HEADER TRANSFERASE 06-DEC-11 3UYL
TITLE SPINOSYN RHAMNOSYLTRANSFERASE SPNG COMPLEXED WITH THYMIDINE
TITLE 2 DIPHOSPHATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NDP-RHAMNOSYLTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 1-386;
COMPND 5 SYNONYM: SPNG;
COMPND 6 EC: 2.4.1.-;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROPOLYSPORA SPINOSA;
SOURCE 3 ORGANISM_TAXID: 60894;
SOURCE 4 GENE: SPNG;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS GLYCOSYLTRANSFERASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.A.ISIORHO,H.-W.LIU,A.T.KEATINGE-CLAY
REVDAT 5 13-SEP-23 3UYL 1 HETSYN
REVDAT 4 29-JUL-20 3UYL 1 COMPND REMARK SEQADV HETNAM
REVDAT 4 2 1 LINK SITE
REVDAT 3 24-JAN-18 3UYL 1 AUTHOR
REVDAT 2 29-FEB-12 3UYL 1 JRNL
REVDAT 1 15-FEB-12 3UYL 0
JRNL AUTH E.A.ISIORHO,H.W.LIU,A.T.KEATINGE-CLAY
JRNL TITL STRUCTURAL STUDIES OF THE SPINOSYN RHAMNOSYLTRANSFERASE,
JRNL TITL 2 SPNG.
JRNL REF BIOCHEMISTRY V. 51 1213 2012
JRNL REFN ISSN 0006-2960
JRNL PMID 22283226
JRNL DOI 10.1021/BI201860Q
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC VERSION: 5.5.0072
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.62
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.0
REMARK 3 NUMBER OF REFLECTIONS : 57920
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) : 0.235
REMARK 3 R VALUE (WORKING SET) : 0.232
REMARK 3 FREE R VALUE : 0.291
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3104
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) : 1.86
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.90
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4076
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.56
REMARK 3 BIN R VALUE (WORKING SET) : 0.4190
REMARK 3 BIN FREE R VALUE SET COUNT : 219
REMARK 3 BIN FREE R VALUE : 0.4550
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5533
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 64
REMARK 3 SOLVENT ATOMS : 417
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.18
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.01000
REMARK 3 B12 (A**2) : -0.01000
REMARK 3 B13 (A**2) : -0.01000
REMARK 3 B23 (A**2) : 0.01000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.189
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.182
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.148
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.337
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.900
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.840
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5736 ; 0.019 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 12 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7880 ; 2.141 ; 1.991
REMARK 3 BOND ANGLES OTHERS (DEGREES): 20 ; 1.886 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 738 ; 6.616 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 225 ;35.257 ;23.289
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 814 ;15.544 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 44 ;20.658 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 918 ; 0.134 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4406 ; 0.012 ; 0.022
REMARK 3 GENERAL PLANES OTHERS (A): 4 ; 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 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 : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 3UYL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-DEC-11.
REMARK 100 THE DEPOSITION ID IS D_1000069371.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JUL-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : ASYMMETRIC CUT SINGLE CRYSTAL
REMARK 200 SI(220)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57920
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 24.620
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.6
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 <I/SIGMA(I)> 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 MR
REMARK 200 STARTING MODEL: PDB ENTRY 3TSA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% W/V PEG3350, 12.5-13.5% W/V
REMARK 280 GLUCOSE, 1% V/V GLYCEROL, 0.1 M MAGNESIUM FORMATE, 0.1 M SODIUM
REMARK 280 CACODYLATE, PH 6.9, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 298.15K
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
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -58.0 KCAL/MOL
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 55
REMARK 465 ASN A 56
REMARK 465 ASP A 57
REMARK 465 ARG A 58
REMARK 465 THR A 59
REMARK 465 GLY A 60
REMARK 465 ASP A 61
REMARK 465 THR A 62
REMARK 465 GLY A 63
REMARK 465 GLY A 64
REMARK 465 THR A 65
REMARK 465 THR A 66
REMARK 465 GLN A 67
REMARK 465 LEU A 68
REMARK 465 ALA A 386
REMARK 465 HIS B 0
REMARK 465 GLY B 55
REMARK 465 ASN B 56
REMARK 465 ASP B 57
REMARK 465 ARG B 58
REMARK 465 THR B 59
REMARK 465 GLY B 60
REMARK 465 ASP B 61
REMARK 465 THR B 62
REMARK 465 GLY B 63
REMARK 465 GLY B 64
REMARK 465 THR B 65
REMARK 465 THR B 66
REMARK 465 GLN B 67
REMARK 465 LEU B 68
REMARK 465 THR B 385
REMARK 465 ALA B 386
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 633 O HOH A 683 2.14
REMARK 500 O HOH B 548 O HOH B 695 2.16
REMARK 500 OE1 GLU A 287 O HOH A 656 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 597 O HOH B 708 1556 1.57
REMARK 500 O HOH A 703 O HOH B 704 1556 1.80
REMARK 500 O HOH A 703 O HOH B 705 1556 1.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 TRP A 112 CE2 TRP A 112 CD2 0.089
REMARK 500 TRP A 142 CE2 TRP A 142 CD2 0.077
REMARK 500 TRP B 142 CE2 TRP B 142 CD2 0.074
REMARK 500 HIS B 166 CG HIS B 166 CD2 0.065
REMARK 500 HIS B 260 CG HIS B 260 CD2 0.061
REMARK 500
REMARK 500 REMARK: NULL
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 PRO A 146 C - N - CA ANGL. DEV. = 9.3 DEGREES
REMARK 500 ARG A 239 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 MET A 372 CG - SD - CE ANGL. DEV. = -14.5 DEGREES
REMARK 500 LEU B 133 CB - CG - CD1 ANGL. DEV. = -11.0 DEGREES
REMARK 500 ARG B 141 NE - CZ - NH2 ANGL. DEV. = -5.3 DEGREES
REMARK 500 PRO B 172 C - N - CA ANGL. DEV. = -11.0 DEGREES
REMARK 500 ARG B 214 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 LEU B 378 CA - CB - CG ANGL. DEV. = -20.0 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 PRO A 9 48.89 -71.54
REMARK 500 THR A 215 -166.26 -115.23
REMARK 500 ASP A 266 49.99 38.39
REMARK 500 SER A 276 58.78 28.11
REMARK 500 PHE A 315 -122.42 54.04
REMARK 500 PRO B 9 49.49 -69.94
REMARK 500 ILE B 125 -38.10 -35.63
REMARK 500 GLN B 192 119.83 -31.82
REMARK 500 PHE B 282 -14.13 -144.64
REMARK 500 PHE B 315 -125.12 49.60
REMARK 500
REMARK 500 REMARK: NULL
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 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 541 O
REMARK 620 2 HOH A 582 O 90.7
REMARK 620 3 HOH A 597 O 75.1 80.6
REMARK 620 4 HOH A 703 O 131.0 98.3 153.9
REMARK 620 N 1 2 3
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3TSA RELATED DB: PDB
REMARK 900 SPINOSYN RHAMNOSYLTRANSFERASE SPNG
REMARK 900 RELATED ID: 3UYK RELATED DB: PDB
REMARK 900 SPINOSYN RHAMNOSYLTRANSFERASE SPNG COMPLEXED WITH SPINOSYN AGLYCONE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE AUTHORS STATE THAT RESIDUE ALA 360 IS CORRECT.
DBREF 3UYL A 1 386 UNP Q9ALM8 Q9ALM8_9PSEU 1 386
DBREF 3UYL B 1 386 UNP Q9ALM8 Q9ALM8_9PSEU 1 386
SEQADV 3UYL HIS A 0 UNP Q9ALM8 EXPRESSION TAG
SEQADV 3UYL ALA A 360 UNP Q9ALM8 SER 360 SEE REMARK 999
SEQADV 3UYL HIS B 0 UNP Q9ALM8 EXPRESSION TAG
SEQADV 3UYL ALA B 360 UNP Q9ALM8 SER 360 SEE REMARK 999
SEQRES 1 A 387 HIS MET ARG VAL LEU VAL VAL PRO LEU PRO TYR PRO THR
SEQRES 2 A 387 HIS LEU MET ALA MET VAL PRO LEU CYS TRP ALA LEU GLN
SEQRES 3 A 387 ALA SER GLY HIS GLU VAL LEU ILE ALA ALA PRO PRO GLU
SEQRES 4 A 387 LEU GLN ALA THR ALA HIS GLY ALA GLY LEU THR THR ALA
SEQRES 5 A 387 GLY ILE ARG GLY ASN ASP ARG THR GLY ASP THR GLY GLY
SEQRES 6 A 387 THR THR GLN LEU ARG PHE PRO ASN PRO ALA PHE GLY GLN
SEQRES 7 A 387 ARG ASP THR GLU ALA GLY ARG GLN LEU TRP GLU GLN THR
SEQRES 8 A 387 ALA SER ASN VAL ALA GLN SER SER LEU ASP GLN LEU PRO
SEQRES 9 A 387 GLU TYR LEU ARG LEU ALA GLU ALA TRP ARG PRO SER VAL
SEQRES 10 A 387 LEU LEU VAL ASP VAL CYS ALA LEU ILE GLY ARG VAL LEU
SEQRES 11 A 387 GLY GLY LEU LEU ASP LEU PRO VAL VAL LEU HIS ARG TRP
SEQRES 12 A 387 GLY VAL ASP PRO THR ALA GLY PRO PHE SER ASP ARG ALA
SEQRES 13 A 387 HIS GLU LEU LEU ASP PRO VAL CYS ARG HIS HIS GLY LEU
SEQRES 14 A 387 THR GLY LEU PRO THR PRO GLU LEU ILE LEU ASP PRO CYS
SEQRES 15 A 387 PRO PRO SER LEU GLN ALA SER ASP ALA PRO GLN GLY ALA
SEQRES 16 A 387 PRO VAL GLN TYR VAL PRO TYR ASN GLY SER GLY ALA PHE
SEQRES 17 A 387 PRO ALA TRP GLY ALA ALA ARG THR SER ALA ARG ARG VAL
SEQRES 18 A 387 CYS ILE CYS MET GLY ARG MET VAL LEU ASN ALA THR GLY
SEQRES 19 A 387 PRO ALA PRO LEU LEU ARG ALA VAL ALA ALA ALA THR GLU
SEQRES 20 A 387 LEU PRO GLY VAL GLU ALA VAL ILE ALA VAL PRO PRO GLU
SEQRES 21 A 387 HIS ARG ALA LEU LEU THR ASP LEU PRO ASP ASN ALA ARG
SEQRES 22 A 387 ILE ALA GLU SER VAL PRO LEU ASN LEU PHE LEU ARG THR
SEQRES 23 A 387 CYS GLU LEU VAL ILE CYS ALA GLY GLY SER GLY THR ALA
SEQRES 24 A 387 PHE THR ALA THR ARG LEU GLY ILE PRO GLN LEU VAL LEU
SEQRES 25 A 387 PRO GLN TYR PHE ASP GLN PHE ASP TYR ALA ARG ASN LEU
SEQRES 26 A 387 ALA ALA ALA GLY ALA GLY ILE CYS LEU PRO ASP GLU GLN
SEQRES 27 A 387 ALA GLN SER ASP HIS GLU GLN PHE THR ASP SER ILE ALA
SEQRES 28 A 387 THR VAL LEU GLY ASP THR GLY PHE ALA ALA ALA ALA ILE
SEQRES 29 A 387 LYS LEU SER ASP GLU ILE THR ALA MET PRO HIS PRO ALA
SEQRES 30 A 387 ALA LEU VAL ARG THR LEU GLU ASN THR ALA
SEQRES 1 B 387 HIS MET ARG VAL LEU VAL VAL PRO LEU PRO TYR PRO THR
SEQRES 2 B 387 HIS LEU MET ALA MET VAL PRO LEU CYS TRP ALA LEU GLN
SEQRES 3 B 387 ALA SER GLY HIS GLU VAL LEU ILE ALA ALA PRO PRO GLU
SEQRES 4 B 387 LEU GLN ALA THR ALA HIS GLY ALA GLY LEU THR THR ALA
SEQRES 5 B 387 GLY ILE ARG GLY ASN ASP ARG THR GLY ASP THR GLY GLY
SEQRES 6 B 387 THR THR GLN LEU ARG PHE PRO ASN PRO ALA PHE GLY GLN
SEQRES 7 B 387 ARG ASP THR GLU ALA GLY ARG GLN LEU TRP GLU GLN THR
SEQRES 8 B 387 ALA SER ASN VAL ALA GLN SER SER LEU ASP GLN LEU PRO
SEQRES 9 B 387 GLU TYR LEU ARG LEU ALA GLU ALA TRP ARG PRO SER VAL
SEQRES 10 B 387 LEU LEU VAL ASP VAL CYS ALA LEU ILE GLY ARG VAL LEU
SEQRES 11 B 387 GLY GLY LEU LEU ASP LEU PRO VAL VAL LEU HIS ARG TRP
SEQRES 12 B 387 GLY VAL ASP PRO THR ALA GLY PRO PHE SER ASP ARG ALA
SEQRES 13 B 387 HIS GLU LEU LEU ASP PRO VAL CYS ARG HIS HIS GLY LEU
SEQRES 14 B 387 THR GLY LEU PRO THR PRO GLU LEU ILE LEU ASP PRO CYS
SEQRES 15 B 387 PRO PRO SER LEU GLN ALA SER ASP ALA PRO GLN GLY ALA
SEQRES 16 B 387 PRO VAL GLN TYR VAL PRO TYR ASN GLY SER GLY ALA PHE
SEQRES 17 B 387 PRO ALA TRP GLY ALA ALA ARG THR SER ALA ARG ARG VAL
SEQRES 18 B 387 CYS ILE CYS MET GLY ARG MET VAL LEU ASN ALA THR GLY
SEQRES 19 B 387 PRO ALA PRO LEU LEU ARG ALA VAL ALA ALA ALA THR GLU
SEQRES 20 B 387 LEU PRO GLY VAL GLU ALA VAL ILE ALA VAL PRO PRO GLU
SEQRES 21 B 387 HIS ARG ALA LEU LEU THR ASP LEU PRO ASP ASN ALA ARG
SEQRES 22 B 387 ILE ALA GLU SER VAL PRO LEU ASN LEU PHE LEU ARG THR
SEQRES 23 B 387 CYS GLU LEU VAL ILE CYS ALA GLY GLY SER GLY THR ALA
SEQRES 24 B 387 PHE THR ALA THR ARG LEU GLY ILE PRO GLN LEU VAL LEU
SEQRES 25 B 387 PRO GLN TYR PHE ASP GLN PHE ASP TYR ALA ARG ASN LEU
SEQRES 26 B 387 ALA ALA ALA GLY ALA GLY ILE CYS LEU PRO ASP GLU GLN
SEQRES 27 B 387 ALA GLN SER ASP HIS GLU GLN PHE THR ASP SER ILE ALA
SEQRES 28 B 387 THR VAL LEU GLY ASP THR GLY PHE ALA ALA ALA ALA ILE
SEQRES 29 B 387 LYS LEU SER ASP GLU ILE THR ALA MET PRO HIS PRO ALA
SEQRES 30 B 387 ALA LEU VAL ARG THR LEU GLU ASN THR ALA
HET TYD A 401 25
HET MG A 402 1
HET TYD B 401 25
HET GLC B 402 12
HET MG B 403 1
HETNAM TYD THYMIDINE-5'-DIPHOSPHATE
HETNAM MG MAGNESIUM ION
HETNAM GLC ALPHA-D-GLUCOPYRANOSE
HETSYN GLC ALPHA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
FORMUL 3 TYD 2(C10 H16 N2 O11 P2)
FORMUL 4 MG 2(MG 2+)
FORMUL 6 GLC C6 H12 O6
FORMUL 8 HOH *417(H2 O)
HELIX 1 1 TYR A 10 ALA A 16 1 7
HELIX 2 2 MET A 17 SER A 27 1 11
HELIX 3 3 PRO A 36 GLU A 38 5 3
HELIX 4 4 LEU A 39 ALA A 46 1 8
HELIX 5 5 ASN A 72 GLN A 77 5 6
HELIX 6 6 THR A 80 ARG A 113 1 34
HELIX 7 7 ALA A 123 LEU A 133 1 11
HELIX 8 8 GLY A 149 HIS A 166 1 18
HELIX 9 9 PRO A 182 GLN A 186 5 5
HELIX 10 10 PRO A 208 ALA A 212 5 5
HELIX 11 11 GLY A 225 GLY A 233 1 9
HELIX 12 12 PRO A 234 LEU A 247 1 14
HELIX 13 13 PRO A 257 LEU A 264 5 8
HELIX 14 14 PRO A 278 CYS A 286 5 9
HELIX 15 15 GLY A 294 LEU A 304 1 11
HELIX 16 16 ASP A 316 ALA A 327 1 12
HELIX 17 17 ASP A 335 SER A 340 1 6
HELIX 18 18 ASP A 341 GLY A 354 1 14
HELIX 19 19 THR A 356 ALA A 371 1 16
HELIX 20 20 HIS A 374 THR A 385 1 12
HELIX 21 21 TYR B 10 ALA B 16 1 7
HELIX 22 22 MET B 17 SER B 27 1 11
HELIX 23 23 PRO B 36 ALA B 46 1 11
HELIX 24 24 ASN B 72 GLN B 77 5 6
HELIX 25 25 THR B 80 ARG B 113 1 34
HELIX 26 26 ALA B 123 ASP B 134 1 12
HELIX 27 27 GLY B 149 HIS B 166 1 18
HELIX 28 28 PRO B 182 GLN B 186 5 5
HELIX 29 29 PRO B 208 ALA B 212 5 5
HELIX 30 30 GLY B 225 GLY B 233 1 9
HELIX 31 31 PRO B 234 LEU B 247 1 14
HELIX 32 32 PRO B 257 LEU B 264 5 8
HELIX 33 33 PRO B 278 CYS B 286 5 9
HELIX 34 34 GLY B 294 LEU B 304 1 11
HELIX 35 35 ASP B 316 ALA B 327 1 12
HELIX 36 36 ASP B 335 SER B 340 1 6
HELIX 37 37 ASP B 341 ASP B 355 1 15
HELIX 38 38 THR B 356 ALA B 371 1 16
HELIX 39 39 HIS B 374 ASN B 384 1 11
SHEET 1 A 8 ALA A 194 PRO A 195 0
SHEET 2 A 8 LEU A 176 ASP A 179 1 N ILE A 177 O ALA A 194
SHEET 3 A 8 VAL A 137 HIS A 140 1 N LEU A 139 O LEU A 178
SHEET 4 A 8 VAL A 116 ASP A 120 1 N LEU A 117 O VAL A 138
SHEET 5 A 8 ARG A 2 VAL A 6 1 N VAL A 6 O LEU A 118
SHEET 6 A 8 GLU A 30 ALA A 35 1 O GLU A 30 N VAL A 3
SHEET 7 A 8 THR A 49 GLY A 52 1 O THR A 49 N ILE A 33
SHEET 8 A 8 GLY B 205 ALA B 206 1 O GLY B 205 N THR A 50
SHEET 1 B 8 GLY A 205 ALA A 206 0
SHEET 2 B 8 THR B 49 GLY B 52 1 O THR B 50 N GLY A 205
SHEET 3 B 8 GLU B 30 ALA B 35 1 N ILE B 33 O ALA B 51
SHEET 4 B 8 ARG B 2 VAL B 6 1 N VAL B 5 O LEU B 32
SHEET 5 B 8 VAL B 116 ASP B 120 1 O LEU B 118 N VAL B 6
SHEET 6 B 8 VAL B 137 HIS B 140 1 O VAL B 138 N LEU B 117
SHEET 7 B 8 LEU B 176 ASP B 179 1 O LEU B 178 N LEU B 139
SHEET 8 B 8 ALA B 194 PRO B 195 1 O ALA B 194 N ILE B 177
SHEET 1 C 6 ALA A 271 GLU A 275 0
SHEET 2 C 6 VAL A 250 VAL A 256 1 N ILE A 254 O ARG A 272
SHEET 3 C 6 ARG A 218 CYS A 223 1 N VAL A 220 O VAL A 253
SHEET 4 C 6 LEU A 288 CYS A 291 1 O ILE A 290 N CYS A 221
SHEET 5 C 6 GLN A 308 VAL A 310 1 O LEU A 309 N VAL A 289
SHEET 6 C 6 GLY A 330 CYS A 332 1 O ILE A 331 N VAL A 310
SHEET 1 D 6 ARG B 272 GLU B 275 0
SHEET 2 D 6 VAL B 250 VAL B 256 1 N ILE B 254 O ARG B 272
SHEET 3 D 6 ARG B 218 CYS B 223 1 N VAL B 220 O VAL B 253
SHEET 4 D 6 LEU B 288 CYS B 291 1 O ILE B 290 N CYS B 221
SHEET 5 D 6 GLN B 308 VAL B 310 1 O LEU B 309 N VAL B 289
SHEET 6 D 6 GLY B 330 CYS B 332 1 O ILE B 331 N VAL B 310
LINK MG MG A 402 O HOH A 541 1555 1555 2.10
LINK MG MG A 402 O HOH A 582 1555 1555 1.95
LINK MG MG A 402 O HOH A 597 1555 1555 2.17
LINK MG MG A 402 O HOH A 703 1555 1555 1.92
CISPEP 1 PHE A 70 PRO A 71 0 -9.17
CISPEP 2 PHE B 70 PRO B 71 0 -0.10
CRYST1 54.152 57.629 68.203 81.63 73.79 85.74 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 0.018467 -0.001376 -0.005234 0.00000
SCALE2 0.000000 0.017400 -0.002288 0.00000
SCALE3 0.000000 0.000000 0.015401 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
