HEADER TRANSFERASE 26-SEP-13 4C7V
TITLE APO TRANSKETOLASE FROM LACTOBACILLUS SALIVARIUS AT 2.2A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSKETOLASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 2.2.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LACTOBACILLUS SALIVARIUS;
SOURCE 3 ORGANISM_TAXID: 362948;
SOURCE 4 STRAIN: UCC118;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: ROSETTA PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: POPINF
KEYWDS TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.M.C.LOBLEY,P.LUKACIK,M.BUMANN,P.ALLER,A.DOUANGAMATH,P.W.O'TOOLE,
AUTHOR 2 M.A.WALSH
REVDAT 3 21-OCT-15 4C7V 1 JRNL
REVDAT 2 14-OCT-15 4C7V 1 TITLE JRNL
REVDAT 1 08-OCT-14 4C7V 0
JRNL AUTH P.LUKACIK,C.M.C.LOBLEY,M.BUMANN,V.ARENA DE SOUZA,R.J.OWENS,
JRNL AUTH 2 P.W.O'TOOLE,M.A.WALSH
JRNL TITL HIGH RESOLUTION CRYSTAL STRUCTURES OF LACTOBACILLUS
JRNL TITL 2 SALIVARIUS TRANSKETOLASE IN THE PRESENCE AND ABSENCE OF
JRNL TITL 3 THIAMINE PYROPHOSPHATE
JRNL REF ACTA CRYSTALLOGR.,SECT.F V. 71 1327 2015
JRNL REFN ISSN 1744-3091
JRNL PMID 26457526
JRNL DOI 10.1107/S2053230X1501657X
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,
REMARK 3 STEINER,NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.14
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.57
REMARK 3 NUMBER OF REFLECTIONS : 32219
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) : 0.16524
REMARK 3 R VALUE (WORKING SET) : 0.16236
REMARK 3 FREE R VALUE : 0.21917
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.1
REMARK 3 FREE R VALUE TEST SET COUNT : 1720
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) : 2.200
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.257
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2360
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.92
REMARK 3 BIN R VALUE (WORKING SET) : 0.238
REMARK 3 BIN FREE R VALUE SET COUNT : 121
REMARK 3 BIN FREE R VALUE : 0.273
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5117
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 246
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.117
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.25
REMARK 3 B22 (A**2) : -0.25
REMARK 3 B33 (A**2) : 0.80
REMARK 3 B12 (A**2) : -0.25
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.257
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.200
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.145
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.233
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.969
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.947
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5234 ; 0.017 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4929 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7097 ; 1.780 ; 1.955
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11390 ; 0.873 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 671 ; 6.509 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 234 ;36.725 ;25.128
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 884 ;15.831 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;20.150 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 772 ; 0.101 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6007 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1157 ; 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): 2657 ; 2.539 ; 3.099
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2656 ; 2.537 ; 3.098
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3322 ; 3.499 ; 4.637
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2577 ; 3.220 ; 3.443
REMARK 3 SIDE-CHAIN ANGLE REFINED 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 : 5
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 1 A 188
REMARK 3 ORIGIN FOR THE GROUP (A): 7.7510 54.4680 -10.4400
REMARK 3 T TENSOR
REMARK 3 T11: 0.0254 T22: 0.1289
REMARK 3 T33: 0.1719 T12: 0.0139
REMARK 3 T13: -0.0451 T23: -0.0269
REMARK 3 L TENSOR
REMARK 3 L11: 0.7794 L22: 0.2795
REMARK 3 L33: 0.4693 L12: -0.0642
REMARK 3 L13: 0.1382 L23: 0.0394
REMARK 3 S TENSOR
REMARK 3 S11: 0.0014 S12: 0.0843 S13: -0.2610
REMARK 3 S21: -0.0773 S22: 0.0078 S23: 0.1702
REMARK 3 S31: -0.0469 S32: -0.2087 S33: -0.0092
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 : A 189 A 337
REMARK 3 ORIGIN FOR THE GROUP (A): 4.9600 49.2120 -11.7830
REMARK 3 T TENSOR
REMARK 3 T11: 0.0231 T22: 0.1424
REMARK 3 T33: 0.2210 T12: -0.0290
REMARK 3 T13: -0.0441 T23: -0.0457
REMARK 3 L TENSOR
REMARK 3 L11: 0.6318 L22: 0.5618
REMARK 3 L33: 0.5778 L12: -0.1816
REMARK 3 L13: 0.3180 L23: -0.0793
REMARK 3 S TENSOR
REMARK 3 S11: 0.0264 S12: 0.0482 S13: -0.2749
REMARK 3 S21: -0.0624 S22: 0.0180 S23: 0.1810
REMARK 3 S31: 0.0446 S32: -0.2080 S33: -0.0445
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 338 A 528
REMARK 3 ORIGIN FOR THE GROUP (A): 23.9320 62.2850 14.1250
REMARK 3 T TENSOR
REMARK 3 T11: 0.0513 T22: 0.0845
REMARK 3 T33: 0.0467 T12: 0.0394
REMARK 3 T13: 0.0125 T23: 0.0363
REMARK 3 L TENSOR
REMARK 3 L11: 0.4907 L22: 0.3302
REMARK 3 L33: 0.9637 L12: -0.0600
REMARK 3 L13: -0.0435 L23: 0.0116
REMARK 3 S TENSOR
REMARK 3 S11: -0.0550 S12: -0.1516 S13: -0.1176
REMARK 3 S21: 0.0269 S22: 0.0588 S23: 0.0786
REMARK 3 S31: -0.1625 S32: -0.0666 S33: -0.0039
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 529 A 637
REMARK 3 ORIGIN FOR THE GROUP (A): 40.2770 79.8550 13.5350
REMARK 3 T TENSOR
REMARK 3 T11: 0.2236 T22: 0.0747
REMARK 3 T33: 0.0340 T12: -0.0741
REMARK 3 T13: -0.0223 T23: -0.0249
REMARK 3 L TENSOR
REMARK 3 L11: 1.0997 L22: 1.0314
REMARK 3 L33: 1.0204 L12: -0.0080
REMARK 3 L13: -0.0429 L23: 0.2977
REMARK 3 S TENSOR
REMARK 3 S11: -0.0467 S12: -0.1546 S13: 0.1687
REMARK 3 S21: 0.0075 S22: 0.0779 S23: -0.0585
REMARK 3 S31: -0.3695 S32: 0.1622 S33: -0.0312
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 638 A 661
REMARK 3 ORIGIN FOR THE GROUP (A): 51.3300 67.8120 19.4190
REMARK 3 T TENSOR
REMARK 3 T11: 0.1718 T22: 0.2875
REMARK 3 T33: 0.0809 T12: -0.0590
REMARK 3 T13: -0.0649 T23: -0.0189
REMARK 3 L TENSOR
REMARK 3 L11: 1.3010 L22: 5.1223
REMARK 3 L33: 0.1911 L12: 0.0278
REMARK 3 L13: -0.3262 L23: -0.6004
REMARK 3 S TENSOR
REMARK 3 S11: -0.0879 S12: -0.2830 S13: 0.0021
REMARK 3 S21: 0.1590 S22: 0.0619 S23: -0.2573
REMARK 3 S31: -0.0334 S32: 0.1585 S33: 0.0261
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 ADDED IN THE
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 4C7V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-SEP-13.
REMARK 100 THE PDBE ID CODE IS EBI-58494.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-MAR-12
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 : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.917
REMARK 200 MONOCHROMATOR : DCM SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL (PILATUS 2M)
REMARK 200 DETECTOR MANUFACTURER : DECTRIS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33992
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.20
REMARK 200 RESOLUTION RANGE LOW (A) : 39.14
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NONE
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 6.6
REMARK 200 R MERGE (I) : 0.06
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.80
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.26
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.8
REMARK 200 R MERGE FOR SHELL (I) : 0.62
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.80
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: NULL
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 % W/V PEG3350, 0.2 M SODIUM
REMARK 280 CHLORIDE
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
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 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 129.67333
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 64.83667
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 64.83667
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 129.67333
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8000 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42580 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.4 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 350 BIOMT1 2 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 A2162 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 MET A -17
REMARK 465 ALA A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 GLU A -5
REMARK 465 VAL A -4
REMARK 465 LEU A -3
REMARK 465 PHE A -2
REMARK 465 GLN A -1
REMARK 465 GLY A 0
REMARK 465 LYS A 663
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 GLU A 237 O HOH A 2112 1.99
REMARK 500 O LYS A 574 N GLY A 576 1.89
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 51 C - N - CA ANGL. DEV. = 9.4 DEGREES
REMARK 500 ARG A 60 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ASP A 469 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ARG A 492 NE - CZ - NH1 ANGL. DEV. = 7.0 DEGREES
REMARK 500 ARG A 492 NE - CZ - NH2 ANGL. DEV. = -6.8 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 HIS A 54 -120.89 53.67
REMARK 500 ALA A 114 149.91 -174.15
REMARK 500 SER A 199 -12.36 -143.15
REMARK 500 TYR A 322 58.96 -112.71
REMARK 500 ASN A 335 31.64 72.65
REMARK 500 ASP A 380 40.03 33.63
REMARK 500 LYS A 386 63.84 78.37
REMARK 500 ILE A 476 -54.46 -130.58
REMARK 500 ASN A 549 -97.98 -107.20
REMARK 500 LYS A 574 -104.68 -58.67
REMARK 500 LYS A 575 2.58 -16.36
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE HIS TAG (THE FIRST 18 RESIDUES ABOVE) IS NOT VISIBLE
REMARK 999 IN THE ELECTRON DENSITY MAP
DBREF 4C7V A 2 663 UNP Q1WQU8 Q1WQU8_LACS1 2 663
SEQADV 4C7V MET A -17 UNP Q1WQU8 EXPRESSION TAG
SEQADV 4C7V ALA A -16 UNP Q1WQU8 EXPRESSION TAG
SEQADV 4C7V HIS A -15 UNP Q1WQU8 EXPRESSION TAG
SEQADV 4C7V HIS A -14 UNP Q1WQU8 EXPRESSION TAG
SEQADV 4C7V HIS A -13 UNP Q1WQU8 EXPRESSION TAG
SEQADV 4C7V HIS A -12 UNP Q1WQU8 EXPRESSION TAG
SEQADV 4C7V HIS A -11 UNP Q1WQU8 EXPRESSION TAG
SEQADV 4C7V HIS A -10 UNP Q1WQU8 EXPRESSION TAG
SEQADV 4C7V SER A -9 UNP Q1WQU8 EXPRESSION TAG
SEQADV 4C7V SER A -8 UNP Q1WQU8 EXPRESSION TAG
SEQADV 4C7V GLY A -7 UNP Q1WQU8 EXPRESSION TAG
SEQADV 4C7V LEU A -6 UNP Q1WQU8 EXPRESSION TAG
SEQADV 4C7V GLU A -5 UNP Q1WQU8 EXPRESSION TAG
SEQADV 4C7V VAL A -4 UNP Q1WQU8 EXPRESSION TAG
SEQADV 4C7V LEU A -3 UNP Q1WQU8 EXPRESSION TAG
SEQADV 4C7V PHE A -2 UNP Q1WQU8 EXPRESSION TAG
SEQADV 4C7V GLN A -1 UNP Q1WQU8 EXPRESSION TAG
SEQADV 4C7V GLY A 0 UNP Q1WQU8 EXPRESSION TAG
SEQADV 4C7V PRO A 1 UNP Q1WQU8 EXPRESSION TAG
SEQRES 1 A 681 MET ALA HIS HIS HIS HIS HIS HIS SER SER GLY LEU GLU
SEQRES 2 A 681 VAL LEU PHE GLN GLY PRO TYR ASP GLN VAL ASP GLN LEU
SEQRES 3 A 681 GLY VAL ASN THR LEU ARG THR LEU SER ILE ASP ALA ILE
SEQRES 4 A 681 GLN ARG ALA ASN SER GLY HIS PRO GLY LEU PRO MET GLY
SEQRES 5 A 681 ALA ALA PRO MET ALA TYR VAL LEU TRP THR ARG HIS LEU
SEQRES 6 A 681 LYS ILE ASN PRO LYS THR HIS MET ASN TRP VAL ASN ARG
SEQRES 7 A 681 ASP ARG PHE VAL LEU SER ALA GLY HIS GLY SER ALA LEU
SEQRES 8 A 681 LEU TYR SER LEU ALA HIS LEU ALA GLY TYR ASP VAL SER
SEQRES 9 A 681 MET ASP ASP LEU LYS ASN PHE ARG GLU TRP LYS SER ASN
SEQRES 10 A 681 THR PRO GLY HIS PRO GLU TYR GLY CYS THR ASP GLY VAL
SEQRES 11 A 681 GLU ALA THR THR GLY PRO LEU GLY GLN GLY ILE SER MET
SEQRES 12 A 681 ALA VAL GLY MET ALA MET ALA GLU ALA HIS LEU GLY LYS
SEQRES 13 A 681 LYS PHE ASN ARG GLU GLY TYR PRO VAL MET ASP HIS TYR
SEQRES 14 A 681 THR TYR ALA LEU ILE GLY ASP GLY ASP LEU MET GLU GLY
SEQRES 15 A 681 VAL ALA SER GLU ALA ALA SER LEU ALA GLY HIS LEU LYS
SEQRES 16 A 681 LEU GLY LYS LEU ILE ALA LEU TYR ASP SER ASN GLY ILE
SEQRES 17 A 681 SER LEU ASP GLY LYS THR SER ALA SER PHE THR GLU ASN
SEQRES 18 A 681 VAL GLY ALA ARG PHE GLU ALA TYR GLY TRP GLN TYR ILE
SEQRES 19 A 681 LEU VAL GLU ASP GLY PHE ASN LEU GLU GLU ILE ASP LYS
SEQRES 20 A 681 ALA ILE VAL GLN ALA LYS ALA GLU SER ASP LYS PRO THR
SEQRES 21 A 681 ILE ILE GLU ILE LYS THR THR ILE GLY TYR GLY SER GLU
SEQRES 22 A 681 ASN GLN GLY THR HIS LYS VAL HIS GLY SER PRO LEU GLY
SEQRES 23 A 681 GLU GLU GLY VAL ALA HIS ALA LYS GLU VAL TYR ASN TRP
SEQRES 24 A 681 ASN TYR PRO PRO PHE THR VAL PRO GLU GLU VAL SER GLN
SEQRES 25 A 681 ARG PHE LYS GLU CYS LEU GLN ASP LYS GLY VAL LYS ALA
SEQRES 26 A 681 GLU ASN LYS TRP ASN GLU MET PHE GLU ALA TYR LYS LYS
SEQRES 27 A 681 GLU TYR SER ASP LEU ALA GLN LYS PHE SER ASP GLY PHE
SEQRES 28 A 681 SER ASN LYS VAL PRO ASN THR LEU GLY ASP ILE LEU PRO
SEQRES 29 A 681 GLN TYR GLY GLU ASP ASP SER ILE ALA THR ARG ALA ALA
SEQRES 30 A 681 SER GLN LYS ALA ILE ASN ALA LEU ALA LYS GLU VAL SER
SEQRES 31 A 681 SER LEU TRP GLY GLY ALA ALA ASP LEU ALA SER SER ASN
SEQRES 32 A 681 LYS THR VAL ILE ALA GLY GLU GLY ASP PHE GLN PRO GLU
SEQRES 33 A 681 SER TYR GLU GLY ARG ASN ILE TRP PHE GLY VAL ARG GLU
SEQRES 34 A 681 PHE GLY MET ALA CYS ALA MET ASN GLY ILE MET LEU HIS
SEQRES 35 A 681 GLY GLY THR ARG ILE PHE GLY SER THR PHE PHE VAL PHE
SEQRES 36 A 681 SER ASP TYR LEU LYS ALA ALA ILE ARG LEU SER ALA ILE
SEQRES 37 A 681 GLN LYS LEU PRO VAL ILE TYR VAL LEU THR HIS ASP SER
SEQRES 38 A 681 VAL ALA VAL GLY LYS ASP GLY PRO THR HIS GLU PRO ILE
SEQRES 39 A 681 GLU GLN LEU ALA SER LEU ARG THR ILE PRO ASN VAL GLN
SEQRES 40 A 681 VAL PHE ARG PRO ALA ASP GLY ASN GLU THR SER ALA ALA
SEQRES 41 A 681 TRP LYS VAL ALA LEU GLU THR LEU ASP LYS PRO THR ILE
SEQRES 42 A 681 LEU VAL LEU SER ARG GLN ASN LEU ASP THR LEU PRO ILE
SEQRES 43 A 681 SER LYS GLU LYS VAL PHE ASP GLY VAL GLU LYS GLY GLY
SEQRES 44 A 681 TYR VAL VAL GLN GLY ALA GLU ASN GLU ALA ASP GLY ILE
SEQRES 45 A 681 LEU ILE ALA THR GLY SER GLU VAL GLY LEU ALA LEU LYS
SEQRES 46 A 681 ALA LYS GLU GLU LEU GLN LYS LYS GLY LYS ASP VAL ILE
SEQRES 47 A 681 VAL VAL SER LEU PRO SER TRP GLU ARG PHE GLU ALA GLN
SEQRES 48 A 681 SER GLU GLU TYR LYS ASN THR VAL ILE PRO PRO GLU LEU
SEQRES 49 A 681 LYS LYS ARG MET THR ILE GLU ALA GLY THR THR TYR GLY
SEQRES 50 A 681 TRP ALA LYS TYR ALA GLY ASP HIS GLY VAL MET ILE GLY
SEQRES 51 A 681 ILE ASP GLU PHE GLY MET SER ALA PRO SER ASP ILE VAL
SEQRES 52 A 681 LEU ARG GLU LEU GLY MET SER VAL GLU ASN ILE VAL ASP
SEQRES 53 A 681 LYS TYR LEU GLU LYS
FORMUL 2 HOH *246(H2 O)
HELIX 1 1 ASP A 3 ASN A 25 1 23
HELIX 2 2 PRO A 29 HIS A 46 1 18
HELIX 3 3 ASN A 50 HIS A 54 5 5
HELIX 4 4 ALA A 67 HIS A 69 5 3
HELIX 5 5 GLY A 70 GLY A 82 1 13
HELIX 6 6 SER A 86 LYS A 91 1 6
HELIX 7 7 GLY A 120 ASN A 141 1 22
HELIX 8 8 GLY A 157 GLU A 163 1 7
HELIX 9 9 GLU A 163 LEU A 176 1 14
HELIX 10 10 SER A 197 SER A 199 5 3
HELIX 11 11 ASN A 203 GLY A 212 1 10
HELIX 12 12 ASN A 223 GLU A 237 1 15
HELIX 13 13 THR A 259 HIS A 263 5 5
HELIX 14 14 GLY A 268 TYR A 279 1 12
HELIX 15 15 PRO A 289 LEU A 300 1 12
HELIX 16 16 LEU A 300 TYR A 322 1 23
HELIX 17 17 TYR A 322 ASN A 335 1 14
HELIX 18 18 THR A 340 LEU A 345 1 6
HELIX 19 19 THR A 356 VAL A 371 1 16
HELIX 20 20 LEU A 381 LYS A 386 1 6
HELIX 21 21 GLN A 396 TYR A 400 5 5
HELIX 22 22 ARG A 410 GLY A 425 1 16
HELIX 23 23 PHE A 437 GLN A 451 1 15
HELIX 24 24 SER A 463 GLY A 467 5 5
HELIX 25 25 GLY A 470 GLU A 474 5 5
HELIX 26 26 GLU A 477 THR A 484 1 8
HELIX 27 27 ASP A 495 THR A 509 1 15
HELIX 28 28 SER A 529 LYS A 539 1 11
HELIX 29 29 SER A 560 LYS A 575 1 16
HELIX 30 30 SER A 586 ALA A 592 1 7
HELIX 31 31 SER A 594 ILE A 602 1 9
HELIX 32 32 TRP A 620 GLY A 625 1 6
HELIX 33 33 PRO A 641 LEU A 649 1 9
HELIX 34 34 SER A 652 GLU A 662 1 11
SHEET 1 AA 5 ARG A 62 LEU A 65 0
SHEET 2 AA 5 THR A 152 ILE A 156 1 O TYR A 153 N VAL A 64
SHEET 3 AA 5 LEU A 181 SER A 187 1 O ILE A 182 N ALA A 154
SHEET 4 AA 5 THR A 242 LYS A 247 1 O THR A 242 N ALA A 183
SHEET 5 AA 5 GLN A 214 VAL A 218 1 O GLN A 214 N ILE A 243
SHEET 1 AB 2 ILE A 190 SER A 191 0
SHEET 2 AB 2 GLY A 194 LYS A 195 -1 O GLY A 194 N SER A 191
SHEET 1 AC 2 SER A 353 ALA A 355 0
SHEET 2 AC 2 ASN A 522 ASP A 524 -1 O LEU A 523 N ILE A 354
SHEET 1 AD 6 ASN A 404 TRP A 406 0
SHEET 2 AD 6 LEU A 374 ALA A 378 1 O GLY A 376 N ILE A 405
SHEET 3 AD 6 ARG A 428 PHE A 434 1 O ARG A 428 N TRP A 375
SHEET 4 AD 6 ILE A 456 THR A 460 1 O ILE A 456 N GLY A 431
SHEET 5 AD 6 THR A 514 VAL A 517 1 O THR A 514 N TYR A 457
SHEET 6 AD 6 GLN A 489 PHE A 491 1 O GLN A 489 N ILE A 515
SHEET 1 AE 5 TYR A 542 GLN A 545 0
SHEET 2 AE 5 VAL A 579 SER A 583 -1 O VAL A 581 N VAL A 544
SHEET 3 AE 5 GLY A 553 ALA A 557 1 O GLY A 553 N ILE A 580
SHEET 4 AE 5 ARG A 609 ILE A 612 1 O MET A 610 N ILE A 556
SHEET 5 AE 5 VAL A 629 ILE A 631 1 O VAL A 629 N THR A 611
CRYST1 76.150 76.150 194.510 90.00 90.00 120.00 P 32 2 1 6
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 0.013132 0.007582 0.000000 0.00000
SCALE2 0.000000 0.015164 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005141 0.00000
(ATOM LINES ARE NOT SHOWN.)
END