| content |
HEADER HYDROLASE 02-FEB-18 5Z95
TITLE STRUCTURAL BASIS FOR SPECIFIC INHIBITION OF HIGHLY SENSITIVE SHHTL7
TITLE 2 RECEPTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOSENSITIVE TO LIGHT 7;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SHHTL7;
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;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS STRIGOLACTONE RECEPTOR, HYDROLASE, STRIGA GERMINATION SIGNALING
EXPDTA X-RAY DIFFRACTION
AUTHOR U.S.HAMEED,S.T.AROLD
REVDAT 1 25-JUL-18 5Z95 0
JRNL AUTH U.S.HAMEED,I.HAIDER,M.JAMIL,B.A.KOUNTCHE,X.GUO,R.A.ZARBAN,
JRNL AUTH 2 D.KIM,S.AL-BABILI,S.T.AROLD
JRNL TITL STRUCTURAL BASIS FOR SPECIFIC INHIBITION OF THE HIGHLY
JRNL TITL 2 SENSITIVE SHHTL7 RECEPTOR
JRNL REF EMBO REP. V. 19 45619 2018
JRNL REFN ISSN 1469-221X
REMARK 2
REMARK 2 RESOLUTION. 1.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0189
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 80.19
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 115730
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.130
REMARK 3 R VALUE (WORKING SET) : 0.129
REMARK 3 FREE R VALUE : 0.143
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6091
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.23
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8365
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.63
REMARK 3 BIN R VALUE (WORKING SET) : 0.3350
REMARK 3 BIN FREE R VALUE SET COUNT : 440
REMARK 3 BIN FREE R VALUE : 0.3520
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2088
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 47
REMARK 3 SOLVENT ATOMS : 289
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.17000
REMARK 3 B22 (A**2) : -0.17000
REMARK 3 B33 (A**2) : 0.54000
REMARK 3 B12 (A**2) : -0.08000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.028
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.028
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.020
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.016
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.983
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.978
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2692 ; 0.013 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2469 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3724 ; 1.685 ; 1.990
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5787 ; 1.040 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 374 ; 6.188 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 103 ;34.173 ;24.078
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 465 ;12.990 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;18.183 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 417 ; 0.107 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3180 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 537 ; 0.003 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1361 ; 1.016 ; 1.335
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1360 ; 1.007 ; 1.333
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1780 ; 1.441 ; 2.012
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1781 ; 1.442 ; 2.014
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1331 ; 1.961 ; 1.721
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1331 ; 1.961 ; 1.721
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1945 ; 2.565 ; 2.464
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 3190 ; 3.090 ;18.271
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 3120 ; 2.709 ;17.559
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 5158 ; 2.011 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 183 ;25.909 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 5171 ;10.768 ; 5.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.00
REMARK 3 ION PROBE RADIUS : 0.70
REMARK 3 SHRINKAGE RADIUS : 0.70
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5Z95 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-FEB-18.
REMARK 100 THE DEPOSITION ID IS D_1300006672.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-JAN-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9789
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 115730
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.200
REMARK 200 RESOLUTION RANGE LOW (A) : 80.190
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 9.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 24.5600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.24
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: MOLREP
REMARK 200 STARTING MODEL: 5CBK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 M LITHIUM SULFATE, 0.1 M HEPES PH
REMARK 280 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 53.50667
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 26.75333
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 40.13000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 13.37667
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 66.88333
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 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 -4
REMARK 465 PRO A -3
REMARK 465 LEU A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 HIS A 271
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 -106.35 29.42
REMARK 500 SER A 95 -112.27 59.52
REMARK 500 ARG A 123 144.18 -175.10
REMARK 500 ASP A 197 89.73 -150.10
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 688 DISTANCE = 6.56 ANGSTROMS
REMARK 525 HOH A 689 DISTANCE = 6.82 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 EGC A 301
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EGC A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 304
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5Z82 RELATED DB: PDB
REMARK 900 RELATED ID: 5Z89 RELATED DB: PDB
REMARK 900 RELATED ID: 5Z8P RELATED DB: PDB
DBREF1 5Z95 A 1 271 UNP A0A0M3PNA2_STRHE
DBREF2 5Z95 A A0A0M3PNA2 1 271
SEQADV 5Z95 GLY A -4 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 5Z95 PRO A -3 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 5Z95 LEU A -2 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 5Z95 GLY A -1 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 5Z95 SER A 0 UNP A0A0M3PNA EXPRESSION TAG
SEQRES 1 A 276 GLY PRO LEU GLY SER MET SER SER ILE GLY LEU ALA HIS
SEQRES 2 A 276 ASN VAL THR ILE LEU GLY SER GLY GLU THR THR VAL VAL
SEQRES 3 A 276 LEU GLY HIS GLY TYR GLY THR ASP GLN SER VAL TRP LYS
SEQRES 4 A 276 LEU LEU VAL PRO TYR LEU VAL ASP ASP TYR LYS VAL LEU
SEQRES 5 A 276 LEU TYR ASP HIS MET GLY ALA GLY THR THR ASN PRO ASP
SEQRES 6 A 276 TYR PHE ASP PHE ASP ARG TYR SER SER LEU GLU GLY TYR
SEQRES 7 A 276 SER TYR ASP LEU ILE ALA ILE LEU GLU GLU PHE GLN VAL
SEQRES 8 A 276 SER LYS CYS ILE TYR VAL GLY HIS SER MET SER SER MET
SEQRES 9 A 276 ALA ALA ALA VAL ALA SER ILE PHE ARG PRO ASP LEU PHE
SEQRES 10 A 276 HIS LYS LEU VAL MET ILE SER PRO THR PRO ARG LEU ILE
SEQRES 11 A 276 ASN THR GLU GLU TYR TYR GLY GLY PHE GLU GLN LYS VAL
SEQRES 12 A 276 MET ASP GLU THR LEU ARG SER LEU ASP GLU ASN PHE LYS
SEQRES 13 A 276 SER LEU SER LEU GLY THR ALA PRO LEU LEU LEU ALA CYS
SEQRES 14 A 276 ASP LEU GLU SER ALA ALA MET GLN GLU TYR CYS ARG THR
SEQRES 15 A 276 LEU PHE ASN MET ARG PRO ASP ILE ALA CYS CYS ILE THR
SEQRES 16 A 276 ARG MET ILE CYS GLY LEU ASP LEU ARG PRO TYR LEU GLY
SEQRES 17 A 276 HIS VAL THR VAL PRO CYS HIS ILE ILE GLN SER SER ASN
SEQRES 18 A 276 ASP ILE MET VAL PRO VAL ALA VAL GLY GLU TYR LEU ARG
SEQRES 19 A 276 LYS ASN LEU GLY GLY PRO SER VAL VAL GLU VAL MET PRO
SEQRES 20 A 276 THR GLU GLY HIS LEU PRO HIS LEU SER MET PRO GLU VAL
SEQRES 21 A 276 THR ILE PRO VAL VAL LEU ARG HIS ILE ARG GLN ASP ILE
SEQRES 22 A 276 THR ASP HIS
HET EGC A 301 31
HET SO4 A 302 5
HET SO4 A 303 5
HET GOL A 304 6
HETNAM EGC 2-(2-{2-[2-(2-{2-[2-(2-{2-[4-(1,1,3,3-TETRAMETHYL-
HETNAM 2 EGC BUTYL)-PHENOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-
HETNAM 3 EGC ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHANOL
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETSYN EGC TRITON X-100
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 EGC C32 H58 O10
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 5 GOL C3 H8 O3
FORMUL 6 HOH *289(H2 O)
HELIX 1 AA1 SER A 3 HIS A 8 1 6
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 SER A 145 1 11
HELIX 9 AA9 LEU A 146 GLU A 148 5 3
HELIX 10 AB1 ASN A 149 ALA A 163 1 15
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 VAL A 222 LEU A 232 1 11
HELIX 15 AB6 LEU A 247 MET A 252 1 6
HELIX 16 AB7 MET A 252 GLN A 266 1 15
SHEET 1 AA1 7 THR A 11 GLY A 14 0
SHEET 2 AA1 7 LYS A 45 TYR A 49 -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 LYS A 45
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 VAL A 237 N ILE A 211
SITE 1 AC1 13 ILE A 106 PHE A 107 PRO A 109 PHE A 134
SITE 2 AC1 13 VAL A 138 THR A 142 THR A 157 LEU A 160
SITE 3 AC1 13 THR A 190 MET A 219 HOH A 402 HOH A 535
SITE 4 AC1 13 HOH A 637
SITE 1 AC2 6 SER A 15 GLY A 16 LYS A 45 ARG A 229
SITE 2 AC2 6 LYS A 230 HOH A 521
SITE 1 AC3 3 THR A 127 ARG A 199 HOH A 606
SITE 1 AC4 6 TYR A 130 TYR A 131 TYR A 227 HOH A 426
SITE 2 AC4 6 HOH A 457 HOH A 516
CRYST1 92.590 92.590 80.260 90.00 90.00 120.00 P 65 6
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 0.010800 0.006236 0.000000 0.00000
SCALE2 0.000000 0.012471 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012460 0.00000
TER 2553 ASP A 270
MASTER 321 0 4 16 7 0 9 6 2424 1 47 22
END |