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HEADER HYDROLASE 11-SEP-19 6KXH
TITLE ALP1U_Y247F MUTANT IN COMPLEX WITH FLUOSTATIN C
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE HYDROLASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: EPOXY HYDROLASE ALP1U;
COMPND 5 EC: 3.3.2.3;
COMPND 6 ENGINEERED: YES;
COMPND 7 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 BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS HYDROLYSE EPOXIDE, CIS-VICINAL DIOL, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.ZHANG,Z.YINGLI,C.D.BIDHAN,C.ZHANG
REVDAT 1 16-SEP-20 6KXH 0
JRNL AUTH L.ZHANG,Z.YINGLI,C.D.BIDHAN,C.ZHANG
JRNL TITL ALP1U W187F/Y247F MUTANT IN COMPLEX WITH FLUOSTATIN C AND
JRNL TITL 2 INTERMEDIATE (SOAKED FLUOSTATIN C FOR 6 HOURS)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.78 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) : 1.78
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.98
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.336
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 111737
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.968
REMARK 3 FREE R VALUE TEST SET COUNT : 5551
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 31.9800 - 5.5229 0.98 3744 176 0.1440 0.1826
REMARK 3 2 5.5229 - 4.3873 1.00 3668 175 0.1292 0.1674
REMARK 3 3 4.3873 - 3.8338 1.00 3617 189 0.1296 0.1351
REMARK 3 4 3.8338 - 3.4837 1.00 3595 178 0.1478 0.1518
REMARK 3 5 3.4837 - 3.2343 1.00 3605 166 0.1741 0.2393
REMARK 3 6 3.2343 - 3.0437 1.00 3542 195 0.1872 0.2255
REMARK 3 7 3.0437 - 2.8914 1.00 3569 192 0.1831 0.2209
REMARK 3 8 2.8914 - 2.7656 1.00 3531 218 0.1760 0.2187
REMARK 3 9 2.7656 - 2.6592 1.00 3528 195 0.1760 0.2157
REMARK 3 10 2.6592 - 2.5675 1.00 3554 184 0.1803 0.2121
REMARK 3 11 2.5675 - 2.4872 1.00 3543 192 0.1758 0.2030
REMARK 3 12 2.4872 - 2.4162 1.00 3516 180 0.1895 0.2541
REMARK 3 13 2.4162 - 2.3526 1.00 3521 186 0.1820 0.2234
REMARK 3 14 2.3526 - 2.2952 1.00 3581 171 0.1821 0.2209
REMARK 3 15 2.2952 - 2.2430 1.00 3504 192 0.2270 0.2735
REMARK 3 16 2.2430 - 2.1953 1.00 3520 197 0.2078 0.2503
REMARK 3 17 2.1953 - 2.1514 1.00 3491 197 0.1883 0.2396
REMARK 3 18 2.1514 - 2.1108 1.00 3525 184 0.1823 0.2282
REMARK 3 19 2.1108 - 2.0731 1.00 3516 172 0.1865 0.2242
REMARK 3 20 2.0731 - 2.0380 1.00 3535 168 0.1912 0.2106
REMARK 3 21 2.0380 - 2.0051 1.00 3539 178 0.1856 0.2071
REMARK 3 22 2.0051 - 1.9743 1.00 3508 192 0.1839 0.2269
REMARK 3 23 1.9743 - 1.9452 1.00 3500 184 0.1992 0.2373
REMARK 3 24 1.9452 - 1.9178 1.00 3527 168 0.2418 0.2805
REMARK 3 25 1.9178 - 1.8919 1.00 3471 200 0.2771 0.3126
REMARK 3 26 1.8919 - 1.8674 1.00 3549 186 0.1982 0.2329
REMARK 3 27 1.8674 - 1.8440 1.00 3498 190 0.2014 0.2559
REMARK 3 28 1.8440 - 1.8218 1.00 3508 189 0.2110 0.2543
REMARK 3 29 1.8218 - 1.8006 1.00 3477 190 0.2128 0.2757
REMARK 3 30 1.8006 - 1.7804 0.98 3404 167 0.2262 0.2846
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.176
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.530
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.42
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.09
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 : 0.007 9515
REMARK 3 ANGLE : 1.087 12984
REMARK 3 CHIRALITY : 0.047 1353
REMARK 3 PLANARITY : 0.005 1796
REMARK 3 DIHEDRAL : 12.648 3448
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): -1.7114 -26.4759 43.6857
REMARK 3 T TENSOR
REMARK 3 T11: 0.1871 T22: 0.1371
REMARK 3 T33: 0.2334 T12: 0.0021
REMARK 3 T13: 0.0449 T23: -0.0155
REMARK 3 L TENSOR
REMARK 3 L11: 0.5685 L22: 0.2810
REMARK 3 L33: 0.8803 L12: -0.0615
REMARK 3 L13: 0.5101 L23: -0.1929
REMARK 3 S TENSOR
REMARK 3 S11: -0.0087 S12: 0.0372 S13: 0.0691
REMARK 3 S21: 0.0266 S22: -0.0224 S23: -0.0328
REMARK 3 S31: -0.0961 S32: 0.0963 S33: 0.0245
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 6KXH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-SEP-19.
REMARK 100 THE DEPOSITION ID IS D_1300013505.
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 : NULL
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 : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 111803
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.780
REMARK 200 RESOLUTION RANGE LOW (A) : 31.980
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 1.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.1800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.78
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.84
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.96
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MMT PH5.0, 25% PEG 1500, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, 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 48.73850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 58.74050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 50.78100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 58.74050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 48.73850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 50.78100
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: 3540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21000 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -45.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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 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 129 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 129 CG CD NE CZ NH1 NH2
REMARK 470 PHE B 274 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG C 124 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 155 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 177 CG CD NE CZ NH1 NH2
REMARK 470 PHE C 274 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU C 277 CG CD OE1 OE2
REMARK 470 ARG D 33 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 129 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 277 CG CD OE1 OE2
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 OE2 GLU B 277 NH2 ARG B 280 2.01
REMARK 500 O HOH C 528 O HOH D 645 2.07
REMARK 500 O HOH C 503 O HOH C 507 2.08
REMARK 500 OG1 THR C 183 O HOH C 501 2.09
REMARK 500 O THR B 264 O HOH B 501 2.11
REMARK 500 O6 DY9 C 402 O HOH C 502 2.12
REMARK 500 SD MET B 83 O HOH B 690 2.14
REMARK 500 O HOH A 502 O HOH A 545 2.14
REMARK 500 OD2 ASP A 161 O HOH A 501 2.15
REMARK 500 OE2 GLU A 277 NH2 ARG A 280 2.16
REMARK 500 O HOH B 533 O HOH B 620 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NH2 ARG D 88 O HOH C 560 4546 2.07
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 LYS A 105 76.24 -119.81
REMARK 500 ASP A 137 -133.40 63.37
REMARK 500 ASP A 161 -40.61 71.09
REMARK 500 THR A 180 -121.92 -92.25
REMARK 500 LEU A 184 49.10 -80.75
REMARK 500 ALA A 194 -52.36 72.89
REMARK 500 SER A 215 -53.56 -145.37
REMARK 500 HIS A 300 -41.05 -151.48
REMARK 500 ASP B 137 -133.36 62.97
REMARK 500 ASP B 161 -40.65 70.83
REMARK 500 THR B 180 -125.28 -120.54
REMARK 500 ALA B 194 -50.58 72.08
REMARK 500 SER B 215 -51.83 -144.46
REMARK 500 HIS B 300 -41.78 -152.64
REMARK 500 ASP C 137 -133.26 61.47
REMARK 500 ASP C 161 -40.88 73.82
REMARK 500 THR C 180 23.09 -153.93
REMARK 500 ALA C 194 -50.18 71.91
REMARK 500 SER C 215 -53.62 -144.42
REMARK 500 HIS C 300 -43.28 -150.44
REMARK 500 ASP D 137 -133.38 62.67
REMARK 500 ASP D 161 -40.99 72.84
REMARK 500 ALA D 194 -51.14 71.63
REMARK 500 SER D 215 -54.80 -144.32
REMARK 500 HIS D 300 -43.38 -152.19
REMARK 500
REMARK 500 REMARK: NULL
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 NA C 401 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 197 OE2
REMARK 620 2 HOH C 548 O 117.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA D 401 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 197 OE2
REMARK 620 2 HOH D 553 O 116.0
REMARK 620 N 1
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 MLT A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DY9 B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DY9 C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DY9 D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
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: 6KXC RELATED DB: PDB
DBREF 6KXH A 1 319 UNP Q1RQU8 Q1RQU8_STRA7 1 319
DBREF 6KXH B 1 319 UNP Q1RQU8 Q1RQU8_STRA7 1 319
DBREF 6KXH C 1 319 UNP Q1RQU8 Q1RQU8_STRA7 1 319
DBREF 6KXH D 1 319 UNP Q1RQU8 Q1RQU8_STRA7 1 319
SEQADV 6KXH MET A -19 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH GLY A -18 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH SER A -17 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH SER A -16 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH HIS A -15 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH HIS A -14 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH HIS A -13 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH HIS A -12 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH HIS A -11 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH HIS A -10 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH SER A -9 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH SER A -8 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH GLY A -7 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH LEU A -6 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH VAL A -5 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH PRO A -4 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH ARG A -3 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH GLY A -2 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH SER A -1 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH HIS A 0 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH PHE A 247 UNP Q1RQU8 TYR 247 ENGINEERED MUTATION
SEQADV 6KXH MET B -19 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH GLY B -18 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH SER B -17 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH SER B -16 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH HIS B -15 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH HIS B -14 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH HIS B -13 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH HIS B -12 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH HIS B -11 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH HIS B -10 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH SER B -9 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH SER B -8 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH GLY B -7 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH LEU B -6 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH VAL B -5 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH PRO B -4 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH ARG B -3 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH GLY B -2 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH SER B -1 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH HIS B 0 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH PHE B 247 UNP Q1RQU8 TYR 247 ENGINEERED MUTATION
SEQADV 6KXH MET C -19 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH GLY C -18 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH SER C -17 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH SER C -16 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH HIS C -15 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH HIS C -14 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH HIS C -13 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH HIS C -12 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH HIS C -11 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH HIS C -10 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH SER C -9 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH SER C -8 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH GLY C -7 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH LEU C -6 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH VAL C -5 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH PRO C -4 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH ARG C -3 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH GLY C -2 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH SER C -1 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH HIS C 0 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH PHE C 247 UNP Q1RQU8 TYR 247 ENGINEERED MUTATION
SEQADV 6KXH MET D -19 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH GLY D -18 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH SER D -17 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH SER D -16 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH HIS D -15 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH HIS D -14 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH HIS D -13 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH HIS D -12 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH HIS D -11 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH HIS D -10 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH SER D -9 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH SER D -8 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH GLY D -7 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH LEU D -6 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH VAL D -5 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH PRO D -4 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH ARG D -3 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH GLY D -2 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH SER D -1 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH HIS D 0 UNP Q1RQU8 EXPRESSION TAG
SEQADV 6KXH 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 TRP 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 TRP 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 TRP 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 TRP 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 MLT A 402 13
HET NA B 401 1
HET DY9 B 402 36
HET NA C 401 1
HET DY9 C 402 36
HET NA D 401 1
HET DY9 D 402 36
HET MLT D 403 13
HETNAM DY9 FLUOSTATIN C
HETNAM MLT D-MALATE
HETNAM NA SODIUM ION
HETSYN MLT (2R)-2-HYDROXYBUTANEDIOIC ACID; 2-HYDROXY-SUCCINIC ACID
FORMUL 5 DY9 4(C18 H12 O6)
FORMUL 6 MLT 2(C4 H6 O5)
FORMUL 7 NA 3(NA 1+)
FORMUL 14 HOH *770(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 TYR A 260 1 12
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 LEU B 39 1 9
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 LEU C 39 1 9
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 LEU D 39 1 9
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 TYR D 260 1 12
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 HIS A 91 VAL A 95 -1 O ALA A 94 N VAL A 58
SHEET 4 AA1 8 PRO A 65 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 66 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 ALA B 295 N GLY B 271
SHEET 1 AA3 8 ARG C 44 VAL C 50 0
SHEET 2 AA3 8 VAL C 53 GLY C 61 -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 LEU C 160 N GLY C 135
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 ALA C 295 N GLY C 271
SHEET 1 AA4 8 ARG D 44 VAL D 50 0
SHEET 2 AA4 8 VAL D 53 GLY D 60 -1 O LEU D 55 N ALA D 48
SHEET 3 AA4 8 HIS D 91 VAL D 95 -1 O ALA D 94 N VAL D 58
SHEET 4 AA4 8 PRO D 65 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 LEU D 160 N GLY D 135
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 ALA D 295 N GLY D 271
LINK OE2 GLU C 197 NA NA C 401 1555 1555 2.79
LINK NA NA C 401 O HOH C 548 1555 1555 2.80
LINK OE2 GLU D 197 NA NA D 401 1555 1555 2.81
LINK NA NA D 401 O HOH D 553 1555 1555 2.88
CISPEP 1 TRP A 72 PRO A 73 0 -13.05
CISPEP 2 TRP B 72 PRO B 73 0 -14.05
CISPEP 3 TRP C 72 PRO C 73 0 -12.09
CISPEP 4 THR C 180 GLY C 181 0 -3.55
CISPEP 5 TRP D 72 PRO D 73 0 -13.15
SITE 1 AC1 15 TRP A 72 ASP A 137 MET A 141 THR A 162
SITE 2 AC1 15 TRP A 186 TRP A 187 LEU A 211 ASN A 214
SITE 3 AC1 15 PHE A 247 VAL A 299 HIS A 300 TYR A 301
SITE 4 AC1 15 HOH A 501 HOH A 508 HOH A 535
SITE 1 AC2 11 HIS A 201 GLY A 202 ASN A 235 PRO A 237
SITE 2 AC2 11 HOH A 539 HOH A 565 HOH A 650 HOH A 700
SITE 3 AC2 11 ARG C 205 GLN C 219 ARG C 227
SITE 1 AC3 3 ARG B 37 ARG B 44 SER B 45
SITE 1 AC4 17 TRP B 72 ASP B 137 MET B 141 THR B 162
SITE 2 AC4 17 TRP B 186 TRP B 187 LEU B 211 ASN B 214
SITE 3 AC4 17 PHE B 247 VAL B 299 HIS B 300 TYR B 301
SITE 4 AC4 17 HOH B 505 HOH B 514 HOH B 563 HOH B 632
SITE 5 AC4 17 HOH B 634
SITE 1 AC5 4 ALA C 194 PRO C 196 GLU C 197 HOH C 548
SITE 1 AC6 15 TRP C 72 ASP C 137 MET C 141 TRP C 186
SITE 2 AC6 15 TRP C 187 LEU C 211 ASN C 214 SER C 215
SITE 3 AC6 15 PHE C 247 VAL C 299 HIS C 300 TYR C 301
SITE 4 AC6 15 HOH C 502 HOH C 504 HOH C 517
SITE 1 AC7 4 ALA D 194 PRO D 196 GLU D 197 HOH D 553
SITE 1 AC8 15 TRP D 72 ASP D 137 MET D 141 THR D 162
SITE 2 AC8 15 TRP D 186 TRP D 187 LEU D 211 ASN D 214
SITE 3 AC8 15 PHE D 247 HIS D 300 TYR D 301 HOH D 506
SITE 4 AC8 15 HOH D 507 HOH D 520 HOH D 551
SITE 1 AC9 13 HIS B 201 GLY B 202 ASN B 235 PRO B 237
SITE 2 AC9 13 HOH B 510 HOH B 608 ARG D 205 GLN D 219
SITE 3 AC9 13 VAL D 222 GLY D 223 ASP D 224 ARG D 227
SITE 4 AC9 13 HOH D 557
CRYST1 97.477 101.562 117.481 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 0.010259 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009846 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008512 0.00000
TER 2296 GLY A 319
TER 4589 GLY B 319
TER 6853 GLY C 319
TER 9129 GLY D 319
MASTER 610 0 9 64 32 0 27 6 9996 4 176 108
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