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HEADER SIGNALING PROTEIN 01-JUL-15 5CBK
TITLE CRYSTAL STRUCTURE OF THE STRIGOLACTONE RECEPTOR SHHTL5 FROM STRIGA
TITLE 2 HERMONTHICA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SHHTL5;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STRIGA HERMONTHICA;
SOURCE 3 ORGANISM_TAXID: 68872;
SOURCE 4 GENE: SHHTL5;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: P15TV LIC
KEYWDS STRIGA HERMONTHICA, STRIGOLACTONE, SIGNALLING, RECEPTOR, SHHTL5,
KEYWDS 2 ALPHA/BETA HYDROLASE, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR P.J.STOGIOS,O.ONOPRIYENKO,V.YIM,A.SAVCHENKO
REVDAT 1 21-OCT-15 5CBK 0
JRNL AUTH S.TOH,D.HOLBROOK-SMITH,P.J.STOGIOS,O.ONOPRIYENKO,S.LUMBA,
JRNL AUTH 2 Y.TSUCHIYA,A.SAVCHENKO,P.MCCOURT
JRNL TITL STRUCTURE-FUNCTION ANALYSIS IDENTIFIES HIGHLY SENSITIVE
JRNL TITL 2 STRIGOLACTONE RECEPTORS IN STRIGA.
JRNL REF SCIENCE V. 350 203 2015
JRNL REFN ESSN 1095-9203
JRNL PMID 26450211
JRNL DOI 10.1126/SCIENCE.AAC9476
REMARK 2
REMARK 2 RESOLUTION. 2.46 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 2.46
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.53
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 11812
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 589
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 29.5284 - 3.9066 1.00 2960 155 0.1470 0.1846
REMARK 3 2 3.9066 - 3.1019 0.99 2776 146 0.1688 0.2453
REMARK 3 3 3.1019 - 2.7101 1.00 2763 144 0.1965 0.2687
REMARK 3 4 2.7101 - 2.4625 0.99 2724 144 0.2068 0.2548
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) : 0.260
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.840
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 : 0.003 2212
REMARK 3 ANGLE : 0.754 2997
REMARK 3 CHIRALITY : 0.026 336
REMARK 3 PLANARITY : 0.003 390
REMARK 3 DIHEDRAL : 14.069 817
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND RESI 1:103
REMARK 3 ORIGIN FOR THE GROUP (A): -6.9554 43.5273 -3.5019
REMARK 3 T TENSOR
REMARK 3 T11: 0.2533 T22: 0.2804
REMARK 3 T33: 0.3420 T12: -0.0851
REMARK 3 T13: -0.0485 T23: 0.0655
REMARK 3 L TENSOR
REMARK 3 L11: 2.3292 L22: 1.9084
REMARK 3 L33: 3.5369 L12: -0.5897
REMARK 3 L13: -0.2085 L23: 0.1330
REMARK 3 S TENSOR
REMARK 3 S11: -0.0880 S12: 0.1238 S13: 0.2523
REMARK 3 S21: -0.1021 S22: -0.0897 S23: -0.2203
REMARK 3 S31: -0.2821 S32: 0.4227 S33: 0.1167
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND RESI 104:146
REMARK 3 ORIGIN FOR THE GROUP (A): -7.1038 25.4633 -1.1774
REMARK 3 T TENSOR
REMARK 3 T11: 0.2225 T22: 0.2984
REMARK 3 T33: 0.2844 T12: -0.0123
REMARK 3 T13: 0.0231 T23: 0.0462
REMARK 3 L TENSOR
REMARK 3 L11: 4.1043 L22: 6.4378
REMARK 3 L33: 4.5638 L12: 2.3787
REMARK 3 L13: 2.7381 L23: 4.1290
REMARK 3 S TENSOR
REMARK 3 S11: 0.1224 S12: 0.3284 S13: -0.4081
REMARK 3 S21: 0.3588 S22: -0.0137 S23: -0.0878
REMARK 3 S31: 0.4599 S32: 0.2723 S33: -0.1024
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND RESI 147:193
REMARK 3 ORIGIN FOR THE GROUP (A): -18.4439 30.6612 -14.2914
REMARK 3 T TENSOR
REMARK 3 T11: 0.3205 T22: 0.2308
REMARK 3 T33: 0.2134 T12: -0.0824
REMARK 3 T13: -0.0723 T23: -0.0221
REMARK 3 L TENSOR
REMARK 3 L11: 7.5304 L22: 6.2362
REMARK 3 L33: 6.5989 L12: -0.2308
REMARK 3 L13: 1.1799 L23: 0.0629
REMARK 3 S TENSOR
REMARK 3 S11: -0.0744 S12: 0.4688 S13: -0.1394
REMARK 3 S21: -0.3088 S22: -0.0546 S23: 0.2990
REMARK 3 S31: 0.0365 S32: -0.2639 S33: 0.1522
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND RESI 194:271
REMARK 3 ORIGIN FOR THE GROUP (A): -13.1528 30.7156 7.9743
REMARK 3 T TENSOR
REMARK 3 T11: 0.2403 T22: 0.2541
REMARK 3 T33: 0.2268 T12: -0.0417
REMARK 3 T13: -0.0010 T23: 0.0568
REMARK 3 L TENSOR
REMARK 3 L11: 4.3941 L22: 3.1087
REMARK 3 L33: 2.1519 L12: -0.3799
REMARK 3 L13: -0.3198 L23: 0.4900
REMARK 3 S TENSOR
REMARK 3 S11: -0.0295 S12: 0.0272 S13: -0.0029
REMARK 3 S21: 0.1212 S22: -0.1138 S23: 0.0578
REMARK 3 S31: 0.0075 S32: 0.0124 S33: 0.1196
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 5CBK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JUL-15.
REMARK 100 THE DEPOSITION ID IS D_1000211348.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-APR-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14453
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 29.527
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 20.30
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09900
REMARK 200 FOR THE DATA SET : 53.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 19.10
REMARK 200 R MERGE FOR SHELL (I) : 0.73200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 7.000
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: 3W06
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.7 M SODIUM CITRATE, 0.01 M MAGNESIUM
REMARK 280 CHLORIDE, 0.05 M HEPES PH 7.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
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 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-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 67.82267
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 33.91133
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 50.86700
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 16.95567
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 84.77833
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 67.82267
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 33.91133
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 16.95567
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 50.86700
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 84.77833
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1030 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 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 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 662 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 663 LIES ON A SPECIAL POSITION.
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 28 -168.82 -126.27
REMARK 500 SER A 95 -110.65 55.25
REMARK 500 ASP A 129 25.86 44.67
REMARK 500 LEU A 166 -148.51 -149.53
REMARK 500 GLU A 167 103.13 -59.38
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 699 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH A 700 DISTANCE = 6.07 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 PE3 A 302
REMARK 610 PE3 A 303
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 A 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 6 O
REMARK 620 2 ASN A 9 OD1 93.9
REMARK 620 3 HOH A 494 O 94.9 84.3
REMARK 620 4 HOH A 427 O 74.8 153.9 73.5
REMARK 620 5 VAL A 12 O 82.2 62.0 145.8 136.6
REMARK 620 6 HOH A 506 O 90.5 89.1 171.8 114.0 29.2
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PE3 A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PE3 A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 304
DBREF 5CBK A 1 271 PDB 5CBK 5CBK 1 271
SEQRES 1 A 271 MET SER THR VAL GLY SER ALA HIS ASN VAL THR VAL LEU
SEQRES 2 A 271 GLY SER GLY GLU THR THR VAL VAL LEU GLY HIS GLY PHE
SEQRES 3 A 271 GLY THR ASP GLN SER VAL TRP LYS TYR LEU VAL PRO HIS
SEQRES 4 A 271 LEU THR ASP ASP TYR ARG VAL LEU LEU TYR ASP ASN MET
SEQRES 5 A 271 GLY ALA GLY THR THR ASP PRO ASN LEU TYR ASP PHE GLU
SEQRES 6 A 271 ARG TYR SER SER LEU GLU GLY HIS SER GLN ASP LEU ILE
SEQRES 7 A 271 ALA ILE LEU GLU GLU PHE HIS VAL THR LYS CYS ILE PHE
SEQRES 8 A 271 VAL GLY HIS SER LEU SER SER MET VAL GLY ALA VAL SER
SEQRES 9 A 271 SER ILE PHE ARG PRO ASP LEU PHE ARG LYS ILE VAL MET
SEQRES 10 A 271 ILE SER ALA CYS PRO ARG VAL ALA ASN ALA ASP ASP TYR
SEQRES 11 A 271 TYR GLY GLY PHE GLU GLU GLU ASP VAL ASN GLN LEU TYR
SEQRES 12 A 271 GLY ALA MET GLU GLU ASN PHE GLN THR MET MET THR GLY
SEQRES 13 A 271 TYR ALA PRO ILE VAL VAL GLY GLY ASP LEU GLU SER GLU
SEQRES 14 A 271 ALA MET GLN GLU PHE SER ARG THR LEU PHE ASN MET ARG
SEQRES 15 A 271 PRO ASP ILE ALA LEU SER ILE CYS ARG MET ILE SER GLY
SEQRES 16 A 271 TYR ASP LEU ARG PRO TYR LEU GLY LEU VAL VAL ILE PRO
SEQRES 17 A 271 CYS HIS ILE ILE GLN SER SER LYS ASP LYS LEU VAL PRO
SEQRES 18 A 271 VAL ALA VAL ALA GLU TYR LEU HIS ARG ASN PHE GLY GLY
SEQRES 19 A 271 LYS SER VAL VAL GLU LEU ILE PRO THR GLU GLY HIS LEU
SEQRES 20 A 271 PRO HIS LEU SER ALA PRO ASP ILE THR ILE PRO VAL LEU
SEQRES 21 A 271 ILE ARG HIS ILE ASN GLN ASP ILE ALA ASP ASP
HET MG A 301 1
HET PE3 A 302 19
HET PE3 A 303 7
HET CL A 304 1
HETNAM MG MAGNESIUM ION
HETNAM PE3 3,6,9,12,15,18,21,24,27,30,33,36,39-
HETNAM 2 PE3 TRIDECAOXAHENTETRACONTANE-1,41-DIOL
HETNAM CL CHLORIDE ION
HETSYN PE3 POLYETHYLENE GLYCOL
FORMUL 2 MG MG 2+
FORMUL 3 PE3 2(C28 H58 O15)
FORMUL 5 CL CL 1-
FORMUL 6 HOH *300(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 ASP A 58 TYR A 62 5 5
HELIX 5 AA5 GLU A 65 SER A 68 5 4
HELIX 6 AA6 SER A 69 PHE A 84 1 16
HELIX 7 AA7 SER A 95 ARG A 108 1 14
HELIX 8 AA8 GLU A 135 ASN A 149 1 15
HELIX 9 AA9 ASN A 149 GLY A 163 1 15
HELIX 10 AB1 SER A 168 PHE A 179 1 12
HELIX 11 AB2 ARG A 182 SER A 194 1 13
HELIX 12 AB3 LEU A 198 VAL A 205 5 8
HELIX 13 AB4 PRO A 221 PHE A 232 1 12
HELIX 14 AB5 LEU A 247 ALA A 252 1 6
HELIX 15 AB6 ALA A 252 GLN A 266 1 15
SHEET 1 AA1 7 THR A 11 GLY A 14 0
SHEET 2 AA1 7 ARG 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 ARG 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 PHE A 91
SHEET 6 AA1 7 CYS A 209 LYS A 216 1 O HIS A 210 N ILE A 115
SHEET 7 AA1 7 SER A 236 GLU A 244 1 O VAL A 237 N ILE A 211
LINK O SER A 6 MG MG A 301 1555 1555 2.14
LINK OD1 ASN A 9 MG MG A 301 1555 1555 2.09
LINK MG MG A 301 O HOH A 494 1555 1555 2.08
LINK MG MG A 301 O HOH A 427 1555 1555 2.08
LINK O VAL A 12 MG MG A 301 1555 12564 2.46
LINK MG MG A 301 O HOH A 506 1555 12564 2.08
CISPEP 1 ASP A 165 LEU A 166 0 -18.42
SITE 1 AC1 6 SER A 6 ASN A 9 VAL A 12 HOH A 427
SITE 2 AC1 6 HOH A 494 HOH A 506
SITE 1 AC2 8 VAL A 103 ILE A 106 PHE A 107 MET A 153
SITE 2 AC2 8 ILE A 160 TYR A 196 ASP A 197 HOH A 575
SITE 1 AC3 5 VAL A 139 TYR A 143 TYR A 157 ILE A 193
SITE 2 AC3 5 SER A 194
SITE 1 AC4 3 PHE A 26 SER A 95 HOH A 597
CRYST1 102.282 102.282 101.734 90.00 90.00 120.00 P 65 2 2 12
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 0.009777 0.005645 0.000000 0.00000
SCALE2 0.000000 0.011289 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009830 0.00000
TER 2130 ASP A 271
MASTER 373 0 4 15 7 0 7 6 2433 1 31 21
END |