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HEADER HYDROLASE 22-JUL-20 7CLZ
TITLE CRYSTAL STRUCTURE OF ALP1U W187F/Y247F IN COMPLEX WITH FLUOSTATIN C
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE HYDROLASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: ALP1U;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES AMBOFACIENS (STRAIN ATCC 23877 /
SOURCE 3 3486 / DSM 40053 / JCM 4204 / NBRC 12836 / NRRL B-2516);
SOURCE 4 ORGANISM_TAXID: 278992;
SOURCE 5 GENE: SAMT0137, SAMT0138;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS SUBSTRATE, COMPLEX, BIOSYNTHESIS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.ZHANG,D.BIDHAN
REVDAT 1 07-OCT-20 7CLZ 0
JRNL AUTH L.ZHANG,Z.YINGLI,C.D.BIDHAN,C.ZHANG
JRNL TITL CRYSTAL STRUCTURE OF WILD TYPE ALP1U FROM THE BIOSYNTHESIS
JRNL TITL 2 OF KINAMYCINS.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692+SVN
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.70
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.333
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 66921
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.203
REMARK 3 FREE R VALUE TEST SET COUNT : 3482
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 8.0400 - 6.1354 0.99 2747 135 0.1653 0.2407
REMARK 3 2 6.1354 - 4.8718 1.00 2615 155 0.1847 0.2281
REMARK 3 3 4.8718 - 4.2565 1.00 2581 144 0.1600 0.1825
REMARK 3 4 4.2565 - 3.8675 1.00 2588 117 0.1676 0.1831
REMARK 3 5 3.8675 - 3.5905 1.00 2542 170 0.1809 0.2195
REMARK 3 6 3.5905 - 3.3789 1.00 2577 136 0.1903 0.2502
REMARK 3 7 3.3789 - 3.2097 1.00 2565 125 0.2077 0.2461
REMARK 3 8 3.2097 - 3.0700 0.99 2548 124 0.2043 0.2717
REMARK 3 9 3.0700 - 2.9518 1.00 2523 145 0.2046 0.2743
REMARK 3 10 2.9518 - 2.8500 1.00 2518 143 0.2085 0.2645
REMARK 3 11 2.8500 - 2.7609 1.00 2522 140 0.2078 0.2344
REMARK 3 12 2.7609 - 2.6820 0.97 2466 132 0.2319 0.3351
REMARK 3 13 2.6820 - 2.6114 0.99 2517 130 0.2111 0.2565
REMARK 3 14 2.6114 - 2.5477 1.00 2535 139 0.2094 0.2986
REMARK 3 15 2.5477 - 2.4898 1.00 2486 161 0.2164 0.2770
REMARK 3 16 2.4898 - 2.4368 1.00 2515 151 0.2285 0.3063
REMARK 3 17 2.4368 - 2.3881 0.99 2497 149 0.2228 0.2935
REMARK 3 18 2.3881 - 2.3430 1.00 2507 136 0.2194 0.2780
REMARK 3 19 2.3430 - 2.3012 1.00 2509 138 0.2121 0.3380
REMARK 3 20 2.3012 - 2.2621 1.00 2560 99 0.2106 0.2841
REMARK 3 21 2.2621 - 2.2257 1.00 2502 132 0.2178 0.2925
REMARK 3 22 2.2257 - 2.1914 1.00 2512 137 0.2189 0.2663
REMARK 3 23 2.1914 - 2.1592 1.00 2527 141 0.2137 0.3213
REMARK 3 24 2.1592 - 2.1288 1.00 2497 154 0.2191 0.3017
REMARK 3 25 2.1288 - 2.1000 1.00 2483 149 0.2167 0.2892
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) : 0.257
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.018
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.17
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.52
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.009 9455
REMARK 3 ANGLE : 1.172 12882
REMARK 3 CHIRALITY : 0.050 1348
REMARK 3 PLANARITY : 0.006 1765
REMARK 3 DIHEDRAL : 13.030 3404
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): -1.2627 -26.2364 43.8728
REMARK 3 T TENSOR
REMARK 3 T11: 0.1573 T22: 0.1901
REMARK 3 T33: 0.2002 T12: -0.0050
REMARK 3 T13: 0.0263 T23: -0.0271
REMARK 3 L TENSOR
REMARK 3 L11: 0.6453 L22: 0.5782
REMARK 3 L33: 0.6024 L12: -0.2669
REMARK 3 L13: 0.2060 L23: -0.2694
REMARK 3 S TENSOR
REMARK 3 S11: 0.0035 S12: 0.0542 S13: 0.0386
REMARK 3 S21: 0.0090 S22: 0.0038 S23: -0.0573
REMARK 3 S31: -0.0486 S32: 0.0812 S33: -0.0138
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'A' AND SEGID 'AA '
REMARK 3 SELECTION : CHAIN 'B' AND SEGID 'BA '
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN 'A' AND SEGID 'AA '
REMARK 3 SELECTION : CHAIN 'C' AND SEGID 'CA '
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN 'A' AND SEGID 'AA '
REMARK 3 SELECTION : CHAIN 'D' AND SEGID 'DA '
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 7CLZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-JUL-20.
REMARK 100 THE DEPOSITION ID IS D_1300017751.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JUN-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL19U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97853
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS 1.9_1692+SVN
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 1.9_1692+SVN
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 67180
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 44.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.03037
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.5800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.18800
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: MOLREP
REMARK 200 STARTING MODEL: 3R3V
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MMT PH 5.0, 25% PEG 1500,
REMARK 280 EVAPORATION, RECRYSTALLIZATION, TEMPERATURE 277K
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 48.33200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 58.72500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 50.10400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 58.72500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 48.33200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 50.10400
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3830 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21190 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 LEU A 2
REMARK 465 ALA A 3
REMARK 465 LEU A 4
REMARK 465 GLY A 5
REMARK 465 THR A 6
REMARK 465 GLY A 7
REMARK 465 ALA A 8
REMARK 465 THR A 9
REMARK 465 ALA A 10
REMARK 465 LEU A 11
REMARK 465 ALA A 12
REMARK 465 VAL A 13
REMARK 465 THR A 14
REMARK 465 GLY A 15
REMARK 465 SER A 16
REMARK 465 PRO A 17
REMARK 465 ALA A 18
REMARK 465 ALA A 19
REMARK 465 ALA A 20
REMARK 465 HIS A 21
REMARK 465 PRO A 22
REMARK 465 GLY A 23
REMARK 465 PRO A 24
REMARK 465 HIS A 25
REMARK 465 PRO A 26
REMARK 465 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 LEU B 2
REMARK 465 ALA B 3
REMARK 465 LEU B 4
REMARK 465 GLY B 5
REMARK 465 THR B 6
REMARK 465 GLY B 7
REMARK 465 ALA B 8
REMARK 465 THR B 9
REMARK 465 ALA B 10
REMARK 465 LEU B 11
REMARK 465 ALA B 12
REMARK 465 VAL B 13
REMARK 465 THR B 14
REMARK 465 GLY B 15
REMARK 465 SER B 16
REMARK 465 PRO B 17
REMARK 465 ALA B 18
REMARK 465 ALA B 19
REMARK 465 ALA B 20
REMARK 465 HIS B 21
REMARK 465 PRO B 22
REMARK 465 GLY B 23
REMARK 465 PRO B 24
REMARK 465 HIS B 25
REMARK 465 PRO B 26
REMARK 465 MET C -19
REMARK 465 GLY C -18
REMARK 465 SER C -17
REMARK 465 SER C -16
REMARK 465 HIS C -15
REMARK 465 HIS C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 HIS C -10
REMARK 465 SER C -9
REMARK 465 SER C -8
REMARK 465 GLY C -7
REMARK 465 LEU C -6
REMARK 465 VAL C -5
REMARK 465 PRO C -4
REMARK 465 ARG C -3
REMARK 465 GLY C -2
REMARK 465 SER C -1
REMARK 465 HIS C 0
REMARK 465 MET C 1
REMARK 465 LEU C 2
REMARK 465 ALA C 3
REMARK 465 LEU C 4
REMARK 465 GLY C 5
REMARK 465 THR C 6
REMARK 465 GLY C 7
REMARK 465 ALA C 8
REMARK 465 THR C 9
REMARK 465 ALA C 10
REMARK 465 LEU C 11
REMARK 465 ALA C 12
REMARK 465 VAL C 13
REMARK 465 THR C 14
REMARK 465 GLY C 15
REMARK 465 SER C 16
REMARK 465 PRO C 17
REMARK 465 ALA C 18
REMARK 465 ALA C 19
REMARK 465 ALA C 20
REMARK 465 HIS C 21
REMARK 465 PRO C 22
REMARK 465 GLY C 23
REMARK 465 PRO C 24
REMARK 465 HIS C 25
REMARK 465 PRO C 26
REMARK 465 MET D -19
REMARK 465 GLY D -18
REMARK 465 SER D -17
REMARK 465 SER D -16
REMARK 465 HIS D -15
REMARK 465 HIS D -14
REMARK 465 HIS D -13
REMARK 465 HIS D -12
REMARK 465 HIS D -11
REMARK 465 HIS D -10
REMARK 465 SER D -9
REMARK 465 SER D -8
REMARK 465 GLY D -7
REMARK 465 LEU D -6
REMARK 465 VAL D -5
REMARK 465 PRO D -4
REMARK 465 ARG D -3
REMARK 465 GLY D -2
REMARK 465 SER D -1
REMARK 465 HIS D 0
REMARK 465 MET D 1
REMARK 465 LEU D 2
REMARK 465 ALA D 3
REMARK 465 LEU D 4
REMARK 465 GLY D 5
REMARK 465 THR D 6
REMARK 465 GLY D 7
REMARK 465 ALA D 8
REMARK 465 THR D 9
REMARK 465 ALA D 10
REMARK 465 LEU D 11
REMARK 465 ALA D 12
REMARK 465 VAL D 13
REMARK 465 THR D 14
REMARK 465 GLY D 15
REMARK 465 SER D 16
REMARK 465 PRO D 17
REMARK 465 ALA D 18
REMARK 465 ALA D 19
REMARK 465 ALA D 20
REMARK 465 HIS D 21
REMARK 465 PRO D 22
REMARK 465 GLY D 23
REMARK 465 PRO D 24
REMARK 465 HIS D 25
REMARK 465 PRO D 26
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 ARG A 44 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 88 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 129 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 129 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 44 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 129 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 44 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 88 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 124 CD NE CZ NH1 NH2
REMARK 470 ARG D 129 CG CD NE CZ NH1 NH2
REMARK 470 ILE D 174 CG1 CG2 CD1
REMARK 470 ARG D 177 CG CD NE CZ NH1 NH2
REMARK 470 PHE D 274 CG CD1 CD2 CE1 CE2 CZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 H DY9 A 401 O HOH A 503 1.43
REMARK 500 H DY9 C 401 O HOH C 505 1.45
REMARK 500 OD1 ASN A 273 NH1 ARG A 294 2.09
REMARK 500 OE1 GLU C 64 NH2 ARG C 155 2.09
REMARK 500 OD2 ASP B 218 OG SER B 220 2.11
REMARK 500 OE2 GLU D 152 O HOH D 501 2.12
REMARK 500 O HOH A 596 O HOH A 597 2.12
REMARK 500 OD1 ASP C 137 O6 DY9 C 401 2.13
REMARK 500 O1 MLT B 402 O HOH B 501 2.14
REMARK 500 NH1 ARG A 245 O HOH A 501 2.15
REMARK 500 OD1 ASP A 137 O6 DY9 A 401 2.16
REMARK 500 O6 DY9 D 401 O HOH D 502 2.17
REMARK 500 OD1 ASN D 273 NH1 ARG D 294 2.17
REMARK 500 O HOH A 501 O HOH A 593 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU B 175 CA - CB - CG ANGL. DEV. = 18.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 137 -132.40 60.20
REMARK 500 ASP A 161 -34.90 72.65
REMARK 500 THR A 180 -80.58 -94.73
REMARK 500 ALA A 194 -47.05 71.68
REMARK 500 SER A 215 -50.74 -147.24
REMARK 500 HIS A 300 -41.73 -149.92
REMARK 500 ASP B 137 -134.22 62.50
REMARK 500 ASP B 161 -32.55 71.41
REMARK 500 THR B 180 -114.66 -104.03
REMARK 500 ALA B 194 -47.66 69.14
REMARK 500 SER B 215 -51.70 -147.74
REMARK 500 HIS B 300 -43.88 -151.75
REMARK 500 PRO C 73 78.79 -101.65
REMARK 500 ASP C 137 -135.19 62.61
REMARK 500 ASP C 161 -33.69 71.62
REMARK 500 ALA C 194 -49.85 69.18
REMARK 500 SER C 215 -49.89 -146.05
REMARK 500 HIS C 300 -43.07 -150.94
REMARK 500 ASP D 137 -135.82 61.16
REMARK 500 ASP D 161 -36.48 72.06
REMARK 500 THR D 180 -127.52 -99.81
REMARK 500 ALA D 194 -50.28 67.84
REMARK 500 SER D 215 -51.97 -146.94
REMARK 500 HIS D 300 -45.09 -151.61
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DY9 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MLT A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MLT B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MLT B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DY9 C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BO3 C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DY9 D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BO3 D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MLT D 403
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6KXH RELATED DB: PDB
DBREF 7CLZ A 1 319 UNP Q1RQU8 Q1RQU8_STRA7 1 319
DBREF 7CLZ B 1 319 UNP Q1RQU8 Q1RQU8_STRA7 1 319
DBREF 7CLZ C 1 319 UNP Q1RQU8 Q1RQU8_STRA7 1 319
DBREF 7CLZ D 1 319 UNP Q1RQU8 Q1RQU8_STRA7 1 319
SEQADV 7CLZ MET A -19 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ GLY A -18 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ SER A -17 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ SER A -16 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ HIS A -15 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ HIS A -14 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ HIS A -13 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ HIS A -12 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ HIS A -11 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ HIS A -10 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ SER A -9 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ SER A -8 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ GLY A -7 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ LEU A -6 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ VAL A -5 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ PRO A -4 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ ARG A -3 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ GLY A -2 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ SER A -1 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ HIS A 0 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ PHE A 187 UNP Q1RQU8 TRP 187 ENGINEERED MUTATION
SEQADV 7CLZ PHE A 247 UNP Q1RQU8 TYR 247 ENGINEERED MUTATION
SEQADV 7CLZ MET B -19 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ GLY B -18 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ SER B -17 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ SER B -16 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ HIS B -15 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ HIS B -14 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ HIS B -13 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ HIS B -12 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ HIS B -11 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ HIS B -10 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ SER B -9 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ SER B -8 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ GLY B -7 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ LEU B -6 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ VAL B -5 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ PRO B -4 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ ARG B -3 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ GLY B -2 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ SER B -1 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ HIS B 0 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ PHE B 187 UNP Q1RQU8 TRP 187 ENGINEERED MUTATION
SEQADV 7CLZ PHE B 247 UNP Q1RQU8 TYR 247 ENGINEERED MUTATION
SEQADV 7CLZ MET C -19 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ GLY C -18 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ SER C -17 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ SER C -16 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ HIS C -15 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ HIS C -14 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ HIS C -13 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ HIS C -12 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ HIS C -11 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ HIS C -10 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ SER C -9 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ SER C -8 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ GLY C -7 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ LEU C -6 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ VAL C -5 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ PRO C -4 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ ARG C -3 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ GLY C -2 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ SER C -1 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ HIS C 0 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ PHE C 187 UNP Q1RQU8 TRP 187 ENGINEERED MUTATION
SEQADV 7CLZ PHE C 247 UNP Q1RQU8 TYR 247 ENGINEERED MUTATION
SEQADV 7CLZ MET D -19 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ GLY D -18 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ SER D -17 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ SER D -16 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ HIS D -15 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ HIS D -14 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ HIS D -13 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ HIS D -12 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ HIS D -11 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ HIS D -10 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ SER D -9 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ SER D -8 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ GLY D -7 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ LEU D -6 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ VAL D -5 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ PRO D -4 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ ARG D -3 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ GLY D -2 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ SER D -1 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ HIS D 0 UNP Q1RQU8 EXPRESSION TAG
SEQADV 7CLZ PHE D 187 UNP Q1RQU8 TRP 187 ENGINEERED MUTATION
SEQADV 7CLZ PHE D 247 UNP Q1RQU8 TYR 247 ENGINEERED MUTATION
SEQRES 1 A 339 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 339 LEU VAL PRO ARG GLY SER HIS MET LEU ALA LEU GLY THR
SEQRES 3 A 339 GLY ALA THR ALA LEU ALA VAL THR GLY SER PRO ALA ALA
SEQRES 4 A 339 ALA HIS PRO GLY PRO HIS PRO GLY PRO VAL PRO SER ASP
SEQRES 5 A 339 ARG GLU LEU ALA ARG SER LEU PRO GLY GLY PHE ARG SER
SEQRES 6 A 339 ARG HIS ALA ARG VAL GLY GLY VAL ARG LEU HIS TYR VAL
SEQRES 7 A 339 SER GLY GLY HIS GLY GLU PRO LEU LEU LEU VAL PRO GLY
SEQRES 8 A 339 TRP PRO GLN THR TRP TRP ALA TYR ARG LYS VAL MET PRO
SEQRES 9 A 339 GLN LEU ALA ARG ARG TYR HIS VAL ILE ALA VAL ASP LEU
SEQRES 10 A 339 ARG GLY MET GLY GLY SER ASP LYS PRO ALA GLY GLY TYR
SEQRES 11 A 339 ASP LYS LYS THR MET ALA ALA ASP LEU HIS ALA LEU VAL
SEQRES 12 A 339 ARG GLY LEU GLY HIS ARG GLN VAL ASN VAL ALA GLY HIS
SEQRES 13 A 339 ASP ILE GLY SER MET VAL ALA PHE ALA PHE ALA ALA ASN
SEQRES 14 A 339 HIS PRO GLU ALA THR ARG LYS VAL ALA LEU LEU ASP THR
SEQRES 15 A 339 PRO HIS PRO ASP GLN SER GLU TYR GLU MET ARG ILE LEU
SEQRES 16 A 339 CYS ARG PRO GLY THR GLY THR THR LEU TRP TRP PHE ALA
SEQRES 17 A 339 PHE ASN GLN LEU GLN ALA LEU PRO GLU GLN LEU MET HIS
SEQRES 18 A 339 GLY ARG MET ARG HIS VAL ILE ASP TRP LEU TYR ALA ASN
SEQRES 19 A 339 SER LEU ALA ASP GLN SER LEU VAL GLY ASP LEU ASP ARG
SEQRES 20 A 339 ASP ILE TYR ALA ASN ALA TYR ASN SER PRO GLN ALA VAL
SEQRES 21 A 339 ARG ALA GLY THR ARG TRP PHE GLN ALA CYS HIS GLN ASP
SEQRES 22 A 339 ILE THR ASP GLN ALA GLY TYR GLY LYS LEU THR MET PRO
SEQRES 23 A 339 VAL LEU GLY ILE GLY GLY ASN PHE THR PHE GLU ASP LEU
SEQRES 24 A 339 ARG ASN LYS LEU THR ALA GLN ALA THR ASP VAL HIS MET
SEQRES 25 A 339 VAL ARG ALA SER LYS SER VAL HIS TYR LEU PRO GLU GLU
SEQRES 26 A 339 GLU PRO ASP VAL VAL ALA GLY ALA LEU LEU ASP PHE PHE
SEQRES 27 A 339 GLY
SEQRES 1 B 339 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 339 LEU VAL PRO ARG GLY SER HIS MET LEU ALA LEU GLY THR
SEQRES 3 B 339 GLY ALA THR ALA LEU ALA VAL THR GLY SER PRO ALA ALA
SEQRES 4 B 339 ALA HIS PRO GLY PRO HIS PRO GLY PRO VAL PRO SER ASP
SEQRES 5 B 339 ARG GLU LEU ALA ARG SER LEU PRO GLY GLY PHE ARG SER
SEQRES 6 B 339 ARG HIS ALA ARG VAL GLY GLY VAL ARG LEU HIS TYR VAL
SEQRES 7 B 339 SER GLY GLY HIS GLY GLU PRO LEU LEU LEU VAL PRO GLY
SEQRES 8 B 339 TRP PRO GLN THR TRP TRP ALA TYR ARG LYS VAL MET PRO
SEQRES 9 B 339 GLN LEU ALA ARG ARG TYR HIS VAL ILE ALA VAL ASP LEU
SEQRES 10 B 339 ARG GLY MET GLY GLY SER ASP LYS PRO ALA GLY GLY TYR
SEQRES 11 B 339 ASP LYS LYS THR MET ALA ALA ASP LEU HIS ALA LEU VAL
SEQRES 12 B 339 ARG GLY LEU GLY HIS ARG GLN VAL ASN VAL ALA GLY HIS
SEQRES 13 B 339 ASP ILE GLY SER MET VAL ALA PHE ALA PHE ALA ALA ASN
SEQRES 14 B 339 HIS PRO GLU ALA THR ARG LYS VAL ALA LEU LEU ASP THR
SEQRES 15 B 339 PRO HIS PRO ASP GLN SER GLU TYR GLU MET ARG ILE LEU
SEQRES 16 B 339 CYS ARG PRO GLY THR GLY THR THR LEU TRP TRP PHE ALA
SEQRES 17 B 339 PHE ASN GLN LEU GLN ALA LEU PRO GLU GLN LEU MET HIS
SEQRES 18 B 339 GLY ARG MET ARG HIS VAL ILE ASP TRP LEU TYR ALA ASN
SEQRES 19 B 339 SER LEU ALA ASP GLN SER LEU VAL GLY ASP LEU ASP ARG
SEQRES 20 B 339 ASP ILE TYR ALA ASN ALA TYR ASN SER PRO GLN ALA VAL
SEQRES 21 B 339 ARG ALA GLY THR ARG TRP PHE GLN ALA CYS HIS GLN ASP
SEQRES 22 B 339 ILE THR ASP GLN ALA GLY TYR GLY LYS LEU THR MET PRO
SEQRES 23 B 339 VAL LEU GLY ILE GLY GLY ASN PHE THR PHE GLU ASP LEU
SEQRES 24 B 339 ARG ASN LYS LEU THR ALA GLN ALA THR ASP VAL HIS MET
SEQRES 25 B 339 VAL ARG ALA SER LYS SER VAL HIS TYR LEU PRO GLU GLU
SEQRES 26 B 339 GLU PRO ASP VAL VAL ALA GLY ALA LEU LEU ASP PHE PHE
SEQRES 27 B 339 GLY
SEQRES 1 C 339 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 339 LEU VAL PRO ARG GLY SER HIS MET LEU ALA LEU GLY THR
SEQRES 3 C 339 GLY ALA THR ALA LEU ALA VAL THR GLY SER PRO ALA ALA
SEQRES 4 C 339 ALA HIS PRO GLY PRO HIS PRO GLY PRO VAL PRO SER ASP
SEQRES 5 C 339 ARG GLU LEU ALA ARG SER LEU PRO GLY GLY PHE ARG SER
SEQRES 6 C 339 ARG HIS ALA ARG VAL GLY GLY VAL ARG LEU HIS TYR VAL
SEQRES 7 C 339 SER GLY GLY HIS GLY GLU PRO LEU LEU LEU VAL PRO GLY
SEQRES 8 C 339 TRP PRO GLN THR TRP TRP ALA TYR ARG LYS VAL MET PRO
SEQRES 9 C 339 GLN LEU ALA ARG ARG TYR HIS VAL ILE ALA VAL ASP LEU
SEQRES 10 C 339 ARG GLY MET GLY GLY SER ASP LYS PRO ALA GLY GLY TYR
SEQRES 11 C 339 ASP LYS LYS THR MET ALA ALA ASP LEU HIS ALA LEU VAL
SEQRES 12 C 339 ARG GLY LEU GLY HIS ARG GLN VAL ASN VAL ALA GLY HIS
SEQRES 13 C 339 ASP ILE GLY SER MET VAL ALA PHE ALA PHE ALA ALA ASN
SEQRES 14 C 339 HIS PRO GLU ALA THR ARG LYS VAL ALA LEU LEU ASP THR
SEQRES 15 C 339 PRO HIS PRO ASP GLN SER GLU TYR GLU MET ARG ILE LEU
SEQRES 16 C 339 CYS ARG PRO GLY THR GLY THR THR LEU TRP TRP PHE ALA
SEQRES 17 C 339 PHE ASN GLN LEU GLN ALA LEU PRO GLU GLN LEU MET HIS
SEQRES 18 C 339 GLY ARG MET ARG HIS VAL ILE ASP TRP LEU TYR ALA ASN
SEQRES 19 C 339 SER LEU ALA ASP GLN SER LEU VAL GLY ASP LEU ASP ARG
SEQRES 20 C 339 ASP ILE TYR ALA ASN ALA TYR ASN SER PRO GLN ALA VAL
SEQRES 21 C 339 ARG ALA GLY THR ARG TRP PHE GLN ALA CYS HIS GLN ASP
SEQRES 22 C 339 ILE THR ASP GLN ALA GLY TYR GLY LYS LEU THR MET PRO
SEQRES 23 C 339 VAL LEU GLY ILE GLY GLY ASN PHE THR PHE GLU ASP LEU
SEQRES 24 C 339 ARG ASN LYS LEU THR ALA GLN ALA THR ASP VAL HIS MET
SEQRES 25 C 339 VAL ARG ALA SER LYS SER VAL HIS TYR LEU PRO GLU GLU
SEQRES 26 C 339 GLU PRO ASP VAL VAL ALA GLY ALA LEU LEU ASP PHE PHE
SEQRES 27 C 339 GLY
SEQRES 1 D 339 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 339 LEU VAL PRO ARG GLY SER HIS MET LEU ALA LEU GLY THR
SEQRES 3 D 339 GLY ALA THR ALA LEU ALA VAL THR GLY SER PRO ALA ALA
SEQRES 4 D 339 ALA HIS PRO GLY PRO HIS PRO GLY PRO VAL PRO SER ASP
SEQRES 5 D 339 ARG GLU LEU ALA ARG SER LEU PRO GLY GLY PHE ARG SER
SEQRES 6 D 339 ARG HIS ALA ARG VAL GLY GLY VAL ARG LEU HIS TYR VAL
SEQRES 7 D 339 SER GLY GLY HIS GLY GLU PRO LEU LEU LEU VAL PRO GLY
SEQRES 8 D 339 TRP PRO GLN THR TRP TRP ALA TYR ARG LYS VAL MET PRO
SEQRES 9 D 339 GLN LEU ALA ARG ARG TYR HIS VAL ILE ALA VAL ASP LEU
SEQRES 10 D 339 ARG GLY MET GLY GLY SER ASP LYS PRO ALA GLY GLY TYR
SEQRES 11 D 339 ASP LYS LYS THR MET ALA ALA ASP LEU HIS ALA LEU VAL
SEQRES 12 D 339 ARG GLY LEU GLY HIS ARG GLN VAL ASN VAL ALA GLY HIS
SEQRES 13 D 339 ASP ILE GLY SER MET VAL ALA PHE ALA PHE ALA ALA ASN
SEQRES 14 D 339 HIS PRO GLU ALA THR ARG LYS VAL ALA LEU LEU ASP THR
SEQRES 15 D 339 PRO HIS PRO ASP GLN SER GLU TYR GLU MET ARG ILE LEU
SEQRES 16 D 339 CYS ARG PRO GLY THR GLY THR THR LEU TRP TRP PHE ALA
SEQRES 17 D 339 PHE ASN GLN LEU GLN ALA LEU PRO GLU GLN LEU MET HIS
SEQRES 18 D 339 GLY ARG MET ARG HIS VAL ILE ASP TRP LEU TYR ALA ASN
SEQRES 19 D 339 SER LEU ALA ASP GLN SER LEU VAL GLY ASP LEU ASP ARG
SEQRES 20 D 339 ASP ILE TYR ALA ASN ALA TYR ASN SER PRO GLN ALA VAL
SEQRES 21 D 339 ARG ALA GLY THR ARG TRP PHE GLN ALA CYS HIS GLN ASP
SEQRES 22 D 339 ILE THR ASP GLN ALA GLY TYR GLY LYS LEU THR MET PRO
SEQRES 23 D 339 VAL LEU GLY ILE GLY GLY ASN PHE THR PHE GLU ASP LEU
SEQRES 24 D 339 ARG ASN LYS LEU THR ALA GLN ALA THR ASP VAL HIS MET
SEQRES 25 D 339 VAL ARG ALA SER LYS SER VAL HIS TYR LEU PRO GLU GLU
SEQRES 26 D 339 GLU PRO ASP VAL VAL ALA GLY ALA LEU LEU ASP PHE PHE
SEQRES 27 D 339 GLY
HET DY9 A 401 36
HET NA A 402 1
HET MLT A 403 13
HET NA B 401 1
HET MLT B 402 13
HET MLT B 403 13
HET DY9 C 401 36
HET BO3 C 402 7
HET DY9 D 401 36
HET BO3 D 402 7
HET MLT D 403 13
HETNAM DY9 FLUOSTATIN C
HETNAM NA SODIUM ION
HETNAM MLT D-MALATE
HETNAM BO3 BORIC ACID
HETSYN MLT (2R)-2-HYDROXYBUTANEDIOIC ACID; 2-HYDROXY-SUCCINIC ACID
FORMUL 5 DY9 3(C18 H12 O6)
FORMUL 6 NA 2(NA 1+)
FORMUL 7 MLT 4(C4 H6 O5)
FORMUL 12 BO3 2(B H3 O3)
FORMUL 16 HOH *354(H2 O)
HELIX 1 AA1 SER A 31 LEU A 39 1 9
HELIX 2 AA2 THR A 75 ARG A 80 5 6
HELIX 3 AA3 VAL A 82 ARG A 88 1 7
HELIX 4 AA4 ASP A 111 LEU A 126 1 16
HELIX 5 AA5 ASP A 137 HIS A 150 1 14
HELIX 6 AA6 ASP A 166 MET A 172 5 7
HELIX 7 AA7 LEU A 184 ASN A 190 1 7
HELIX 8 AA8 ALA A 194 HIS A 201 1 8
HELIX 9 AA9 ARG A 203 ASN A 214 1 12
HELIX 10 AB1 ASP A 218 VAL A 222 5 5
HELIX 11 AB2 GLY A 223 ASN A 235 1 13
HELIX 12 AB3 SER A 236 ALA A 249 1 14
HELIX 13 AB4 ALA A 249 GLY A 259 1 11
HELIX 14 AB5 THR A 275 ALA A 287 1 13
HELIX 15 AB6 TYR A 301 GLU A 306 1 6
HELIX 16 AB7 GLU A 306 GLY A 319 1 14
HELIX 17 AB8 SER B 31 SER B 38 1 8
HELIX 18 AB9 THR B 75 ARG B 80 5 6
HELIX 19 AC1 VAL B 82 ARG B 88 1 7
HELIX 20 AC2 ASP B 111 LEU B 126 1 16
HELIX 21 AC3 ASP B 137 HIS B 150 1 14
HELIX 22 AC4 ASP B 166 MET B 172 5 7
HELIX 23 AC5 LEU B 184 ASN B 190 1 7
HELIX 24 AC6 ALA B 194 HIS B 201 1 8
HELIX 25 AC7 ARG B 203 ASN B 214 1 12
HELIX 26 AC8 ASP B 218 VAL B 222 5 5
HELIX 27 AC9 GLY B 223 ASN B 235 1 13
HELIX 28 AD1 SER B 236 ALA B 249 1 14
HELIX 29 AD2 ALA B 249 GLY B 259 1 11
HELIX 30 AD3 THR B 275 ALA B 287 1 13
HELIX 31 AD4 TYR B 301 GLU B 306 1 6
HELIX 32 AD5 GLU B 306 GLY B 319 1 14
HELIX 33 AD6 SER C 31 SER C 38 1 8
HELIX 34 AD7 THR C 75 ARG C 80 5 6
HELIX 35 AD8 VAL C 82 ARG C 88 1 7
HELIX 36 AD9 ASP C 111 LEU C 126 1 16
HELIX 37 AE1 ASP C 137 HIS C 150 1 14
HELIX 38 AE2 ASP C 166 MET C 172 5 7
HELIX 39 AE3 LEU C 184 ASN C 190 1 7
HELIX 40 AE4 ALA C 194 HIS C 201 1 8
HELIX 41 AE5 ARG C 203 ASN C 214 1 12
HELIX 42 AE6 ASP C 218 VAL C 222 5 5
HELIX 43 AE7 GLY C 223 ASN C 235 1 13
HELIX 44 AE8 SER C 236 ALA C 249 1 14
HELIX 45 AE9 ALA C 249 GLY C 259 1 11
HELIX 46 AF1 THR C 275 ALA C 287 1 13
HELIX 47 AF2 TYR C 301 GLU C 306 1 6
HELIX 48 AF3 GLU C 306 GLY C 319 1 14
HELIX 49 AF4 SER D 31 SER D 38 1 8
HELIX 50 AF5 THR D 75 ARG D 80 5 6
HELIX 51 AF6 VAL D 82 ARG D 88 1 7
HELIX 52 AF7 ASP D 111 LEU D 126 1 16
HELIX 53 AF8 ASP D 137 HIS D 150 1 14
HELIX 54 AF9 ASP D 166 MET D 172 5 7
HELIX 55 AG1 LEU D 184 ASN D 190 1 7
HELIX 56 AG2 ALA D 194 HIS D 201 1 8
HELIX 57 AG3 ARG D 203 ASN D 214 1 12
HELIX 58 AG4 ASP D 218 VAL D 222 5 5
HELIX 59 AG5 GLY D 223 ASN D 235 1 13
HELIX 60 AG6 SER D 236 ALA D 249 1 14
HELIX 61 AG7 ALA D 249 GLY D 259 1 11
HELIX 62 AG8 THR D 275 ALA D 287 1 13
HELIX 63 AG9 TYR D 301 GLU D 306 1 6
HELIX 64 AH1 GLU D 306 GLY D 319 1 14
SHEET 1 AA1 8 ARG A 44 VAL A 50 0
SHEET 2 AA1 8 VAL A 53 GLY A 60 -1 O TYR A 57 N ARG A 46
SHEET 3 AA1 8 TYR A 90 VAL A 95 -1 O ALA A 94 N VAL A 58
SHEET 4 AA1 8 GLU A 64 VAL A 69 1 N LEU A 66 O ILE A 93
SHEET 5 AA1 8 VAL A 131 HIS A 136 1 O ASN A 132 N LEU A 67
SHEET 6 AA1 8 THR A 154 LEU A 160 1 O LEU A 160 N GLY A 135
SHEET 7 AA1 8 VAL A 267 GLY A 272 1 O LEU A 268 N LEU A 159
SHEET 8 AA1 8 VAL A 290 ALA A 295 1 O ALA A 295 N GLY A 271
SHEET 1 AA2 8 ARG B 44 VAL B 50 0
SHEET 2 AA2 8 VAL B 53 GLY B 60 -1 O TYR B 57 N ARG B 46
SHEET 3 AA2 8 TYR B 90 VAL B 95 -1 O ALA B 94 N VAL B 58
SHEET 4 AA2 8 GLU B 64 VAL B 69 1 N LEU B 68 O ILE B 93
SHEET 5 AA2 8 VAL B 131 HIS B 136 1 O ASN B 132 N LEU B 67
SHEET 6 AA2 8 THR B 154 LEU B 160 1 O LEU B 160 N GLY B 135
SHEET 7 AA2 8 VAL B 267 GLY B 272 1 O LEU B 268 N LEU B 159
SHEET 8 AA2 8 VAL B 290 ALA B 295 1 O HIS B 291 N GLY B 269
SHEET 1 AA3 8 ARG C 44 VAL C 50 0
SHEET 2 AA3 8 VAL C 53 GLY C 60 -1 O TYR C 57 N ARG C 46
SHEET 3 AA3 8 TYR C 90 VAL C 95 -1 O ALA C 94 N VAL C 58
SHEET 4 AA3 8 GLU C 64 VAL C 69 1 N LEU C 66 O ILE C 93
SHEET 5 AA3 8 VAL C 131 HIS C 136 1 O ASN C 132 N LEU C 67
SHEET 6 AA3 8 THR C 154 LEU C 160 1 O ARG C 155 N VAL C 131
SHEET 7 AA3 8 VAL C 267 GLY C 272 1 O LEU C 268 N LEU C 159
SHEET 8 AA3 8 VAL C 290 ALA C 295 1 O HIS C 291 N GLY C 269
SHEET 1 AA4 8 ARG D 44 VAL D 50 0
SHEET 2 AA4 8 VAL D 53 GLY D 60 -1 O TYR D 57 N ARG D 46
SHEET 3 AA4 8 TYR D 90 VAL D 95 -1 O ALA D 94 N VAL D 58
SHEET 4 AA4 8 GLU D 64 VAL D 69 1 N LEU D 66 O ILE D 93
SHEET 5 AA4 8 VAL D 131 HIS D 136 1 O ASN D 132 N LEU D 67
SHEET 6 AA4 8 THR D 154 LEU D 160 1 O ALA D 158 N VAL D 133
SHEET 7 AA4 8 VAL D 267 GLY D 272 1 O LEU D 268 N LEU D 159
SHEET 8 AA4 8 VAL D 290 ALA D 295 1 O HIS D 291 N GLY D 269
CISPEP 1 TRP A 72 PRO A 73 0 -9.46
CISPEP 2 TRP B 72 PRO B 73 0 -12.26
CISPEP 3 TRP C 72 PRO C 73 0 -10.15
CISPEP 4 TRP D 72 PRO D 73 0 -11.23
SITE 1 AC1 12 TRP A 72 ASP A 137 MET A 141 THR A 162
SITE 2 AC1 12 TRP A 186 PHE A 187 LEU A 211 ASN A 214
SITE 3 AC1 12 VAL A 299 HIS A 300 TYR A 301 HOH A 503
SITE 1 AC2 3 ARG A 33 ARG A 37 SER A 45
SITE 1 AC3 10 HIS A 201 GLY A 202 ASN A 235 PRO A 237
SITE 2 AC3 10 HOH A 519 HOH A 569 ARG D 205 GLN D 219
SITE 3 AC3 10 VAL D 222 ARG D 227
SITE 1 AC4 4 ARG B 33 ARG B 37 ARG B 44 SER B 45
SITE 1 AC5 9 HIS B 201 GLY B 202 ASN B 235 SER B 236
SITE 2 AC5 9 PRO B 237 HOH B 501 ARG C 205 GLN C 219
SITE 3 AC5 9 ARG C 227
SITE 1 AC6 9 LYS B 105 PRO B 106 ALA B 107 TYR B 110
SITE 2 AC6 9 GLN B 238 ARG B 241 ALA B 242 ARG B 245
SITE 3 AC6 9 HOH B 577
SITE 1 AC7 12 TRP C 72 ASP C 137 THR C 162 TRP C 186
SITE 2 AC7 12 PHE C 187 LEU C 211 ASN C 214 PHE C 247
SITE 3 AC7 12 VAL C 299 HIS C 300 TYR C 301 HOH C 505
SITE 1 AC8 5 LYS C 105 PRO C 106 ALA C 107 ARG C 241
SITE 2 AC8 5 ARG C 245
SITE 1 AC9 11 TRP D 72 ASP D 137 THR D 162 TRP D 186
SITE 2 AC9 11 PHE D 187 LEU D 211 ASN D 214 PHE D 247
SITE 3 AC9 11 HIS D 300 TYR D 301 HOH D 502
SITE 1 AD1 4 PRO D 106 ALA D 107 ARG D 241 ARG D 245
SITE 1 AD2 11 HOH B 532 GLY C 202 HIS C 206 HOH C 539
SITE 2 AD2 11 HOH C 555 GLY D 202 ARG D 205 HIS D 206
SITE 3 AD2 11 HOH D 509 HOH D 533 HOH D 556
CRYST1 96.664 100.208 117.450 90.00 90.00 90.00 P 21 21 21 16
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 0.010345 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009979 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008514 0.00000
TER 2271 GLY A 319
TER 4554 GLY B 319
TER 6831 GLY C 319
TER 9082 GLY D 319
MASTER 600 0 11 64 32 0 26 6 9550 4 174 108
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