS G 24 TYR G 26 0
SHEET 2 AB3 3 MET G 38 LEU G 46 -1 O LEU G 46 N LYS G 24
SHEET 3 AB3 3 THR G 30 SER G 33 -1 N VAL G 31 O ARG G 40
SHEET 1 AB4 8 LYS G 24 TYR G 26 0
SHEET 2 AB4 8 MET G 38 LEU G 46 -1 O LEU G 46 N LYS G 24
SHEET 3 AB4 8 ILE G 96 PRO G 100 -1 O ILE G 97 N TYR G 45
SHEET 4 AB4 8 VAL G 59 LEU G 63 1 N LEU G 60 O ILE G 96
SHEET 5 AB4 8 ARG G 144 LEU G 149 1 O ALA G 145 N TYR G 61
SHEET 6 AB4 8 ALA G 169 LEU G 173 1 O LEU G 173 N GLY G 148
SHEET 7 AB4 8 ARG G 227 GLY G 233 1 O TYR G 229 N VAL G 170
SHEET 8 AB4 8 GLU G 257 LYS G 261 1 O GLU G 257 N ILE G 230
SHEET 1 AB5 3 LYS H 24 TYR H 26 0
SHEET 2 AB5 3 MET H 38 LEU H 46 -1 O LEU H 46 N LYS H 24
SHEET 3 AB5 3 THR H 30 SER H 33 -1 N VAL H 31 O ARG H 40
SHEET 1 AB6 8 LYS H 24 TYR H 26 0
SHEET 2 AB6 8 MET H 38 LEU H 46 -1 O LEU H 46 N LYS H 24
SHEET 3 AB6 8 ILE H 96 PRO H 100 -1 O MET H 99 N SER H 43
SHEET 4 AB6 8 VAL H 59 LEU H 63 1 N LEU H 60 O ILE H 96
SHEET 5 AB6 8 ARG H 144 LEU H 149 1 O ALA H 145 N TYR H 61
SHEET 6 AB6 8 ALA H 169 LEU H 173 1 O LEU H 173 N GLY H 148
SHEET 7 AB6 8 ARG H 227 GLY H 233 1 O ARG H 227 N VAL H 170
SHEET 8 AB6 8 GLU H 257 LYS H 261 1 O ARG H 259 N ILE H 230
SHEET 1 AB7 3 LYS I 24 TYR I 26 0
SHEET 2 AB7 3 MET I 38 LEU I 46 -1 O LEU I 46 N LYS I 24
SHEET 3 AB7 3 THR I 30 SER I 33 -1 N VAL I 31 O ARG I 40
SHEET 1 AB8 8 LYS I 24 TYR I 26 0
SHEET 2 AB8 8 MET I 38 LEU I 46 -1 O LEU I 46 N LYS I 24
SHEET 3 AB8 8 ILE I 96 PRO I 100 -1 O MET I 99 N SER I 43
SHEET 4 AB8 8 VAL I 59 LEU I 63 1 N LEU I 62 O VAL I 98
SHEET 5 AB8 8 ARG I 144 LEU I 149 1 O SER I 147 N LEU I 63
SHEET 6 AB8 8 ALA I 169 LEU I 173 1 O LEU I 173 N GLY I 148
SHEET 7 AB8 8 ARG I 227 SER I 231 1 O TYR I 229 N VAL I 170
SHEET 8 AB8 8 HIS I 256 ARG I 259 1 O GLU I 257 N ILE I 230
SHEET 1 AB9 3 LYS J 24 TYR J 26 0
SHEET 2 AB9 3 MET J 38 LEU J 46 -1 O LEU J 46 N LYS J 24
SHEET 3 AB9 3 THR J 30 SER J 33 -1 N SER J 33 O MET J 38
SHEET 1 AC1 8 LYS J 24 TYR J 26 0
SHEET 2 AC1 8 MET J 38 LEU J 46 -1 O LEU J 46 N LYS J 24
SHEET 3 AC1 8 ILE J 96 PRO J 100 -1 O MET J 99 N SER J 43
SHEET 4 AC1 8 VAL J 59 LEU J 63 1 N LEU J 62 O VAL J 98
SHEET 5 AC1 8 ARG J 144 LEU J 149 1 O SER J 147 N LEU J 63
SHEET 6 AC1 8 ALA J 169 LEU J 173 1 O LEU J 173 N GLY J 148
SHEET 7 AC1 8 ARG J 227 GLY J 233 1 O TYR J 229 N VAL J 170
SHEET 8 AC1 8 HIS J 256 LYS J 261 1 O GLU J 257 N ILE J 230
LINK OD1 ASP A 235 CA CA A 301 1555 1555 2.97
LINK OD2 ASP A 235 CA CA A 301 1555 1555 2.22
LINK OE1 GLU A 257 CA CA B 301 1555 1555 2.45
LINK OE2 GLU A 257 CA CA B 301 1555 1555 2.18
LINK OD1 ASP A 262 CA CA A 301 1555 1555 2.55
LINK CA CA A 301 OE1 GLU B 257 1555 1555 2.35
LINK CA CA A 301 OE2 GLU B 257 1555 1555 2.28
LINK OD1 ASP B 234 CA CA B 301 1555 1555 2.96
LINK OD2 ASP B 234 CA CA B 301 1555 1555 2.71
LINK OD1 ASP B 235 CA CA B 301 1555 1555 2.38
LINK OD2 ASP B 235 CA CA B 301 1555 1555 2.17
LINK OD1 ASP B 262 CA CA B 301 1555 1555 2.91
LINK OD2 ASP C 235 CA CA C 301 1555 1555 2.37
LINK OE1 GLU C 257 CA CA E 301 1555 1555 2.30
LINK OE2 GLU C 257 CA CA E 301 1555 1555 2.46
LINK CA CA C 301 OE1 GLU E 257 1555 1555 2.31
LINK OD1 ASP D 234 CA CA D 301 1555 1555 3.04
LINK OD2 ASP D 234 CA CA D 301 1555 1555 3.09
LINK OD1 ASP D 235 CA CA D 301 1555 1555 2.40
LINK OD2 ASP D 235 CA CA D 301 1555 1555 2.21
LINK OE1 GLU D 257 CA CA G 301 1555 1555 3.09
LINK OE2 GLU D 257 CA CA G 301 1555 1555 2.24
LINK OD1 ASP D 262 CA CA D 301 1555 1555 2.44
LINK CA CA D 301 OE1 GLU G 257 1555 1555 2.28
LINK CA CA D 301 OE2 GLU G 257 1555 1555 2.30
LINK OD2 ASP E 234 CA CA E 301 1555 1555 2.57
LINK OD1 ASP E 235 CA CA E 301 1555 1555 2.27
LINK OD2 ASP E 235 CA CA E 301 1555 1555 2.34
LINK OD1 ASP F 234 CA CA F 301 1555 1555 2.26
LINK OD2 ASP F 234 CA CA F 301 1555 1555 2.51
LINK OD1 ASP F 235 CA CA F 301 1555 1555 2.98
LINK OD2 ASP F 235 CA CA F 301 1555 1555 2.12
LINK OE1 GLU F 257 CA CA H 301 1555 1555 2.45
LINK OE2 GLU F 257 CA CA H 301 1555 1555 2.18
LINK OD1 ASP F 262 CA CA F 301 1555 1555 2.37
LINK CA CA F 301 OE1 GLU H 257 1555 1555 2.38
LINK CA CA F 301 OE2 GLU H 257 1555 1555 2.17
LINK OD1 ASP G 234 CA CA G 301 1555 1555 2.95
LINK OD1 ASP G 235 CA CA G 301 1555 1555 2.77
LINK OD1 ASP G 262 CA CA G 301 1555 1555 2.39
LINK OD1 ASP H 234 CA CA H 301 1555 1555 2.51
LINK OD2 ASP H 234 CA CA H 301 1555 1555 2.53
LINK OD1 ASP H 235 CA CA H 301 1555 1555 2.72
LINK OD2 ASP H 235 CA CA H 301 1555 1555 2.14
LINK OD1 ASP H 262 CA CA H 301 1555 1555 2.44
LINK OD1 ASP I 235 CA CA I 301 1555 1555 2.84
LINK OD2 ASP I 235 CA CA I 301 1555 1555 2.04
LINK OE1 GLU I 257 CA CA I 303 1555 1555 2.24
LINK OE2 GLU I 257 CA CA I 303 1555 1555 2.65
LINK OD1 ASP I 262 CA CA I 301 1555 1555 2.21
LINK CA CA I 301 OE1 GLU J 257 1555 1555 2.22
LINK CA CA I 301 OE2 GLU J 257 1555 1555 2.14
LINK CA CA I 303 OD2 ASP J 235 1555 1555 2.28
LINK CA CA I 303 OD1 ASP J 262 1555 1555 3.07
CRYST1 146.854 153.548 165.548 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 0.006809 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006513 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006041 0.00000
TER 2161 TYR A 288
TER 4326 TYR B 288
TER 6487 TYR C 288
TER 8639 TYR D 288
TER 10800 TYR E 288
TER 12953 TYR F 288
TER 15106 TYR G 288
TER 17259 TYR H 288
TER 19412 TYR I 288
TER 21565 TYR J 288
MASTER 685 0 17 140 107 0 0 622128 10 177 230
END |