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HEADER HYDROLASE 30-JAN-18 5Z7Z
TITLE CRYSTAL STRUCTURE OF STRIGA HERMONTHICA DWARF14 (SHD14)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DWARF 14;
COMPND 3 CHAIN: A, B;
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 5Z7Z 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. 1.98 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) : 1.98
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.31
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 36501
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.210
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.860
REMARK 3 FREE R VALUE TEST SET COUNT : 1775
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 38.3203 - 4.6484 0.97 2679 139 0.1797 0.2203
REMARK 3 2 4.6484 - 3.6905 0.99 2688 145 0.1676 0.2425
REMARK 3 3 3.6905 - 3.2243 1.00 2654 160 0.1841 0.2162
REMARK 3 4 3.2243 - 2.9296 1.00 2677 142 0.2095 0.2426
REMARK 3 5 2.9296 - 2.7197 1.00 2725 101 0.2163 0.2854
REMARK 3 6 2.7197 - 2.5594 1.00 2660 142 0.2273 0.2571
REMARK 3 7 2.5594 - 2.4312 1.00 2668 140 0.2254 0.2718
REMARK 3 8 2.4312 - 2.3254 1.00 2654 150 0.2341 0.3061
REMARK 3 9 2.3254 - 2.2359 1.00 2642 130 0.2508 0.2814
REMARK 3 10 2.2359 - 2.1588 1.00 2711 103 0.2543 0.3020
REMARK 3 11 2.1588 - 2.0913 1.00 2683 141 0.2575 0.2793
REMARK 3 12 2.0913 - 2.0315 1.00 2617 139 0.2823 0.3137
REMARK 3 13 2.0315 - 1.9780 1.00 2668 143 0.3085 0.3827
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) : 0.270
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.720
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 4243
REMARK 3 ANGLE : 0.648 5753
REMARK 3 CHIRALITY : 0.043 660
REMARK 3 PLANARITY : 0.004 742
REMARK 3 DIHEDRAL : 12.901 2519
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 5Z7Z 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_1300006460.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-OCT-15
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : 10.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NW12A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36505
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.978
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 (%) : 99.6
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.98
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.000
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: 3VXK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM CAPS (PH 10.0), 200MM NACL, 20%
REMARK 280 (W/V) PEG 8000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 35.15800
REMARK 290 SMTRY3 2 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: 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: 10730 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: 11190 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 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 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 GLY A -8
REMARK 465 PRO A -7
REMARK 465 GLY A -6
REMARK 465 TYR A -5
REMARK 465 GLN A -4
REMARK 465 ASP A -3
REMARK 465 PRO A -2
REMARK 465 ASN A -1
REMARK 465 ARG A 266
REMARK 465 GLY B -8
REMARK 465 PRO B -7
REMARK 465 GLY B -6
REMARK 465 TYR B -5
REMARK 465 GLN B -4
REMARK 465 ARG B 266
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 THR A 29 -169.71 -129.31
REMARK 500 TYR A 68 46.05 -79.94
REMARK 500 SER A 96 -112.64 53.10
REMARK 500 ARG A 124 122.00 -172.28
REMARK 500 LYS A 129 106.06 -56.45
REMARK 500 ASN A 130 8.25 54.97
REMARK 500 SER A 215 -71.26 -61.94
REMARK 500 LYS A 216 71.96 -116.81
REMARK 500 THR B 29 -169.97 -116.29
REMARK 500 THR B 29 -167.52 -127.17
REMARK 500 PHE B 41 -17.20 -150.84
REMARK 500 TYR B 68 48.62 -82.03
REMARK 500 SER B 96 -114.65 49.87
REMARK 500 ARG B 124 121.82 -172.94
REMARK 500 SER B 215 -79.59 -68.70
REMARK 500 LYS B 216 68.56 -105.00
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 627 DISTANCE = 5.87 ANGSTROMS
REMARK 525 HOH B 631 DISTANCE = 5.86 ANGSTROMS
REMARK 525 HOH B 632 DISTANCE = 6.46 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 305
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUE 202 IS LEU ACCORDING TO THE SEQUENCE OF GENBANK ALB07155.1.
DBREF1 5Z7Z A 4 266 UNP A0A0M5I7R9_STRHE
DBREF2 5Z7Z A A0A0M5I7R9 4 266
DBREF1 5Z7Z B 4 266 UNP A0A0M5I7R9_STRHE
DBREF2 5Z7Z B A0A0M5I7R9 4 266
SEQADV 5Z7Z GLY A -8 UNP A0A0M5I7R EXPRESSION TAG
SEQADV 5Z7Z PRO A -7 UNP A0A0M5I7R EXPRESSION TAG
SEQADV 5Z7Z GLY A -6 UNP A0A0M5I7R EXPRESSION TAG
SEQADV 5Z7Z TYR A -5 UNP A0A0M5I7R EXPRESSION TAG
SEQADV 5Z7Z GLN A -4 UNP A0A0M5I7R EXPRESSION TAG
SEQADV 5Z7Z ASP A -3 UNP A0A0M5I7R EXPRESSION TAG
SEQADV 5Z7Z PRO A -2 UNP A0A0M5I7R EXPRESSION TAG
SEQADV 5Z7Z ASN A -1 UNP A0A0M5I7R EXPRESSION TAG
SEQADV 5Z7Z SER A 0 UNP A0A0M5I7R EXPRESSION TAG
SEQADV 5Z7Z LEU A 202 UNP A0A0M5I7R VAL 202 SEE SEQUENCE DETAILS
SEQADV 5Z7Z GLY B -8 UNP A0A0M5I7R EXPRESSION TAG
SEQADV 5Z7Z PRO B -7 UNP A0A0M5I7R EXPRESSION TAG
SEQADV 5Z7Z GLY B -6 UNP A0A0M5I7R EXPRESSION TAG
SEQADV 5Z7Z TYR B -5 UNP A0A0M5I7R EXPRESSION TAG
SEQADV 5Z7Z GLN B -4 UNP A0A0M5I7R EXPRESSION TAG
SEQADV 5Z7Z ASP B -3 UNP A0A0M5I7R EXPRESSION TAG
SEQADV 5Z7Z PRO B -2 UNP A0A0M5I7R EXPRESSION TAG
SEQADV 5Z7Z ASN B -1 UNP A0A0M5I7R EXPRESSION TAG
SEQADV 5Z7Z SER B 0 UNP A0A0M5I7R EXPRESSION TAG
SEQADV 5Z7Z LEU B 202 UNP A0A0M5I7R VAL 202 SEE SEQUENCE DETAILS
SEQRES 1 A 272 GLY PRO GLY TYR GLN ASP PRO ASN SER SER LEU LEU GLU
SEQRES 2 A 272 ALA LEU ASN VAL ARG VAL VAL GLY SER GLY GLU LYS VAL
SEQRES 3 A 272 LEU VAL LEU ALA HIS GLY VAL GLY THR ASP GLN SER ALA
SEQRES 4 A 272 TRP GLN ARG ILE LEU PRO TYR PHE VAL ARG ASP HIS ARG
SEQRES 5 A 272 VAL VAL LEU TYR ASP LEU VAL CYS ALA GLY SER VAL ASN
SEQRES 6 A 272 PRO ASP TYR PHE ASP PHE ARG ARG TYR THR SER LEU ASP
SEQRES 7 A 272 ALA PHE VAL ASP ASP LEU LEU ALA ILE LEU ASP ALA LEU
SEQRES 8 A 272 ARG LEU GLY ARG CYS THR TYR VAL GLY HIS SER VAL SER
SEQRES 9 A 272 ALA SER ILE GLY ILE LEU ALA SER ILE ARG ARG PRO ASP
SEQRES 10 A 272 LEU PHE ALA LYS LEU ILE LEU ILE GLY ALA SER PRO ARG
SEQRES 11 A 272 PHE LEU ASN ASP LYS ASN TYR HIS GLY GLY PHE ALA ASP
SEQRES 12 A 272 GLY GLU ILE ASP THR VAL PHE ALA ALA MET GLU ALA ASN
SEQRES 13 A 272 TYR ALA ALA TRP VAL SER GLY PHE ALA PRO LEU ALA VAL
SEQRES 14 A 272 GLY ALA ASP VAL PRO GLU ALA VAL ARG GLU PHE SER ARG
SEQRES 15 A 272 THR LEU PHE ASN MET ARG PRO ASP ILE THR LEU PHE VAL
SEQRES 16 A 272 SER ARG MET VAL PHE ASN SER ASP LEU ARG GLY VAL LEU
SEQRES 17 A 272 GLY LEU VAL THR VAL PRO CYS SER VAL LEU GLN THR SER
SEQRES 18 A 272 LYS ASP HIS SER VAL PRO GLU SER MET ALA ALA TYR LEU
SEQRES 19 A 272 LYS GLU ASN LEU GLY GLY ARG THR THR VAL HIS MET LEU
SEQRES 20 A 272 ASP ILE GLU GLY HIS LEU PRO HIS LEU SER ALA PRO ASN
SEQRES 21 A 272 LEU LEU ALA GLN GLU LEU ARG ARG ALA LEU PRO ARG
SEQRES 1 B 272 GLY PRO GLY TYR GLN ASP PRO ASN SER SER LEU LEU GLU
SEQRES 2 B 272 ALA LEU ASN VAL ARG VAL VAL GLY SER GLY GLU LYS VAL
SEQRES 3 B 272 LEU VAL LEU ALA HIS GLY VAL GLY THR ASP GLN SER ALA
SEQRES 4 B 272 TRP GLN ARG ILE LEU PRO TYR PHE VAL ARG ASP HIS ARG
SEQRES 5 B 272 VAL VAL LEU TYR ASP LEU VAL CYS ALA GLY SER VAL ASN
SEQRES 6 B 272 PRO ASP TYR PHE ASP PHE ARG ARG TYR THR SER LEU ASP
SEQRES 7 B 272 ALA PHE VAL ASP ASP LEU LEU ALA ILE LEU ASP ALA LEU
SEQRES 8 B 272 ARG LEU GLY ARG CYS THR TYR VAL GLY HIS SER VAL SER
SEQRES 9 B 272 ALA SER ILE GLY ILE LEU ALA SER ILE ARG ARG PRO ASP
SEQRES 10 B 272 LEU PHE ALA LYS LEU ILE LEU ILE GLY ALA SER PRO ARG
SEQRES 11 B 272 PHE LEU ASN ASP LYS ASN TYR HIS GLY GLY PHE ALA ASP
SEQRES 12 B 272 GLY GLU ILE ASP THR VAL PHE ALA ALA MET GLU ALA ASN
SEQRES 13 B 272 TYR ALA ALA TRP VAL SER GLY PHE ALA PRO LEU ALA VAL
SEQRES 14 B 272 GLY ALA ASP VAL PRO GLU ALA VAL ARG GLU PHE SER ARG
SEQRES 15 B 272 THR LEU PHE ASN MET ARG PRO ASP ILE THR LEU PHE VAL
SEQRES 16 B 272 SER ARG MET VAL PHE ASN SER ASP LEU ARG GLY VAL LEU
SEQRES 17 B 272 GLY LEU VAL THR VAL PRO CYS SER VAL LEU GLN THR SER
SEQRES 18 B 272 LYS ASP HIS SER VAL PRO GLU SER MET ALA ALA TYR LEU
SEQRES 19 B 272 LYS GLU ASN LEU GLY GLY ARG THR THR VAL HIS MET LEU
SEQRES 20 B 272 ASP ILE GLU GLY HIS LEU PRO HIS LEU SER ALA PRO ASN
SEQRES 21 B 272 LEU LEU ALA GLN GLU LEU ARG ARG ALA LEU PRO ARG
HET PEG A 301 7
HET PEG A 302 7
HET GOL A 303 6
HET EDO A 304 4
HET EDO A 305 4
HET PEG B 301 7
HET PEG B 302 7
HET GOL B 303 6
HET EDO B 304 4
HET EDO B 305 4
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM GOL GLYCEROL
HETNAM EDO 1,2-ETHANEDIOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 PEG 4(C4 H10 O3)
FORMUL 5 GOL 2(C3 H8 O3)
FORMUL 6 EDO 4(C2 H6 O2)
FORMUL 13 HOH *459(H2 O)
HELIX 1 AA1 ASP A 30 GLN A 35 5 6
HELIX 2 AA2 ILE A 37 PHE A 41 5 5
HELIX 3 AA3 ASN A 59 PHE A 63 5 5
HELIX 4 AA4 SER A 70 ARG A 86 1 17
HELIX 5 AA5 SER A 96 ARG A 109 1 14
HELIX 6 AA6 GLY A 138 ASN A 150 1 13
HELIX 7 AA7 ASN A 150 GLY A 164 1 15
HELIX 8 AA8 VAL A 167 MET A 181 1 15
HELIX 9 AA9 ARG A 182 SER A 196 1 15
HELIX 10 AB1 LEU A 198 GLY A 203 1 6
HELIX 11 AB2 GLU A 222 LEU A 232 1 11
HELIX 12 AB3 LEU A 247 ALA A 252 1 6
HELIX 13 AB4 ALA A 252 LEU A 264 1 13
HELIX 14 AB5 PRO B -2 LEU B 9 1 9
HELIX 15 AB6 ASP B 30 GLN B 35 5 6
HELIX 16 AB7 ILE B 37 PHE B 41 5 5
HELIX 17 AB8 ASN B 59 PHE B 63 5 5
HELIX 18 AB9 SER B 70 ARG B 86 1 17
HELIX 19 AC1 SER B 96 ARG B 109 1 14
HELIX 20 AC2 GLY B 138 ASN B 150 1 13
HELIX 21 AC3 ASN B 150 GLY B 164 1 15
HELIX 22 AC4 VAL B 167 MET B 181 1 15
HELIX 23 AC5 ARG B 182 ASN B 195 1 14
HELIX 24 AC6 LEU B 198 VAL B 205 5 8
HELIX 25 AC7 GLU B 222 LEU B 232 1 11
HELIX 26 AC8 LEU B 247 ALA B 252 1 6
HELIX 27 AC9 ALA B 252 LEU B 264 1 13
SHEET 1 AA1 7 ARG A 12 VAL A 14 0
SHEET 2 AA1 7 ARG A 46 LEU A 49 -1 O VAL A 47 N VAL A 14
SHEET 3 AA1 7 VAL A 20 ALA A 24 1 N LEU A 21 O VAL A 48
SHEET 4 AA1 7 CYS A 90 HIS A 95 1 O VAL A 93 N VAL A 22
SHEET 5 AA1 7 PHE A 113 ILE A 119 1 O ILE A 117 N TYR A 92
SHEET 6 AA1 7 CYS A 209 GLN A 213 1 O SER A 210 N LEU A 118
SHEET 7 AA1 7 THR A 236 MET A 240 1 O THR A 237 N VAL A 211
SHEET 1 AA2 7 ARG B 12 GLY B 15 0
SHEET 2 AA2 7 ARG B 46 LEU B 49 -1 O VAL B 47 N VAL B 14
SHEET 3 AA2 7 VAL B 20 ALA B 24 1 N LEU B 21 O VAL B 48
SHEET 4 AA2 7 CYS B 90 HIS B 95 1 O THR B 91 N VAL B 20
SHEET 5 AA2 7 PHE B 113 ILE B 119 1 O ILE B 117 N TYR B 92
SHEET 6 AA2 7 CYS B 209 GLN B 213 1 O SER B 210 N LEU B 118
SHEET 7 AA2 7 THR B 236 MET B 240 1 O HIS B 239 N VAL B 211
SITE 1 AC1 5 GLN A 35 ARG A 172 GLU A 173 HOH A 448
SITE 2 AC1 5 ARG B 182
SITE 1 AC2 6 ILE A 140 VAL A 143 PHE A 158 SER A 190
SITE 2 AC2 6 HOH A 416 HOH A 462
SITE 1 AC3 4 LYS A 229 GLU A 230 HOH A 488 HOH A 528
SITE 1 AC4 5 THR A 69 MET A 192 ASN A 195 HOH A 413
SITE 2 AC4 5 HOH A 452
SITE 1 AC5 5 SER A 223 TYR A 227 GLU A 230 HOH A 428
SITE 2 AC5 5 HOH A 486
SITE 1 AC6 6 GLU B 148 PRO B 183 ASP B 184 LEU B 187
SITE 2 AC6 6 PHE B 188 HOH B 539
SITE 1 AC7 4 ARG A 176 GLY B 56 ASN B 180 HOH B 425
SITE 1 AC8 3 PRO B 110 ASP B 111 HOH B 416
SITE 1 AC9 3 ASP B 72 ARG B 108 HOH B 498
SITE 1 AD1 2 ALA B 226 GLU B 230
CRYST1 44.662 70.316 84.684 90.00 94.03 90.00 P 1 21 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 0.022390 0.000000 0.001576 0.00000
SCALE2 0.000000 0.014222 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011838 0.00000
TER 2046 PRO A 265
TER 4107 PRO B 265
MASTER 323 0 10 27 14 0 15 6 4598 2 56 42
END |