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HEADER HYDROLASE 21-MAY-19 6RS4
TITLE STRUCTURE OF TABERSONINE SYNTHASE - AN ALPHA-BETA HYDROLASE FROM
TITLE 2 CATHARANTHUS ROSEUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TABERSONINE SYNTHASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: HYDROLASE 2,CRHL2;
COMPND 5 EC: 4.-.-.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CATHARANTHUS ROSEUS;
SOURCE 3 ORGANISM_COMMON: MADAGASCAR PERIWINKLE;
SOURCE 4 ORGANISM_TAXID: 4058;
SOURCE 5 GENE: TS, HL2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: SOLUBL21;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: POPINF
KEYWDS ALKALOID, TABERSONINE, NATURAL PRODUCT, BIOSYNTHESIS, ALPHA/BETA
KEYWDS 2 HYDROLASE FOLD, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.CAPUTI,J.FRANKE,K.BUSSEY,S.C.FARROW,I.J.CURCINO VIEIRA,
AUTHOR 2 C.E.M.STEVENSON,D.M.LAWSON,S.E.O'CONNOR
REVDAT 1 04-MAR-20 6RS4 0
JRNL AUTH L.CAPUTI,J.FRANKE,K.BUSSEY,S.C.FARROW,I.J.C.VIEIRA,
JRNL AUTH 2 C.E.M.STEVENSON,D.M.LAWSON,S.E.O'CONNOR
JRNL TITL STRUCTURAL BASIS OF CYCLOADDITION IN BIOSYNTHESIS OF IBOGA
JRNL TITL 2 AND ASPIDOSPERMA ALKALOIDS.
JRNL REF NAT.CHEM.BIOL. 2020
JRNL REFN ESSN 1552-4469
JRNL PMID 32066966
JRNL DOI 10.1038/S41589-019-0460-X
REMARK 2
REMARK 2 RESOLUTION. 1.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0238
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) : 1.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 59.95
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 168522
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) : 0.134
REMARK 3 R VALUE (WORKING SET) : 0.133
REMARK 3 FREE R VALUE : 0.162
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 8863
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) : 1.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.33
REMARK 3 REFLECTION IN BIN (WORKING SET) : 12394
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.82
REMARK 3 BIN R VALUE (WORKING SET) : 0.2810
REMARK 3 BIN FREE R VALUE SET COUNT : 689
REMARK 3 BIN FREE R VALUE : 0.3110
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4968
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 44
REMARK 3 SOLVENT ATOMS : 699
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 10.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.17
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.63000
REMARK 3 B22 (A**2) : 1.80000
REMARK 3 B33 (A**2) : -1.59000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.73000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.040
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.040
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.033
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.907
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.981
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.975
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5463 ; 0.010 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 4931 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7475 ; 1.636 ; 1.639
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11481 ; 1.506 ; 1.570
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 710 ; 6.753 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 266 ;33.774 ;23.271
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 862 ;12.624 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;17.114 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 702 ; 0.098 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6251 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1169 ; 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): 10394 ; 7.269 ; 3.000
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 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 : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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 : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 6RS4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-MAY-19.
REMARK 100 THE DEPOSITION ID IS D_1292102507.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-JUL-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS 20160517
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 177427
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.300
REMARK 200 RESOLUTION RANGE LOW (A) : 59.950
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.11100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.50
REMARK 200 R MERGE FOR SHELL (I) : 1.68000
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 2.6.1
REMARK 200 STARTING MODEL: 2O7R
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL, PH 5, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 293K
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 54.48100
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 0
REMARK 465 PRO A 1
REMARK 465 GLY A 2
REMARK 465 SER A 3
REMARK 465 SER A 4
REMARK 465 ASP A 5
REMARK 465 GLY B 0
REMARK 465 PRO B 1
REMARK 465 GLY B 2
REMARK 465 SER B 3
REMARK 465 SER B 4
REMARK 465 ASP B 5
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 6 CG CD OE1 OE2
REMARK 470 LYS A 16 NZ
REMARK 470 LYS A 19 CG CD CE NZ
REMARK 470 ARG A 22 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 24 CD OE1 OE2
REMARK 470 LEU A 26 CG CD1 CD2
REMARK 470 HIS A 27 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 63 NZ
REMARK 470 LYS A 104 CE NZ
REMARK 470 LYS A 194 CD CE NZ
REMARK 470 LYS A 226 CE NZ
REMARK 470 GLU A 304 CG CD OE1 OE2
REMARK 470 LYS A 309 CG CD CE NZ
REMARK 470 ARG A 313 CZ NH1 NH2
REMARK 470 LEU B 11 CD1 CD2
REMARK 470 LYS B 16 NZ
REMARK 470 LYS B 19 CG CD CE NZ
REMARK 470 ARG B 22 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 24 CG CD OE1 OE2
REMARK 470 HIS B 27 CG ND1 CD2 CE1 NE2
REMARK 470 LYS B 104 CD CE NZ
REMARK 470 LYS B 146 CE NZ
REMARK 470 LYS B 194 CD CE NZ
REMARK 470 LYS B 212 CD CE NZ
REMARK 470 ARG B 222 CZ NH1 NH2
REMARK 470 LYS B 309 CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 TYR A 254 CB - CG - CD1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 TYR B 254 CB - CG - CD1 ANGL. DEV. = 4.4 DEGREES
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 ALA A 80 48.56 82.13
REMARK 500 GLU A 85 -173.18 67.85
REMARK 500 SER A 170 -112.67 44.96
REMARK 500 GLN A 213 -157.56 -100.80
REMARK 500 ASN A 219 -89.38 -125.97
REMARK 500 ALA B 80 51.40 83.74
REMARK 500 PHE B 82 -1.43 69.29
REMARK 500 GLU B 85 -174.69 69.03
REMARK 500 SER B 170 -114.20 46.68
REMARK 500 ASN B 219 -78.48 -112.32
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 848 DISTANCE = 6.11 ANGSTROMS
REMARK 525 HOH B 851 DISTANCE = 6.10 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 405
DBREF1 6RS4 A 2 320 UNP TS_CATRO
DBREF2 6RS4 A A0A2P1GIW3 2 320
DBREF1 6RS4 B 2 320 UNP TS_CATRO
DBREF2 6RS4 B A0A2P1GIW3 2 320
SEQADV 6RS4 GLY A 0 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RS4 PRO A 1 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RS4 GLY B 0 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RS4 PRO B 1 UNP A0A2P1GIW EXPRESSION TAG
SEQRES 1 A 321 GLY PRO GLY SER SER ASP GLU THR ILE PHE ASP LEU PRO
SEQRES 2 A 321 PRO TYR ILE LYS VAL PHE LYS ASP GLY ARG VAL GLU ARG
SEQRES 3 A 321 LEU HIS SER SER PRO TYR VAL PRO PRO SER LEU ASN ASP
SEQRES 4 A 321 PRO GLU THR GLY GLY VAL SER TRP LYS ASP VAL PRO ILE
SEQRES 5 A 321 SER SER VAL VAL SER ALA ARG ILE TYR LEU PRO LYS ILE
SEQRES 6 A 321 ASN ASN HIS ASP GLU LYS LEU PRO ILE ILE VAL TYR PHE
SEQRES 7 A 321 HIS GLY ALA GLY PHE CYS LEU GLU SER ALA PHE LYS SER
SEQRES 8 A 321 PHE PHE HIS THR TYR VAL LYS HIS PHE VAL ALA GLU ALA
SEQRES 9 A 321 LYS ALA ILE ALA VAL SER VAL GLU PHE ARG LEU ALA PRO
SEQRES 10 A 321 GLU ASN HIS LEU PRO ALA ALA TYR GLU ASP CYS TRP GLU
SEQRES 11 A 321 ALA LEU GLN TRP VAL ALA SER HIS VAL GLY LEU ASP ILE
SEQRES 12 A 321 SER SER LEU LYS THR CYS ILE ASP LYS ASP PRO TRP ILE
SEQRES 13 A 321 ILE ASN TYR ALA ASP PHE ASP ARG LEU TYR LEU TRP GLY
SEQRES 14 A 321 ASP SER THR GLY ALA ASN ILE VAL HIS ASN THR LEU ILE
SEQRES 15 A 321 ARG SER GLY LYS GLU LYS LEU ASN GLY GLY LYS VAL LYS
SEQRES 16 A 321 ILE LEU GLY ALA ILE LEU TYR TYR PRO TYR PHE LEU ILE
SEQRES 17 A 321 ARG THR SER SER LYS GLN SER ASP TYR MET GLU ASN GLU
SEQRES 18 A 321 TYR ARG SER TYR TRP LYS LEU ALA TYR PRO ASP ALA PRO
SEQRES 19 A 321 GLY GLY ASN ASP ASN PRO MET ILE ASN PRO THR ALA GLU
SEQRES 20 A 321 ASN ALA PRO ASP LEU ALA GLY TYR GLY CYS SER ARG LEU
SEQRES 21 A 321 LEU ILE SER MET VAL ALA ASP GLU ALA ARG ASP ILE THR
SEQRES 22 A 321 LEU LEU TYR ILE ASP ALA LEU GLU LYS SER GLY TRP LYS
SEQRES 23 A 321 GLY GLU LEU ASP VAL ALA ASP PHE ASP LYS GLN TYR PHE
SEQRES 24 A 321 GLU LEU PHE GLU MET GLU THR GLU VAL ALA LYS ASN MET
SEQRES 25 A 321 LEU ARG ARG LEU ALA SER PHE ILE LYS
SEQRES 1 B 321 GLY PRO GLY SER SER ASP GLU THR ILE PHE ASP LEU PRO
SEQRES 2 B 321 PRO TYR ILE LYS VAL PHE LYS ASP GLY ARG VAL GLU ARG
SEQRES 3 B 321 LEU HIS SER SER PRO TYR VAL PRO PRO SER LEU ASN ASP
SEQRES 4 B 321 PRO GLU THR GLY GLY VAL SER TRP LYS ASP VAL PRO ILE
SEQRES 5 B 321 SER SER VAL VAL SER ALA ARG ILE TYR LEU PRO LYS ILE
SEQRES 6 B 321 ASN ASN HIS ASP GLU LYS LEU PRO ILE ILE VAL TYR PHE
SEQRES 7 B 321 HIS GLY ALA GLY PHE CYS LEU GLU SER ALA PHE LYS SER
SEQRES 8 B 321 PHE PHE HIS THR TYR VAL LYS HIS PHE VAL ALA GLU ALA
SEQRES 9 B 321 LYS ALA ILE ALA VAL SER VAL GLU PHE ARG LEU ALA PRO
SEQRES 10 B 321 GLU ASN HIS LEU PRO ALA ALA TYR GLU ASP CYS TRP GLU
SEQRES 11 B 321 ALA LEU GLN TRP VAL ALA SER HIS VAL GLY LEU ASP ILE
SEQRES 12 B 321 SER SER LEU LYS THR CYS ILE ASP LYS ASP PRO TRP ILE
SEQRES 13 B 321 ILE ASN TYR ALA ASP PHE ASP ARG LEU TYR LEU TRP GLY
SEQRES 14 B 321 ASP SER THR GLY ALA ASN ILE VAL HIS ASN THR LEU ILE
SEQRES 15 B 321 ARG SER GLY LYS GLU LYS LEU ASN GLY GLY LYS VAL LYS
SEQRES 16 B 321 ILE LEU GLY ALA ILE LEU TYR TYR PRO TYR PHE LEU ILE
SEQRES 17 B 321 ARG THR SER SER LYS GLN SER ASP TYR MET GLU ASN GLU
SEQRES 18 B 321 TYR ARG SER TYR TRP LYS LEU ALA TYR PRO ASP ALA PRO
SEQRES 19 B 321 GLY GLY ASN ASP ASN PRO MET ILE ASN PRO THR ALA GLU
SEQRES 20 B 321 ASN ALA PRO ASP LEU ALA GLY TYR GLY CYS SER ARG LEU
SEQRES 21 B 321 LEU ILE SER MET VAL ALA ASP GLU ALA ARG ASP ILE THR
SEQRES 22 B 321 LEU LEU TYR ILE ASP ALA LEU GLU LYS SER GLY TRP LYS
SEQRES 23 B 321 GLY GLU LEU ASP VAL ALA ASP PHE ASP LYS GLN TYR PHE
SEQRES 24 B 321 GLU LEU PHE GLU MET GLU THR GLU VAL ALA LYS ASN MET
SEQRES 25 B 321 LEU ARG ARG LEU ALA SER PHE ILE LYS
HET EDO A 401 4
HET EDO A 402 4
HET EDO A 403 4
HET EDO A 404 4
HET EDO A 405 4
HET EDO A 406 8
HET EDO B 401 8
HET EDO B 402 4
HET EDO B 403 4
HET EDO B 404 4
HET EDO B 405 8
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 EDO 11(C2 H6 O2)
FORMUL 14 HOH *699(H2 O)
HELIX 1 AA1 LYS A 89 LYS A 104 1 16
HELIX 2 AA2 PRO A 121 SER A 136 1 16
HELIX 3 AA3 ASP A 141 THR A 147 5 7
HELIX 4 AA4 ASP A 152 TYR A 158 1 7
HELIX 5 AA5 SER A 170 GLY A 184 1 15
HELIX 6 AA6 LYS A 187 LYS A 192 5 6
HELIX 7 AA7 SER A 214 ASN A 219 1 6
HELIX 8 AA8 ASN A 219 TYR A 229 1 11
HELIX 9 AA9 GLY A 234 ASN A 238 5 5
HELIX 10 AB1 ASP A 250 TYR A 254 5 5
HELIX 11 AB2 GLU A 267 GLY A 283 1 17
HELIX 12 AB3 GLN A 296 GLU A 302 5 7
HELIX 13 AB4 THR A 305 SER A 317 1 13
HELIX 14 AB5 LYS B 89 LYS B 104 1 16
HELIX 15 AB6 PRO B 121 SER B 136 1 16
HELIX 16 AB7 ASP B 141 THR B 147 5 7
HELIX 17 AB8 ASP B 152 TYR B 158 1 7
HELIX 18 AB9 SER B 170 GLU B 186 1 17
HELIX 19 AC1 LYS B 187 LYS B 192 5 6
HELIX 20 AC2 SER B 214 ASN B 219 1 6
HELIX 21 AC3 ASN B 219 TYR B 229 1 11
HELIX 22 AC4 GLY B 234 ASN B 238 5 5
HELIX 23 AC5 ASP B 250 TYR B 254 5 5
HELIX 24 AC6 ALA B 268 SER B 282 1 15
HELIX 25 AC7 GLN B 296 GLU B 302 5 7
HELIX 26 AC8 THR B 305 SER B 317 1 13
SHEET 1 AA1 3 THR A 7 LEU A 11 0
SHEET 2 AA1 3 ILE A 15 PHE A 18 -1 O ILE A 15 N LEU A 11
SHEET 3 AA1 3 VAL A 23 ARG A 25 -1 O GLU A 24 N LYS A 16
SHEET 1 AA2 8 SER A 45 PRO A 50 0
SHEET 2 AA2 8 SER A 56 LEU A 61 -1 O ILE A 59 N LYS A 47
SHEET 3 AA2 8 ILE A 106 GLU A 111 -1 O GLU A 111 N SER A 56
SHEET 4 AA2 8 LEU A 71 PHE A 77 1 N ILE A 74 O ILE A 106
SHEET 5 AA2 8 ALA A 159 ASP A 169 1 O TYR A 165 N ILE A 73
SHEET 6 AA2 8 GLY A 197 TYR A 201 1 O TYR A 201 N GLY A 168
SHEET 7 AA2 8 ARG A 258 MET A 263 1 O LEU A 260 N LEU A 200
SHEET 8 AA2 8 GLU A 287 ASP A 292 1 O ASP A 289 N LEU A 259
SHEET 1 AA3 3 THR B 7 LEU B 11 0
SHEET 2 AA3 3 ILE B 15 PHE B 18 -1 O VAL B 17 N PHE B 9
SHEET 3 AA3 3 VAL B 23 GLU B 24 -1 O GLU B 24 N LYS B 16
SHEET 1 AA4 8 SER B 45 PRO B 50 0
SHEET 2 AA4 8 SER B 56 LEU B 61 -1 O ILE B 59 N LYS B 47
SHEET 3 AA4 8 ILE B 106 GLU B 111 -1 O GLU B 111 N SER B 56
SHEET 4 AA4 8 LEU B 71 PHE B 77 1 N ILE B 74 O ILE B 106
SHEET 5 AA4 8 ALA B 159 ASP B 169 1 O TYR B 165 N ILE B 73
SHEET 6 AA4 8 GLY B 197 TYR B 201 1 O TYR B 201 N GLY B 168
SHEET 7 AA4 8 ARG B 258 MET B 263 1 O LEU B 260 N LEU B 200
SHEET 8 AA4 8 GLU B 287 ASP B 292 1 O ASP B 289 N LEU B 259
CISPEP 1 PRO A 12 PRO A 13 0 -2.79
CISPEP 2 ALA A 115 PRO A 116 0 -1.24
CISPEP 3 LEU A 120 PRO A 121 0 10.53
CISPEP 4 PRO B 12 PRO B 13 0 -3.40
CISPEP 5 ALA B 115 PRO B 116 0 -4.05
CISPEP 6 LEU B 120 PRO B 121 0 9.39
SITE 1 AC1 7 GLY A 81 SER A 170 THR A 171 TYR A 204
SITE 2 AC1 7 HOH A 505 HOH A 697 HOH A 733
SITE 1 AC2 5 SER A 28 GLU A 85 LYS A 89 EDO A 403
SITE 2 AC2 5 HOH A 587
SITE 1 AC3 7 TYR A 31 SER A 86 LYS A 89 EDO A 402
SITE 2 AC3 7 HOH A 720 HOH A 729 TYR B 31
SITE 1 AC4 8 HIS A 137 VAL A 138 GLY A 139 LEU A 140
SITE 2 AC4 8 ILE A 156 PHE A 161 HOH A 510 HOH A 702
SITE 1 AC5 7 LEU A 206 ILE A 207 ARG A 208 ARG A 222
SITE 2 AC5 7 ASN A 236 ASP A 237 HOH A 633
SITE 1 AC6 10 GLU A 129 GLN A 132 TRP A 133 SER A 136
SITE 2 AC6 10 LYS A 151 HOH A 507 HOH A 521 HOH A 522
SITE 3 AC6 10 HOH A 537 HOH A 547
SITE 1 AC7 11 GLY B 81 SER B 170 THR B 171 TYR B 202
SITE 2 AC7 11 TYR B 204 TYR B 221 TYR B 224 HOH B 509
SITE 3 AC7 11 HOH B 556 HOH B 565 HOH B 632
SITE 1 AC8 5 PRO A 30 TYR A 31 HOH A 729 LYS B 89
SITE 2 AC8 5 HOH B 569
SITE 1 AC9 7 HIS B 137 VAL B 138 GLY B 139 LEU B 140
SITE 2 AC9 7 PHE B 161 HOH B 547 HOH B 715
SITE 1 AD1 5 ARG B 25 SER B 86 LYS B 89 HOH B 520
SITE 2 AD1 5 HOH B 607
SITE 1 AD2 10 GLU B 129 GLN B 132 TRP B 133 SER B 136
SITE 2 AD2 10 LYS B 151 HOH B 506 HOH B 511 HOH B 527
SITE 3 AD2 10 HOH B 528 HOH B 553
CRYST1 56.485 108.962 63.235 90.00 108.54 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 0.017704 0.000000 0.005937 0.00000
SCALE2 0.000000 0.009178 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016680 0.00000
TER 2611 LYS A 320
TER 5236 LYS B 320
MASTER 383 0 11 26 22 0 25 6 5711 2 56 50
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