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HEADER HYDROLASE 30-JAN-18 5Z82
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 5Z82 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. 1.69 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1_2575)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.69
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.09
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.110
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 60066
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 3013
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 35.0974 - 4.7442 1.00 2616 141 0.1663 0.1720
REMARK 3 2 4.7442 - 3.7670 1.00 2610 137 0.1488 0.1586
REMARK 3 3 3.7670 - 3.2912 1.00 2649 137 0.1652 0.1833
REMARK 3 4 3.2912 - 2.9905 1.00 2601 139 0.1773 0.2149
REMARK 3 5 2.9905 - 2.7763 1.00 2609 136 0.1876 0.2318
REMARK 3 6 2.7763 - 2.6126 1.00 2644 138 0.1886 0.2239
REMARK 3 7 2.6126 - 2.4818 1.00 2573 132 0.1897 0.2346
REMARK 3 8 2.4818 - 2.3738 1.00 2663 142 0.1790 0.1909
REMARK 3 9 2.3738 - 2.2824 1.00 2618 139 0.1825 0.2601
REMARK 3 10 2.2824 - 2.2037 1.00 2592 141 0.1924 0.2718
REMARK 3 11 2.2037 - 2.1348 1.00 2643 140 0.1946 0.2495
REMARK 3 12 2.1348 - 2.0738 1.00 2577 140 0.2139 0.2217
REMARK 3 13 2.0738 - 2.0192 1.00 2645 139 0.2177 0.3101
REMARK 3 14 2.0192 - 1.9699 1.00 2624 134 0.3052 0.3313
REMARK 3 15 1.9699 - 1.9252 1.00 2598 139 0.3364 0.3976
REMARK 3 16 1.9252 - 1.8842 1.00 2593 135 0.3385 0.3561
REMARK 3 17 1.8842 - 1.8465 1.00 2602 141 0.3365 0.3684
REMARK 3 18 1.8465 - 1.8117 1.00 2627 140 0.3749 0.3815
REMARK 3 19 1.8117 - 1.7793 1.00 2649 140 0.3892 0.4187
REMARK 3 20 1.7793 - 1.7491 1.00 2566 128 0.3932 0.4081
REMARK 3 21 1.7491 - 1.7209 1.00 2606 137 0.4030 0.3797
REMARK 3 22 1.7209 - 1.6945 0.81 2148 118 0.4597 0.4248
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.310
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.790
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 : 0.007 2141
REMARK 3 ANGLE : 0.791 2911
REMARK 3 CHIRALITY : 0.052 336
REMARK 3 PLANARITY : 0.005 370
REMARK 3 DIHEDRAL : 11.273 1282
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): 12.9771 24.5514 15.0055
REMARK 3 T TENSOR
REMARK 3 T11: 0.2741 T22: 0.2389
REMARK 3 T33: 0.2587 T12: 0.0036
REMARK 3 T13: -0.0067 T23: 0.0247
REMARK 3 L TENSOR
REMARK 3 L11: 3.2450 L22: 1.1573
REMARK 3 L33: 2.0782 L12: 0.1720
REMARK 3 L13: -0.2449 L23: -0.3754
REMARK 3 S TENSOR
REMARK 3 S11: -0.0230 S12: -0.1473 S13: 0.0215
REMARK 3 S21: 0.0858 S22: 0.0509 S23: 0.0659
REMARK 3 S31: -0.0039 S32: 0.0165 S33: -0.0348
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 5Z82 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-FEB-18.
REMARK 100 THE DEPOSITION ID IS D_1300006631.
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 : 8.5
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) : 0.97857
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 : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 60066
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.690
REMARK 200 RESOLUTION RANGE LOW (A) : 45.280
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 9.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.0500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
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 (%): 47.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, MAGNESIUM CHLORIDE, TRIS-HCL
REMARK 280 PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 36.99000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 42.02000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 45.27500
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 36.99000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 42.02000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 45.27500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 36.99000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 42.02000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 45.27500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 36.99000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 42.02000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 45.27500
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 455 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 522 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 600 LIES ON A SPECIAL POSITION.
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 -117.61 47.45
REMARK 500 ARG A 123 128.11 -173.17
REMARK 500 SER A 145 53.21 -114.13
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 610 DISTANCE = 6.99 ANGSTROMS
REMARK 525 HOH A 611 DISTANCE = 7.76 ANGSTROMS
REMARK 525 HOH A 612 DISTANCE = 8.31 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 301
DBREF1 5Z82 A 1 271 UNP A0A0M3PNA2_STRHE
DBREF2 5Z82 A A0A0M3PNA2 1 271
SEQADV 5Z82 GLY A -4 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 5Z82 PRO A -3 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 5Z82 LEU A -2 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 5Z82 GLY A -1 UNP A0A0M3PNA EXPRESSION TAG
SEQADV 5Z82 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 GOL A 301 14
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 GOL C3 H8 O3
FORMUL 3 HOH *212(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 LEU A 143 1 9
HELIX 9 AA9 SER A 145 ALA A 163 1 19
HELIX 10 AB1 SER A 168 MET A 181 1 14
HELIX 11 AB2 ARG A 182 GLY A 195 1 14
HELIX 12 AB3 LEU A 198 VAL A 205 5 8
HELIX 13 AB4 PRO A 221 LEU A 232 1 12
HELIX 14 AB5 LEU A 247 MET A 252 1 6
HELIX 15 AB6 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 GLY A 23
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 LEU A 115
SHEET 7 AA1 7 SER A 236 GLU A 244 1 O MET A 241 N GLN A 213
SITE 1 AC1 7 ASP A 60 TYR A 130 TYR A 131 ALA A 223
SITE 2 AC1 7 TYR A 227 HOH A 413 HOH A 515
CRYST1 73.980 84.040 90.550 90.00 90.00 90.00 I 2 2 2 8
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 0.013517 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011899 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011044 0.00000
TER 2089 ASP A 270
MASTER 304 0 1 15 7 0 2 6 2306 1 14 22
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