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HEADER HYDROLASE 27-SEP-19 6UH9
TITLE CRYSTAL STRUCTURE OF DAD2 D166A MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DECREASED APICAL DOMINANCE 2;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: DAD2;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PETUNIA HYBRIDA;
SOURCE 3 ORGANISM_COMMON: PETUNIA;
SOURCE 4 ORGANISM_TAXID: 4102;
SOURCE 5 GENE: DAD2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA GAMI 2
KEYWDS STRIGOLACTONE RECEPTOR, DAD2, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.SHARMA,C.HAMIAUX,K.C.SNOWDEN
REVDAT 1 26-FEB-20 6UH9 0
JRNL AUTH H.W.LEE,P.SHARMA,B.J.JANSSEN,R.S.M.DRUMMOND,Z.LUO,C.HAMIAUX,
JRNL AUTH 2 T.COLLIER,J.R.ALLISON,R.D.NEWCOMB,K.C.SNOWDEN
JRNL TITL FLEXIBILITY OF THE PETUNIA STRIGOLACTONE RECEPTOR DAD2
JRNL TITL 2 PROMOTES ITS INTERACTION WITH SIGNALING PARTNERS
JRNL REF J.BIOL.CHEM. 2020
JRNL REFN ESSN 1083-351X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.HAMIAUX,R.S.DRUMMOND,B.J.JANSSEN,S.E.LEDGER,J.M.COONEY,
REMARK 1 AUTH 2 R.D.NEWCOMB,K.C.SNOWDEN
REMARK 1 TITL DAD2 IS AN ALPHA/BETA HYDROLASE LIKELY TO BE INVOLVED IN THE
REMARK 1 TITL 2 PERCEPTION OF THE PLANT BRANCHING HORMONE, STRIGOLACTONE.
REMARK 1 REF CURR. BIOL. V. 22 2032 2012
REMARK 1 REFN ISSN 1879-0445
REMARK 1 PMID 22959345
REMARK 1 DOI 10.1016/J.CUB.2012.08.007
REMARK 2
REMARK 2 RESOLUTION. 1.52 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0257
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.52
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.33
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.1
REMARK 3 NUMBER OF REFLECTIONS : 71299
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) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3718
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) : 1.52
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.56
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5164
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.44
REMARK 3 BIN R VALUE (WORKING SET) : 0.2610
REMARK 3 BIN FREE R VALUE SET COUNT : 275
REMARK 3 BIN FREE R VALUE : 0.2730
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4148
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 13
REMARK 3 SOLVENT ATOMS : 711
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.78
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.61000
REMARK 3 B22 (A**2) : -0.82000
REMARK 3 B33 (A**2) : -0.02000
REMARK 3 B12 (A**2) : -0.13000
REMARK 3 B13 (A**2) : 0.10000
REMARK 3 B23 (A**2) : 1.46000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.083
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.082
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.068
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.722
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4339 ; 0.009 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 4042 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5908 ; 1.513 ; 1.631
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9299 ; 1.479 ; 1.569
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 541 ; 6.427 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 243 ;26.229 ;20.412
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 678 ;12.544 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 39 ;17.607 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 544 ; 0.084 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4947 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1018 ; 0.001 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 3 266 B 3 266 8564 0.090 0.050
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 3 A 266
REMARK 3 ORIGIN FOR THE GROUP (A): -2.4950 3.8110 -15.5030
REMARK 3 T TENSOR
REMARK 3 T11: 0.0184 T22: 0.1986
REMARK 3 T33: 0.0879 T12: -0.0116
REMARK 3 T13: 0.0215 T23: -0.1173
REMARK 3 L TENSOR
REMARK 3 L11: 1.1675 L22: 0.3946
REMARK 3 L33: 0.6759 L12: 0.3870
REMARK 3 L13: 0.1961 L23: 0.0485
REMARK 3 S TENSOR
REMARK 3 S11: 0.0136 S12: -0.0907 S13: 0.0453
REMARK 3 S21: -0.0119 S22: -0.0553 S23: -0.0245
REMARK 3 S31: 0.0251 S32: -0.0383 S33: 0.0416
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 3 B 265
REMARK 3 ORIGIN FOR THE GROUP (A): 0.6610 23.7110 18.6850
REMARK 3 T TENSOR
REMARK 3 T11: 0.0198 T22: 0.2193
REMARK 3 T33: 0.0993 T12: -0.0175
REMARK 3 T13: 0.0224 T23: -0.1365
REMARK 3 L TENSOR
REMARK 3 L11: 1.4662 L22: 0.3733
REMARK 3 L33: 0.5066 L12: 0.2081
REMARK 3 L13: 0.2005 L23: 0.1481
REMARK 3 S TENSOR
REMARK 3 S11: 0.0109 S12: 0.1394 S13: -0.1285
REMARK 3 S21: 0.0206 S22: 0.0383 S23: -0.0014
REMARK 3 S31: -0.0028 S32: 0.0042 S33: -0.0493
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.00
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 6UH9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-SEP-19.
REMARK 100 THE DEPOSITION ID IS D_1000244606.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-JUN-18
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 : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9537
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.6.2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 75017
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.520
REMARK 200 RESOLUTION RANGE LOW (A) : 30.330
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.1
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.08900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.52
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.55
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.66900
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: PHASER 2.8.2
REMARK 200 STARTING MODEL: 4DNP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIZMA-ACETATE-BICINE (PH 8.5),
REMARK 280 0.06 M DIVALENTS (MGCL2 AND CACL2), 45-55% PEG 500 MME PEG 20000,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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
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 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 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 -1
REMARK 465 GLY A 0
REMARK 465 MET A 1
REMARK 465 GLY A 2
REMARK 465 ARG A 267
REMARK 465 GLY B -1
REMARK 465 GLY B 0
REMARK 465 MET B 1
REMARK 465 GLY B 2
REMARK 465 ARG B 267
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 605 O HOH A 624 1.14
REMARK 500 O HOH A 450 O HOH B 307 1.95
REMARK 500 O HOH A 422 O HOH A 499 1.96
REMARK 500 NZ LYS B 115 O HOH B 301 2.03
REMARK 500 O HOH A 541 O HOH A 657 2.05
REMARK 500 O HOH B 310 O HOH B 432 2.06
REMARK 500 O HOH B 406 O HOH B 506 2.11
REMARK 500 OD2 ASP B 61 O HOH B 302 2.14
REMARK 500 OE1 GLU B 129 O HOH B 303 2.14
REMARK 500 OD1 ASP B 72 O HOH B 304 2.17
REMARK 500
REMARK 500 REMARK: NULL
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 96 -127.17 64.07
REMARK 500 ALA A 252 56.86 -143.94
REMARK 500 SER B 96 -125.48 62.32
REMARK 500 ALA B 166 70.91 -68.54
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 776 DISTANCE = 6.17 ANGSTROMS
REMARK 525 HOH A 777 DISTANCE = 6.27 ANGSTROMS
REMARK 525 HOH B 633 DISTANCE = 6.33 ANGSTROMS
REMARK 525 HOH B 634 DISTANCE = 6.75 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 A 301
DBREF 6UH9 A -1 267 UNP L7MTK5 L7MTK5_PETHY 1 269
DBREF 6UH9 B -1 267 UNP L7MTK5 L7MTK5_PETHY 1 269
SEQADV 6UH9 GLN A 89 UNP L7MTK5 CYS 91 ENGINEERED MUTATION
SEQADV 6UH9 ALA A 166 UNP L7MTK5 ASP 168 ENGINEERED MUTATION
SEQADV 6UH9 GLN B 89 UNP L7MTK5 CYS 91 ENGINEERED MUTATION
SEQADV 6UH9 ALA B 166 UNP L7MTK5 ASP 168 ENGINEERED MUTATION
SEQRES 1 A 269 GLY GLY MET GLY GLN THR LEU LEU ASP ALA LEU ASN VAL
SEQRES 2 A 269 ARG VAL VAL GLY SER GLY GLU ARG VAL LEU VAL LEU ALA
SEQRES 3 A 269 HIS GLY PHE GLY THR ASP GLN SER ALA TRP ASN ARG ILE
SEQRES 4 A 269 LEU PRO PHE PHE LEU ARG ASP TYR ARG VAL VAL LEU TYR
SEQRES 5 A 269 ASP LEU VAL CYS ALA GLY SER VAL ASN PRO ASP PHE PHE
SEQRES 6 A 269 ASP PHE ARG ARG TYR THR THR LEU ASP PRO TYR VAL ASP
SEQRES 7 A 269 ASP LEU LEU HIS ILE LEU ASP ALA LEU GLY ILE ASP GLN
SEQRES 8 A 269 CYS ALA TYR VAL GLY HIS SER VAL SER ALA MET ILE GLY
SEQRES 9 A 269 ILE LEU ALA SER ILE ARG ARG PRO GLU LEU PHE SER LYS
SEQRES 10 A 269 LEU ILE LEU ILE GLY ALA SER PRO ARG PHE LEU ASN ASP
SEQRES 11 A 269 GLU ASP TYR HIS GLY GLY PHE GLU GLN GLY GLU ILE GLU
SEQRES 12 A 269 LYS VAL PHE SER ALA MET GLU ALA ASN TYR GLU ALA TRP
SEQRES 13 A 269 VAL ASN GLY PHE ALA PRO LEU ALA VAL GLY ALA ALA VAL
SEQRES 14 A 269 PRO ALA ALA VAL ARG GLU PHE SER ARG THR LEU PHE ASN
SEQRES 15 A 269 MET ARG PRO ASP ILE THR LEU PHE VAL SER ARG THR VAL
SEQRES 16 A 269 PHE ASN SER ASP MET ARG GLY VAL LEU GLY LEU VAL LYS
SEQRES 17 A 269 VAL PRO CYS HIS ILE PHE GLN THR ALA ARG ASP HIS SER
SEQRES 18 A 269 VAL PRO ALA SER VAL ALA THR TYR LEU LYS ASN HIS LEU
SEQRES 19 A 269 GLY GLY LYS ASN THR VAL HIS TRP LEU ASN ILE GLU GLY
SEQRES 20 A 269 HIS LEU PRO HIS LEU SER ALA PRO THR LEU LEU ALA GLN
SEQRES 21 A 269 GLU LEU ARG ARG ALA LEU SER HIS ARG
SEQRES 1 B 269 GLY GLY MET GLY GLN THR LEU LEU ASP ALA LEU ASN VAL
SEQRES 2 B 269 ARG VAL VAL GLY SER GLY GLU ARG VAL LEU VAL LEU ALA
SEQRES 3 B 269 HIS GLY PHE GLY THR ASP GLN SER ALA TRP ASN ARG ILE
SEQRES 4 B 269 LEU PRO PHE PHE LEU ARG ASP TYR ARG VAL VAL LEU TYR
SEQRES 5 B 269 ASP LEU VAL CYS ALA GLY SER VAL ASN PRO ASP PHE PHE
SEQRES 6 B 269 ASP PHE ARG ARG TYR THR THR LEU ASP PRO TYR VAL ASP
SEQRES 7 B 269 ASP LEU LEU HIS ILE LEU ASP ALA LEU GLY ILE ASP GLN
SEQRES 8 B 269 CYS ALA TYR VAL GLY HIS SER VAL SER ALA MET ILE GLY
SEQRES 9 B 269 ILE LEU ALA SER ILE ARG ARG PRO GLU LEU PHE SER LYS
SEQRES 10 B 269 LEU ILE LEU ILE GLY ALA SER PRO ARG PHE LEU ASN ASP
SEQRES 11 B 269 GLU ASP TYR HIS GLY GLY PHE GLU GLN GLY GLU ILE GLU
SEQRES 12 B 269 LYS VAL PHE SER ALA MET GLU ALA ASN TYR GLU ALA TRP
SEQRES 13 B 269 VAL ASN GLY PHE ALA PRO LEU ALA VAL GLY ALA ALA VAL
SEQRES 14 B 269 PRO ALA ALA VAL ARG GLU PHE SER ARG THR LEU PHE ASN
SEQRES 15 B 269 MET ARG PRO ASP ILE THR LEU PHE VAL SER ARG THR VAL
SEQRES 16 B 269 PHE ASN SER ASP MET ARG GLY VAL LEU GLY LEU VAL LYS
SEQRES 17 B 269 VAL PRO CYS HIS ILE PHE GLN THR ALA ARG ASP HIS SER
SEQRES 18 B 269 VAL PRO ALA SER VAL ALA THR TYR LEU LYS ASN HIS LEU
SEQRES 19 B 269 GLY GLY LYS ASN THR VAL HIS TRP LEU ASN ILE GLU GLY
SEQRES 20 B 269 HIS LEU PRO HIS LEU SER ALA PRO THR LEU LEU ALA GLN
SEQRES 21 B 269 GLU LEU ARG ARG ALA LEU SER HIS ARG
HET PG4 A 301 13
HETNAM PG4 TETRAETHYLENE GLYCOL
FORMUL 3 PG4 C8 H18 O5
FORMUL 4 HOH *711(H2 O)
HELIX 1 AA1 GLN A 3 LEU A 9 1 7
HELIX 2 AA2 ASP A 30 ASN A 35 5 6
HELIX 3 AA3 ILE A 37 PHE A 41 5 5
HELIX 4 AA4 ASN A 59 PHE A 63 5 5
HELIX 5 AA5 LEU A 71 LEU A 85 1 15
HELIX 6 AA6 SER A 96 ARG A 109 1 14
HELIX 7 AA7 GLU A 136 ASN A 150 1 15
HELIX 8 AA8 ASN A 150 GLY A 164 1 15
HELIX 9 AA9 VAL A 167 MET A 181 1 15
HELIX 10 AB1 ARG A 182 SER A 196 1 15
HELIX 11 AB2 MET A 198 VAL A 205 5 8
HELIX 12 AB3 PRO A 221 LEU A 232 1 12
HELIX 13 AB4 LEU A 247 ALA A 252 1 6
HELIX 14 AB5 ALA A 252 HIS A 266 1 15
HELIX 15 AB6 THR B 4 LEU B 9 1 6
HELIX 16 AB7 ASP B 30 ASN B 35 5 6
HELIX 17 AB8 ILE B 37 PHE B 41 5 5
HELIX 18 AB9 ASN B 59 PHE B 63 5 5
HELIX 19 AC1 LEU B 71 LEU B 85 1 15
HELIX 20 AC2 SER B 96 ARG B 109 1 14
HELIX 21 AC3 GLU B 136 ASN B 150 1 15
HELIX 22 AC4 ASN B 150 GLY B 164 1 15
HELIX 23 AC5 VAL B 167 MET B 181 1 15
HELIX 24 AC6 ARG B 182 SER B 196 1 15
HELIX 25 AC7 MET B 198 VAL B 205 5 8
HELIX 26 AC8 PRO B 221 LEU B 232 1 12
HELIX 27 AC9 LEU B 247 ALA B 252 1 6
HELIX 28 AD1 ALA B 252 HIS B 266 1 15
SHEET 1 AA1 7 ARG A 12 VAL A 14 0
SHEET 2 AA1 7 ARG A 46 TYR A 50 -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 ALA A 215 1 O PHE A 212 N LEU A 118
SHEET 7 AA1 7 ASN A 236 GLU A 244 1 O THR A 237 N ILE A 211
SHEET 1 AA2 7 ARG B 12 VAL B 14 0
SHEET 2 AA2 7 TYR B 45 TYR B 50 -1 O VAL B 47 N VAL B 14
SHEET 3 AA2 7 ARG B 19 ALA B 24 1 N ARG B 19 O ARG B 46
SHEET 4 AA2 7 CYS B 90 HIS B 95 1 O VAL B 93 N VAL B 22
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 ALA B 215 1 O PHE B 212 N LEU B 118
SHEET 7 AA2 7 ASN B 236 GLU B 244 1 O HIS B 239 N ILE B 211
SITE 1 AC1 7 VAL A 143 SER A 190 PHE A 194 HOH A 469
SITE 2 AC1 7 HOH A 646 HOH A 654 HOH A 677
CRYST1 36.690 56.530 68.040 94.47 94.67 108.83 P 1 2
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 0.027255 0.009294 0.003273 0.00000
SCALE2 0.000000 0.018690 0.002077 0.00000
SCALE3 0.000000 0.000000 0.014837 0.00000
TER 2109 HIS A 266
TER 4214 HIS B 266
MASTER 361 0 1 28 14 0 2 6 4872 2 13 42
END |