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HEADER HYDROLASE 30-JAN-18 5Z7Y
TITLE CRYSTAL STRUCTURE OF STRIGA HERMONTHICA HTL7 (SHHTL7)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOSENSITIVE TO LIGHT 7;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: HYDROLASE, ALPHA/BETA FOLD FAMILY PROTEIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STRIGA HERMONTHICA;
SOURCE 3 ORGANISM_COMMON: PURPLE WITCHWEED;
SOURCE 4 ORGANISM_TAXID: 68872;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS HYDROLASE ACTIVITY, PUTATIVE RECEPTOR OF STRIGOLACTONE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.XU,T.MIYAKAWA,A.NAKAMURA,M.TANOKURA
REVDAT 1 29-AUG-18 5Z7Y 0
JRNL AUTH Y.XU,T.MIYAKAWA,S.NOSAKI,A.NAKAMURA,Y.LYU,H.NAKAMURA,U.OHTO,
JRNL AUTH 2 H.ISHIDA,T.SHIMIZU,T.ASAMI,M.TANOKURA
JRNL TITL COMPREHENSIVE STRUCTURAL STUDIES REVEAL EVOLUTION OF
JRNL TITL 2 STRIGOLACTONE/KARRIKIN SELECTIVITY OF HTL AND D14 PROTEINS
JRNL TITL 3 IN STRIGA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.62
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.010
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.8
REMARK 3 NUMBER OF REFLECTIONS : 72939
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.213
REMARK 3 R VALUE (WORKING SET) : 0.211
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.950
REMARK 3 FREE R VALUE TEST SET COUNT : 3608
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 43.6285 - 5.6236 0.96 2716 149 0.2063 0.2286
REMARK 3 2 5.6236 - 4.4650 0.93 2646 144 0.1816 0.2119
REMARK 3 3 4.4650 - 3.9010 0.94 2675 148 0.1688 0.2015
REMARK 3 4 3.9010 - 3.5445 0.94 2663 149 0.1722 0.2163
REMARK 3 5 3.5445 - 3.2906 0.94 2654 141 0.1872 0.2397
REMARK 3 6 3.2906 - 3.0966 0.95 2719 141 0.1991 0.2108
REMARK 3 7 3.0966 - 2.9416 0.96 2754 132 0.2118 0.2519
REMARK 3 8 2.9416 - 2.8135 0.96 2725 141 0.2060 0.2730
REMARK 3 9 2.8135 - 2.7052 0.95 2662 153 0.2063 0.2726
REMARK 3 10 2.7052 - 2.6119 0.95 2720 143 0.2138 0.2739
REMARK 3 11 2.6119 - 2.5302 0.95 2713 137 0.2170 0.2896
REMARK 3 12 2.5302 - 2.4579 0.96 2735 146 0.2229 0.2842
REMARK 3 13 2.4579 - 2.3932 0.95 2732 139 0.2246 0.2658
REMARK 3 14 2.3932 - 2.3348 0.96 2715 129 0.2190 0.2787
REMARK 3 15 2.3348 - 2.2818 0.95 2724 137 0.2234 0.2760
REMARK 3 16 2.2818 - 2.2332 0.95 2705 140 0.2359 0.2618
REMARK 3 17 2.2332 - 2.1885 0.95 2664 123 0.2314 0.2882
REMARK 3 18 2.1885 - 2.1472 0.95 2747 124 0.2394 0.3011
REMARK 3 19 2.1472 - 2.1089 0.95 2657 140 0.2485 0.3056
REMARK 3 20 2.1089 - 2.0731 0.95 2746 151 0.2530 0.2826
REMARK 3 21 2.0731 - 2.0397 0.96 2751 136 0.2521 0.3034
REMARK 3 22 2.0397 - 2.0083 0.95 2676 134 0.2720 0.2846
REMARK 3 23 2.0083 - 1.9788 0.95 2698 154 0.2781 0.3418
REMARK 3 24 1.9788 - 1.9509 0.94 2689 143 0.2932 0.3248
REMARK 3 25 1.9509 - 1.9245 0.85 2402 131 0.2996 0.3570
REMARK 3 26 1.9245 - 1.8996 0.72 2043 103 0.3005 0.3400
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) : 0.260
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.990
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.004 8549
REMARK 3 ANGLE : 0.663 11627
REMARK 3 CHIRALITY : 0.046 1341
REMARK 3 PLANARITY : 0.004 1481
REMARK 3 DIHEDRAL : 13.329 5125
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 5Z7Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-FEB-18.
REMARK 100 THE DEPOSITION ID IS D_1300006459.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-NOV-16
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-17A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9800
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
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 72978
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.8
REMARK 200 DATA REDUNDANCY : 2.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.01
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.200
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: 5Z7X
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 90MM TRIS-HCL (PH 8.5), 27% (W/V) PEG
REMARK 280 5000, 180MM MGCL2, 3.5% 1,4-DIOXANE, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11720 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 -1
REMARK 465 GLY A 0
REMARK 465 MET A 1
REMARK 465 THR A 269
REMARK 465 ASP A 270
REMARK 465 HIS A 271
REMARK 465 THR A 272
REMARK 465 ARG A 273
REMARK 465 HIS A 274
REMARK 465 HIS A 275
REMARK 465 HIS A 276
REMARK 465 HIS A 277
REMARK 465 HIS A 278
REMARK 465 HIS A 279
REMARK 465 MET B -1
REMARK 465 GLY B 0
REMARK 465 MET B 1
REMARK 465 THR B 269
REMARK 465 ASP B 270
REMARK 465 HIS B 271
REMARK 465 THR B 272
REMARK 465 ARG B 273
REMARK 465 HIS B 274
REMARK 465 HIS B 275
REMARK 465 HIS B 276
REMARK 465 HIS B 277
REMARK 465 HIS B 278
REMARK 465 HIS B 279
REMARK 465 MET C -1
REMARK 465 GLY C 0
REMARK 465 MET C 1
REMARK 465 HIS C 271
REMARK 465 THR C 272
REMARK 465 ARG C 273
REMARK 465 HIS C 274
REMARK 465 HIS C 275
REMARK 465 HIS C 276
REMARK 465 HIS C 277
REMARK 465 HIS C 278
REMARK 465 HIS C 279
REMARK 465 MET D -1
REMARK 465 GLY D 0
REMARK 465 MET D 1
REMARK 465 THR D 269
REMARK 465 ASP D 270
REMARK 465 HIS D 271
REMARK 465 THR D 272
REMARK 465 ARG D 273
REMARK 465 HIS D 274
REMARK 465 HIS D 275
REMARK 465 HIS D 276
REMARK 465 HIS D 277
REMARK 465 HIS D 278
REMARK 465 HIS D 279
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 SER A 95 -131.56 60.66
REMARK 500 ARG A 123 131.35 -171.45
REMARK 500 THR A 127 -161.59 -129.70
REMARK 500 LEU A 146 -78.88 -34.95
REMARK 500 SER B 95 -122.60 63.04
REMARK 500 THR B 127 -165.71 -129.22
REMARK 500 SER C 95 -125.12 55.93
REMARK 500 ARG C 123 132.39 -175.07
REMARK 500 LEU C 146 -65.83 11.40
REMARK 500 LEU C 247 64.53 -119.70
REMARK 500 SER D 95 -119.94 57.66
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 576 DISTANCE = 6.13 ANGSTROMS
REMARK 525 HOH A 577 DISTANCE = 6.35 ANGSTROMS
REMARK 525 HOH B 582 DISTANCE = 5.91 ANGSTROMS
REMARK 525 HOH B 583 DISTANCE = 6.24 ANGSTROMS
REMARK 525 HOH B 584 DISTANCE = 6.54 ANGSTROMS
REMARK 525 HOH C 574 DISTANCE = 6.11 ANGSTROMS
REMARK 525 HOH C 575 DISTANCE = 6.72 ANGSTROMS
REMARK 525 HOH C 576 DISTANCE = 7.97 ANGSTROMS
REMARK 525 HOH C 577 DISTANCE = 8.23 ANGSTROMS
REMARK 525 HOH D 573 DISTANCE = 6.11 ANGSTROMS
REMARK 525 HOH D 574 DISTANCE = 6.73 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C 417 O
REMARK 620 2 HOH C 556 O 62.4
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 DIO A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DIO D 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 303
DBREF1 5Z7Y A 1 271 UNP A0A0M3PNA2_STRHE
DBREF2 5Z7Y A A0A0M3PNA2 1 271
DBREF1 5Z7Y B 1 271 UNP A0A0M3PNA2_STRHE
DBREF2 5Z7Y B A0A0M3PNA2 1 271
DBREF1 5Z7Y C 1 271 UNP A0A0M3PNA2_STRHE
DBREF2 5Z7Y C A0A0M3PNA2 1 271
DBREF1 5Z7Y D 1 271 UNP A0A0M3PNA2_STRHE
DBREF2 5Z7Y D A0A0M3PNA2 1 271
SEQADV 5Z7Y MET A -1 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 5Z7Y GLY A 0 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 5Z7Y THR A 272 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 5Z7Y ARG A 273 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 5Z7Y HIS A 274 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 5Z7Y HIS A 275 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 5Z7Y HIS A 276 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 5Z7Y HIS A 277 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 5Z7Y HIS A 278 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 5Z7Y HIS A 279 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 5Z7Y MET B -1 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 5Z7Y GLY B 0 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 5Z7Y THR B 272 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 5Z7Y ARG B 273 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 5Z7Y HIS B 274 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 5Z7Y HIS B 275 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 5Z7Y HIS B 276 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 5Z7Y HIS B 277 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 5Z7Y HIS B 278 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 5Z7Y HIS B 279 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 5Z7Y MET C -1 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 5Z7Y GLY C 0 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 5Z7Y THR C 272 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 5Z7Y ARG C 273 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 5Z7Y HIS C 274 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 5Z7Y HIS C 275 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 5Z7Y HIS C 276 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 5Z7Y HIS C 277 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 5Z7Y HIS C 278 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 5Z7Y HIS C 279 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 5Z7Y MET D -1 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 5Z7Y GLY D 0 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 5Z7Y THR D 272 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 5Z7Y ARG D 273 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 5Z7Y HIS D 274 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 5Z7Y HIS D 275 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 5Z7Y HIS D 276 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 5Z7Y HIS D 277 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 5Z7Y HIS D 278 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 5Z7Y HIS D 279 UNP A0A0M3PNA EXPRESSION TAG
SEQRES 1 A 281 MET GLY MET SER SER ILE GLY LEU ALA HIS ASN VAL THR
SEQRES 2 A 281 ILE LEU GLY SER GLY GLU THR THR VAL VAL LEU GLY HIS
SEQRES 3 A 281 GLY TYR GLY THR ASP GLN SER VAL TRP LYS LEU LEU VAL
SEQRES 4 A 281 PRO TYR LEU VAL ASP ASP TYR LYS VAL LEU LEU TYR ASP
SEQRES 5 A 281 HIS MET GLY ALA GLY THR THR ASN PRO ASP TYR PHE ASP
SEQRES 6 A 281 PHE ASP ARG TYR SER SER LEU GLU GLY TYR SER TYR ASP
SEQRES 7 A 281 LEU ILE ALA ILE LEU GLU GLU PHE GLN VAL SER LYS CYS
SEQRES 8 A 281 ILE TYR VAL GLY HIS SER MET SER SER MET ALA ALA ALA
SEQRES 9 A 281 VAL ALA SER ILE PHE ARG PRO ASP LEU PHE HIS LYS LEU
SEQRES 10 A 281 VAL MET ILE SER PRO THR PRO ARG LEU ILE ASN THR GLU
SEQRES 11 A 281 GLU TYR TYR GLY GLY PHE GLU GLN LYS VAL MET ASP GLU
SEQRES 12 A 281 THR LEU ARG SER LEU ASP GLU ASN PHE LYS SER LEU SER
SEQRES 13 A 281 LEU GLY THR ALA PRO LEU LEU LEU ALA CYS ASP LEU GLU
SEQRES 14 A 281 SER ALA ALA MET GLN GLU TYR CYS ARG THR LEU PHE ASN
SEQRES 15 A 281 MET ARG PRO ASP ILE ALA CYS CYS ILE THR ARG MET ILE
SEQRES 16 A 281 CYS GLY LEU ASP LEU ARG PRO TYR LEU GLY HIS VAL THR
SEQRES 17 A 281 VAL PRO CYS HIS ILE ILE GLN SER SER ASN ASP ILE MET
SEQRES 18 A 281 VAL PRO VAL ALA VAL GLY GLU TYR LEU ARG LYS ASN LEU
SEQRES 19 A 281 GLY GLY PRO SER VAL VAL GLU VAL MET PRO THR GLU GLY
SEQRES 20 A 281 HIS LEU PRO HIS LEU SER MET PRO GLU VAL THR ILE PRO
SEQRES 21 A 281 VAL VAL LEU ARG HIS ILE ARG GLN ASP ILE THR ASP HIS
SEQRES 22 A 281 THR ARG HIS HIS HIS HIS HIS HIS
SEQRES 1 B 281 MET GLY MET SER SER ILE GLY LEU ALA HIS ASN VAL THR
SEQRES 2 B 281 ILE LEU GLY SER GLY GLU THR THR VAL VAL LEU GLY HIS
SEQRES 3 B 281 GLY TYR GLY THR ASP GLN SER VAL TRP LYS LEU LEU VAL
SEQRES 4 B 281 PRO TYR LEU VAL ASP ASP TYR LYS VAL LEU LEU TYR ASP
SEQRES 5 B 281 HIS MET GLY ALA GLY THR THR ASN PRO ASP TYR PHE ASP
SEQRES 6 B 281 PHE ASP ARG TYR SER SER LEU GLU GLY TYR SER TYR ASP
SEQRES 7 B 281 LEU ILE ALA ILE LEU GLU GLU PHE GLN VAL SER LYS CYS
SEQRES 8 B 281 ILE TYR VAL GLY HIS SER MET SER SER MET ALA ALA ALA
SEQRES 9 B 281 VAL ALA SER ILE PHE ARG PRO ASP LEU PHE HIS LYS LEU
SEQRES 10 B 281 VAL MET ILE SER PRO THR PRO ARG LEU ILE ASN THR GLU
SEQRES 11 B 281 GLU TYR TYR GLY GLY PHE GLU GLN LYS VAL MET ASP GLU
SEQRES 12 B 281 THR LEU ARG SER LEU ASP GLU ASN PHE LYS SER LEU SER
SEQRES 13 B 281 LEU GLY THR ALA PRO LEU LEU LEU ALA CYS ASP LEU GLU
SEQRES 14 B 281 SER ALA ALA MET GLN GLU TYR CYS ARG THR LEU PHE ASN
SEQRES 15 B 281 MET ARG PRO ASP ILE ALA CYS CYS ILE THR ARG MET ILE
SEQRES 16 B 281 CYS GLY LEU ASP LEU ARG PRO TYR LEU GLY HIS VAL THR
SEQRES 17 B 281 VAL PRO CYS HIS ILE ILE GLN SER SER ASN ASP ILE MET
SEQRES 18 B 281 VAL PRO VAL ALA VAL GLY GLU TYR LEU ARG LYS ASN LEU
SEQRES 19 B 281 GLY GLY PRO SER VAL VAL GLU VAL MET PRO THR GLU GLY
SEQRES 20 B 281 HIS LEU PRO HIS LEU SER MET PRO GLU VAL THR ILE PRO
SEQRES 21 B 281 VAL VAL LEU ARG HIS ILE ARG GLN ASP ILE THR ASP HIS
SEQRES 22 B 281 THR ARG HIS HIS HIS HIS HIS HIS
SEQRES 1 C 281 MET GLY MET SER SER ILE GLY LEU ALA HIS ASN VAL THR
SEQRES 2 C 281 ILE LEU GLY SER GLY GLU THR THR VAL VAL LEU GLY HIS
SEQRES 3 C 281 GLY TYR GLY THR ASP GLN SER VAL TRP LYS LEU LEU VAL
SEQRES 4 C 281 PRO TYR LEU VAL ASP ASP TYR LYS VAL LEU LEU TYR ASP
SEQRES 5 C 281 HIS MET GLY ALA GLY THR THR ASN PRO ASP TYR PHE ASP
SEQRES 6 C 281 PHE ASP ARG TYR SER SER LEU GLU GLY TYR SER TYR ASP
SEQRES 7 C 281 LEU ILE ALA ILE LEU GLU GLU PHE GLN VAL SER LYS CYS
SEQRES 8 C 281 ILE TYR VAL GLY HIS SER MET SER SER MET ALA ALA ALA
SEQRES 9 C 281 VAL ALA SER ILE PHE ARG PRO ASP LEU PHE HIS LYS LEU
SEQRES 10 C 281 VAL MET ILE SER PRO THR PRO ARG LEU ILE ASN THR GLU
SEQRES 11 C 281 GLU TYR TYR GLY GLY PHE GLU GLN LYS VAL MET ASP GLU
SEQRES 12 C 281 THR LEU ARG SER LEU ASP GLU ASN PHE LYS SER LEU SER
SEQRES 13 C 281 LEU GLY THR ALA PRO LEU LEU LEU ALA CYS ASP LEU GLU
SEQRES 14 C 281 SER ALA ALA MET GLN GLU TYR CYS ARG THR LEU PHE ASN
SEQRES 15 C 281 MET ARG PRO ASP ILE ALA CYS CYS ILE THR ARG MET ILE
SEQRES 16 C 281 CYS GLY LEU ASP LEU ARG PRO TYR LEU GLY HIS VAL THR
SEQRES 17 C 281 VAL PRO CYS HIS ILE ILE GLN SER SER ASN ASP ILE MET
SEQRES 18 C 281 VAL PRO VAL ALA VAL GLY GLU TYR LEU ARG LYS ASN LEU
SEQRES 19 C 281 GLY GLY PRO SER VAL VAL GLU VAL MET PRO THR GLU GLY
SEQRES 20 C 281 HIS LEU PRO HIS LEU SER MET PRO GLU VAL THR ILE PRO
SEQRES 21 C 281 VAL VAL LEU ARG HIS ILE ARG GLN ASP ILE THR ASP HIS
SEQRES 22 C 281 THR ARG HIS HIS HIS HIS HIS HIS
SEQRES 1 D 281 MET GLY MET SER SER ILE GLY LEU ALA HIS ASN VAL THR
SEQRES 2 D 281 ILE LEU GLY SER GLY GLU THR THR VAL VAL LEU GLY HIS
SEQRES 3 D 281 GLY TYR GLY THR ASP GLN SER VAL TRP LYS LEU LEU VAL
SEQRES 4 D 281 PRO TYR LEU VAL ASP ASP TYR LYS VAL LEU LEU TYR ASP
SEQRES 5 D 281 HIS MET GLY ALA GLY THR THR ASN PRO ASP TYR PHE ASP
SEQRES 6 D 281 PHE ASP ARG TYR SER SER LEU GLU GLY TYR SER TYR ASP
SEQRES 7 D 281 LEU ILE ALA ILE LEU GLU GLU PHE GLN VAL SER LYS CYS
SEQRES 8 D 281 ILE TYR VAL GLY HIS SER MET SER SER MET ALA ALA ALA
SEQRES 9 D 281 VAL ALA SER ILE PHE ARG PRO ASP LEU PHE HIS LYS LEU
SEQRES 10 D 281 VAL MET ILE SER PRO THR PRO ARG LEU ILE ASN THR GLU
SEQRES 11 D 281 GLU TYR TYR GLY GLY PHE GLU GLN LYS VAL MET ASP GLU
SEQRES 12 D 281 THR LEU ARG SER LEU ASP GLU ASN PHE LYS SER LEU SER
SEQRES 13 D 281 LEU GLY THR ALA PRO LEU LEU LEU ALA CYS ASP LEU GLU
SEQRES 14 D 281 SER ALA ALA MET GLN GLU TYR CYS ARG THR LEU PHE ASN
SEQRES 15 D 281 MET ARG PRO ASP ILE ALA CYS CYS ILE THR ARG MET ILE
SEQRES 16 D 281 CYS GLY LEU ASP LEU ARG PRO TYR LEU GLY HIS VAL THR
SEQRES 17 D 281 VAL PRO CYS HIS ILE ILE GLN SER SER ASN ASP ILE MET
SEQRES 18 D 281 VAL PRO VAL ALA VAL GLY GLU TYR LEU ARG LYS ASN LEU
SEQRES 19 D 281 GLY GLY PRO SER VAL VAL GLU VAL MET PRO THR GLU GLY
SEQRES 20 D 281 HIS LEU PRO HIS LEU SER MET PRO GLU VAL THR ILE PRO
SEQRES 21 D 281 VAL VAL LEU ARG HIS ILE ARG GLN ASP ILE THR ASP HIS
SEQRES 22 D 281 THR ARG HIS HIS HIS HIS HIS HIS
HET DIO A 301 6
HET MG A 302 1
HET MG A 303 1
HET MG B 301 1
HET MG C 301 1
HET EDO C 302 4
HET DIO D 301 6
HET MG D 302 1
HET EDO D 303 4
HETNAM DIO 1,4-DIETHYLENE DIOXIDE
HETNAM MG MAGNESIUM ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 5 DIO 2(C4 H8 O2)
FORMUL 6 MG 5(MG 2+)
FORMUL 10 EDO 2(C2 H6 O2)
FORMUL 14 HOH *712(H2 O)
HELIX 1 AA1 SER A 2 HIS A 8 1 7
HELIX 2 AA2 ASP A 29 LYS A 34 5 6
HELIX 3 AA3 LEU A 36 LEU A 40 5 5
HELIX 4 AA4 ASN A 58 PHE A 62 5 5
HELIX 5 AA5 ASP A 65 SER A 69 5 5
HELIX 6 AA6 LEU A 70 PHE A 84 1 15
HELIX 7 AA7 SER A 95 ARG A 108 1 14
HELIX 8 AA8 GLU A 135 ARG A 144 1 10
HELIX 9 AA9 ASN A 149 THR A 157 1 9
HELIX 10 AB1 THR A 157 ALA A 163 1 7
HELIX 11 AB2 SER A 168 PHE A 179 1 12
HELIX 12 AB3 ARG A 182 GLY A 195 1 14
HELIX 13 AB4 LEU A 198 VAL A 205 5 8
HELIX 14 AB5 PRO A 221 LEU A 232 1 12
HELIX 15 AB6 LEU A 247 MET A 252 1 6
HELIX 16 AB7 MET A 252 GLN A 266 1 15
HELIX 17 AB8 SER B 3 HIS B 8 1 6
HELIX 18 AB9 ASP B 29 LYS B 34 5 6
HELIX 19 AC1 LEU B 36 LEU B 40 5 5
HELIX 20 AC2 ASN B 58 PHE B 62 5 5
HELIX 21 AC3 ASP B 65 SER B 68 5 4
HELIX 22 AC4 SER B 69 PHE B 84 1 16
HELIX 23 AC5 SER B 95 ARG B 108 1 14
HELIX 24 AC6 GLU B 135 SER B 145 1 11
HELIX 25 AC7 ASN B 149 ALA B 163 1 15
HELIX 26 AC8 SER B 168 PHE B 179 1 12
HELIX 27 AC9 ARG B 182 GLY B 195 1 14
HELIX 28 AD1 LEU B 198 VAL B 205 5 8
HELIX 29 AD2 PRO B 221 LEU B 232 1 12
HELIX 30 AD3 LEU B 247 MET B 252 1 6
HELIX 31 AD4 MET B 252 GLN B 266 1 15
HELIX 32 AD5 SER C 3 HIS C 8 1 6
HELIX 33 AD6 ASP C 29 LYS C 34 5 6
HELIX 34 AD7 LEU C 36 LEU C 40 5 5
HELIX 35 AD8 ASN C 58 PHE C 62 5 5
HELIX 36 AD9 ASP C 65 SER C 68 5 4
HELIX 37 AE1 SER C 69 PHE C 84 1 16
HELIX 38 AE2 SER C 95 ARG C 108 1 14
HELIX 39 AE3 GLU C 135 LEU C 146 1 12
HELIX 40 AE4 ASN C 149 THR C 157 1 9
HELIX 41 AE5 THR C 157 ALA C 163 1 7
HELIX 42 AE6 SER C 168 PHE C 179 1 12
HELIX 43 AE7 ARG C 182 GLY C 195 1 14
HELIX 44 AE8 LEU C 198 VAL C 205 5 8
HELIX 45 AE9 PRO C 221 LEU C 232 1 12
HELIX 46 AF1 LEU C 247 MET C 252 1 6
HELIX 47 AF2 MET C 252 GLN C 266 1 15
HELIX 48 AF3 SER D 3 HIS D 8 1 6
HELIX 49 AF4 ASP D 29 LYS D 34 5 6
HELIX 50 AF5 LEU D 36 LEU D 40 5 5
HELIX 51 AF6 ASN D 58 PHE D 62 5 5
HELIX 52 AF7 SER D 69 PHE D 84 1 16
HELIX 53 AF8 SER D 95 ARG D 108 1 14
HELIX 54 AF9 GLU D 135 SER D 145 1 11
HELIX 55 AG1 SER D 145 ALA D 163 1 19
HELIX 56 AG2 SER D 168 PHE D 179 1 12
HELIX 57 AG3 ARG D 182 LEU D 196 1 15
HELIX 58 AG4 LEU D 198 VAL D 205 5 8
HELIX 59 AG5 PRO D 221 LEU D 232 1 12
HELIX 60 AG6 LEU D 247 MET D 252 1 6
HELIX 61 AG7 MET D 252 GLN D 266 1 15
SHEET 1 AA1 7 THR A 11 GLY A 14 0
SHEET 2 AA1 7 LYS A 45 LEU A 48 -1 O VAL A 46 N LEU A 13
SHEET 3 AA1 7 THR A 19 GLY A 23 1 N VAL A 20 O LEU A 47
SHEET 4 AA1 7 CYS A 89 HIS A 94 1 O VAL A 92 N VAL A 21
SHEET 5 AA1 7 PHE A 112 ILE A 118 1 O VAL A 116 N TYR A 91
SHEET 6 AA1 7 CYS A 209 ASN A 216 1 O HIS A 210 N MET A 117
SHEET 7 AA1 7 SER A 236 GLU A 244 1 O MET A 241 N GLN A 213
SHEET 1 AA2 7 THR B 11 GLY B 14 0
SHEET 2 AA2 7 LYS B 45 TYR B 49 -1 O LEU B 48 N THR B 11
SHEET 3 AA2 7 THR B 19 GLY B 23 1 N VAL B 20 O LYS B 45
SHEET 4 AA2 7 CYS B 89 HIS B 94 1 O VAL B 92 N GLY B 23
SHEET 5 AA2 7 PHE B 112 ILE B 118 1 O VAL B 116 N TYR B 91
SHEET 6 AA2 7 CYS B 209 ASN B 216 1 O HIS B 210 N MET B 117
SHEET 7 AA2 7 SER B 236 GLU B 244 1 O VAL B 237 N ILE B 211
SHEET 1 AA3 7 THR C 11 GLY C 14 0
SHEET 2 AA3 7 LYS C 45 LEU C 48 -1 O LEU C 48 N THR C 11
SHEET 3 AA3 7 THR C 19 GLY C 23 1 N VAL C 20 O LYS C 45
SHEET 4 AA3 7 CYS C 89 HIS C 94 1 O VAL C 92 N VAL C 21
SHEET 5 AA3 7 PHE C 112 ILE C 118 1 O VAL C 116 N TYR C 91
SHEET 6 AA3 7 CYS C 209 ASN C 216 1 O ILE C 212 N MET C 117
SHEET 7 AA3 7 SER C 236 GLU C 244 1 O VAL C 237 N ILE C 211
SHEET 1 AA4 7 THR D 11 GLY D 14 0
SHEET 2 AA4 7 LYS D 45 TYR D 49 -1 O VAL D 46 N LEU D 13
SHEET 3 AA4 7 THR D 19 GLY D 23 1 N VAL D 20 O LYS D 45
SHEET 4 AA4 7 CYS D 89 HIS D 94 1 O VAL D 92 N VAL D 21
SHEET 5 AA4 7 PHE D 112 ILE D 118 1 O VAL D 116 N TYR D 91
SHEET 6 AA4 7 CYS D 209 ASN D 216 1 O HIS D 210 N MET D 117
SHEET 7 AA4 7 SER D 236 GLU D 244 1 O VAL D 237 N ILE D 211
LINK OG SER A 95 MG MG A 302 1555 1555 2.76
LINK MG MG C 301 O HOH C 417 1555 1555 2.51
LINK MG MG C 301 O HOH C 556 1555 1555 2.58
LINK MG MG D 302 O HOH D 559 1555 1555 2.27
LINK MG MG A 303 O HOH D 544 1555 1544 2.10
SITE 1 AC1 6 GLY A 25 TYR A 26 TYR A 73 MET A 96
SITE 2 AC1 6 SER A 97 MG A 302
SITE 1 AC2 4 TYR A 26 SER A 95 MET A 96 DIO A 301
SITE 1 AC3 2 PRO D 242 HOH D 544
SITE 1 AC4 2 HOH C 417 HOH C 556
SITE 1 AC5 6 SER C 68 CYS C 188 ARG C 191 MET C 192
SITE 2 AC5 6 HOH C 423 HOH C 445
SITE 1 AC6 6 TYR A 39 ILE A 257 PRO A 258 TYR D 39
SITE 2 AC6 6 GLU D 254 PRO D 258
SITE 1 AC7 1 HOH D 559
SITE 1 AC8 2 TYR D 26 HOH D 412
CRYST1 46.086 72.609 81.122 97.69 95.39 107.07 P 1 4
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 0.021699 0.006664 0.003226 0.00000
SCALE2 0.000000 0.014407 0.002480 0.00000
SCALE3 0.000000 0.000000 0.012564 0.00000
TER 2080 ILE A 268
TER 4163 ILE B 268
TER 6258 ASP C 270
TER 8341 ILE D 268
MASTER 398 0 9 61 28 0 11 6 9068 4 27 88
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