HEADER TRANSPORT PROTEIN 26-APR-12 4EVR
TITLE CRYSTAL STRUCTURE OF ABC TRANSPORTER FROM R. PALUSTRIS - SOLUTE
TITLE 2 BINDING PROTEIN (RPA0668) IN COMPLEX WITH BENZOATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE ABC TRANSPORTER SUBUNIT, SUBSTRATE-BINDING
COMPND 3 COMPONENT;
COMPND 4 CHAIN: A;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOPSEUDOMONAS PALUSTRIS;
SOURCE 3 ORGANISM_TAXID: 258594;
SOURCE 4 STRAIN: CGA009;
SOURCE 5 GENE: HBAE, RPA0668;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)MAGIC;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS STRUCTURAL GENOMICS, PSI-BIOLOGY, MIDWEST CENTER FOR STRUCTURAL
KEYWDS 2 GENOMICS, MCSG, ABC TRANSPORTER, SOLUTE BINDING PROTEIN, BENZOATE-
KEYWDS 3 DERIVATIVES BINDING, TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR K.MICHALSKA,J.C.MACK,S.ZERBS,F.R.COLLART,A.JOACHIMIAK,MIDWEST CENTER
AUTHOR 2 FOR STRUCTURAL GENOMICS (MCSG)
REVDAT 3 09-JAN-13 4EVR 1 JRNL
REVDAT 2 05-SEP-12 4EVR 1 JRNL
REVDAT 1 23-MAY-12 4EVR 0
JRNL AUTH K.MICHALSKA,C.CHANG,J.C.MACK,S.ZERBS,A.JOACHIMIAK,
JRNL AUTH 2 F.R.COLLART
JRNL TITL CHARACTERIZATION OF TRANSPORT PROTEINS FOR AROMATIC
JRNL TITL 2 COMPOUNDS DERIVED FROM LIGNIN: BENZOATE DERIVATIVE BINDING
JRNL TITL 3 PROTEINS.
JRNL REF J.MOL.BIOL. V. 423 555 2012
JRNL REFN ISSN 0022-2836
JRNL PMID 22925578
JRNL DOI 10.1016/J.JMB.2012.08.017
REMARK 2
REMARK 2 RESOLUTION. 1.84 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.0
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.84
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 22.62
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 3 NUMBER OF REFLECTIONS : 28268
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) : 0.152
REMARK 3 R VALUE (WORKING SET) : 0.150
REMARK 3 FREE R VALUE : 0.185
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 1428
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 14
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.84
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.91
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.57
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2627
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.1785
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2506
REMARK 3 BIN R VALUE (WORKING SET) : 0.1766
REMARK 3 BIN FREE R VALUE : 0.2171
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.61
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 121
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2633
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 9
REMARK 3 SOLVENT ATOMS : 174
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.75
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.72660
REMARK 3 B22 (A**2) : 0.02600
REMARK 3 B33 (A**2) : -5.75250
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.20
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.19
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.942
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 5380 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 9777 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1485 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 55 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 784 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 5380 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 355 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 5893 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.015
REMARK 3 BOND ANGLES (DEGREES) : 1.23
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 4.45
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 2.83
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: {A|32 - A|79}
REMARK 3 ORIGIN FOR THE GROUP (A): 28.8927 27.1843 4.5292
REMARK 3 T TENSOR
REMARK 3 T11: 0.0155 T22: -0.1058
REMARK 3 T33: 0.0126 T12: -0.0060
REMARK 3 T13: 0.0551 T23: -0.0134
REMARK 3 L TENSOR
REMARK 3 L11: 1.5851 L22: 1.2066
REMARK 3 L33: 1.8273 L12: 0.0868
REMARK 3 L13: -0.6123 L23: 0.1591
REMARK 3 S TENSOR
REMARK 3 S11: -0.1268 S12: 0.0844 S13: -0.5144
REMARK 3 S21: -0.0601 S22: -0.0980 S23: 0.0514
REMARK 3 S31: 0.4127 S32: 0.0057 S33: 0.2248
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: {A|80 - A|95}
REMARK 3 ORIGIN FOR THE GROUP (A): 15.8212 24.2958 14.3606
REMARK 3 T TENSOR
REMARK 3 T11: 0.0234 T22: -0.1143
REMARK 3 T33: 0.1054 T12: -0.1171
REMARK 3 T13: 0.1476 T23: 0.0194
REMARK 3 L TENSOR
REMARK 3 L11: 0.0332 L22: 2.8756
REMARK 3 L33: 0.0000 L12: 2.3969
REMARK 3 L13: 1.0709 L23: -0.0719
REMARK 3 S TENSOR
REMARK 3 S11: -0.0639 S12: -0.1583 S13: -0.5227
REMARK 3 S21: 0.0799 S22: -0.1224 S23: 0.0924
REMARK 3 S31: 0.2719 S32: -0.4166 S33: 0.1863
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: {A|96 - A|155}
REMARK 3 ORIGIN FOR THE GROUP (A): 27.2044 26.3342 19.8909
REMARK 3 T TENSOR
REMARK 3 T11: 0.0317 T22: -0.0887
REMARK 3 T33: -0.0351 T12: -0.0027
REMARK 3 T13: 0.0722 T23: 0.1134
REMARK 3 L TENSOR
REMARK 3 L11: 2.5479 L22: 0.4552
REMARK 3 L33: 2.3925 L12: -0.2326
REMARK 3 L13: -0.4649 L23: 0.0086
REMARK 3 S TENSOR
REMARK 3 S11: -0.1377 S12: -0.4876 S13: -0.5442
REMARK 3 S21: 0.2054 S22: -0.0421 S23: 0.0882
REMARK 3 S31: 0.5442 S32: 0.0695 S33: 0.1799
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: {A|156 - A|174}
REMARK 3 ORIGIN FOR THE GROUP (A): 30.6147 54.1623 28.0121
REMARK 3 T TENSOR
REMARK 3 T11: 0.0082 T22: 0.0824
REMARK 3 T33: -0.0786 T12: -0.1071
REMARK 3 T13: 0.0255 T23: -0.1520
REMARK 3 L TENSOR
REMARK 3 L11: 0.8962 L22: 1.6664
REMARK 3 L33: 3.2431 L12: -1.1761
REMARK 3 L13: -0.3431 L23: -0.2521
REMARK 3 S TENSOR
REMARK 3 S11: 0.0042 S12: -0.5427 S13: 0.3066
REMARK 3 S21: 0.2955 S22: -0.0242 S23: -0.1069
REMARK 3 S31: -0.3396 S32: 0.2916 S33: 0.0201
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: {A|175 - A|224}
REMARK 3 ORIGIN FOR THE GROUP (A): 19.4718 50.3573 26.1253
REMARK 3 T TENSOR
REMARK 3 T11: -0.0282 T22: 0.0383
REMARK 3 T33: -0.0694 T12: -0.0465
REMARK 3 T13: 0.0619 T23: -0.1149
REMARK 3 L TENSOR
REMARK 3 L11: 1.9080 L22: 0.7719
REMARK 3 L33: 1.6100 L12: 0.0207
REMARK 3 L13: -0.7506 L23: -0.1690
REMARK 3 S TENSOR
REMARK 3 S11: 0.1026 S12: -0.5442 S13: 0.3205
REMARK 3 S21: 0.2463 S22: -0.0724 S23: 0.1666
REMARK 3 S31: -0.1844 S32: -0.0334 S33: -0.0302
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: {A|225 - A|292}
REMARK 3 ORIGIN FOR THE GROUP (A): 28.7433 50.7826 13.1026
REMARK 3 T TENSOR
REMARK 3 T11: -0.0239 T22: -0.0623
REMARK 3 T33: -0.0096 T12: -0.0290
REMARK 3 T13: 0.0157 T23: -0.0338
REMARK 3 L TENSOR
REMARK 3 L11: 2.0826 L22: 0.7757
REMARK 3 L33: 1.0238 L12: 0.1569
REMARK 3 L13: -0.5717 L23: 0.1098
REMARK 3 S TENSOR
REMARK 3 S11: 0.1123 S12: -0.2317 S13: 0.3447
REMARK 3 S21: 0.0592 S22: -0.0743 S23: 0.0571
REMARK 3 S31: -0.1726 S32: 0.1261 S33: -0.0380
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: {A|293 - A|358}
REMARK 3 ORIGIN FOR THE GROUP (A): 38.4803 28.5140 11.3153
REMARK 3 T TENSOR
REMARK 3 T11: -0.0278 T22: -0.0829
REMARK 3 T33: -0.0175 T12: 0.0563
REMARK 3 T13: 0.0344 T23: 0.0655
REMARK 3 L TENSOR
REMARK 3 L11: 1.9750 L22: 0.5175
REMARK 3 L33: 2.7643 L12: 0.1086
REMARK 3 L13: -0.4656 L23: -0.2765
REMARK 3 S TENSOR
REMARK 3 S11: -0.0909 S12: -0.2051 S13: -0.4845
REMARK 3 S21: 0.0668 S22: -0.0839 S23: -0.0050
REMARK 3 S31: 0.4728 S32: 0.3654 S33: 0.1748
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: {A|359 - A|391}
REMARK 3 ORIGIN FOR THE GROUP (A): 38.0177 43.9558 20.4809
REMARK 3 T TENSOR
REMARK 3 T11: -0.0685 T22: 0.0382
REMARK 3 T33: -0.1350 T12: -0.0442
REMARK 3 T13: -0.0016 T23: -0.0186
REMARK 3 L TENSOR
REMARK 3 L11: 2.7885 L22: 5.4751
REMARK 3 L33: 2.3212 L12: -1.1336
REMARK 3 L13: 0.3428 L23: -2.8197
REMARK 3 S TENSOR
REMARK 3 S11: 0.0606 S12: -0.5219 S13: 0.0310
REMARK 3 S21: 0.4130 S22: -0.1629 S23: -0.1510
REMARK 3 S31: -0.1375 S32: 0.4414 S33: 0.1023
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGEN ATOMS HAVE BEEN ADDED AT
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 4EVR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAY-12.
REMARK 100 THE RCSB ID CODE IS RCSB072129.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-FEB-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97929
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28325
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.840
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 200 DATA REDUNDANCY : 5.300
REMARK 200 R MERGE (I) : 0.09800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.3000
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) : 1.88
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 5.20
REMARK 200 R MERGE FOR SHELL (I) : 0.77400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.050
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELX, MLPHARE, DM, ARP/WARP, COOT
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE, 25% PEG4000, 8%
REMARK 280 2-PROPANOL, 5 MM SODIUM BENZOATE, PH 8.0, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 297K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 21.15300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 66.94450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 28.88900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 66.94450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.15300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 28.88900
REMARK 290 SMTRY3 4 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: 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 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 SER A 18
REMARK 465 ASN A 19
REMARK 465 ALA A 20
REMARK 465 GLY A 21
REMARK 465 PRO A 22
REMARK 465 PHE A 23
REMARK 465 ILE A 24
REMARK 465 ARG A 25
REMARK 465 PRO A 26
REMARK 465 SER A 27
REMARK 465 TYR A 28
REMARK 465 ALA A 29
REMARK 465 GLN A 30
REMARK 465 ALA A 31
REMARK 465 SER A 392
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 ASN A 130 -63.47 -157.32
REMARK 500 ALA A 131 118.73 -38.55
REMARK 500 ARG A 138 -109.99 -134.10
REMARK 500 SER A 149 -91.68 -105.06
REMARK 500 LYS A 201 146.60 -170.82
REMARK 500 PRO A 208 40.30 -102.33
REMARK 500 HIS A 356 34.61 72.45
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEZ A 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4EVQ RELATED DB: PDB
REMARK 900 RELATED ID: MCSG-APC102204 RELATED DB: TARGETTRACK
DBREF 4EVR A 21 392 UNP G3XCQ4 G3XCQ4_RHOPA 21 392
SEQADV 4EVR SER A 18 UNP G3XCQ4 EXPRESSION TAG
SEQADV 4EVR ASN A 19 UNP G3XCQ4 EXPRESSION TAG
SEQADV 4EVR ALA A 20 UNP G3XCQ4 EXPRESSION TAG
SEQRES 1 A 375 SER ASN ALA GLY PRO PHE ILE ARG PRO SER TYR ALA GLN
SEQRES 2 A 375 ALA GLY ALA LEU LYS VAL GLY LEU LEU LEU PRO TYR SER
SEQRES 3 A 375 GLY THR TYR ALA PRO LEU GLY GLU ALA ILE THR ARG GLY
SEQRES 4 A 375 LEU GLU LEU TYR VAL GLN SER GLN GLY GLY LYS LEU GLY
SEQRES 5 A 375 GLY ARG SER ILE SER PHE VAL LYS VAL ASP ASP GLU SER
SEQRES 6 A 375 ALA PRO PRO LYS ALA THR GLU LEU THR THR LYS LEU ILE
SEQRES 7 A 375 GLN SER GLU LYS ALA ASP VAL LEU ILE GLY THR VAL HIS
SEQRES 8 A 375 SER GLY VAL ALA MSE ALA MSE VAL LYS ILE ALA ARG GLU
SEQRES 9 A 375 ASP GLY ILE PRO THR ILE VAL PRO ASN ALA GLY ALA ASP
SEQRES 10 A 375 ILE ILE THR ARG ALA MSE CYS ALA PRO ASN VAL PHE ARG
SEQRES 11 A 375 THR SER PHE ALA ASN GLY GLN ILE GLY ARG ALA THR GLY
SEQRES 12 A 375 ASP ALA MSE ILE LYS ALA GLY LEU LYS LYS ALA VAL THR
SEQRES 13 A 375 VAL THR TRP LYS TYR ALA ALA GLY GLU GLU MSE VAL SER
SEQRES 14 A 375 GLY PHE LYS LYS SER PHE THR ALA GLY LYS GLY GLU VAL
SEQRES 15 A 375 VAL LYS ASP ILE THR ILE ALA PHE PRO ASP VAL GLU PHE
SEQRES 16 A 375 GLN SER ALA LEU ALA GLU ILE ALA SER LEU LYS PRO ASP
SEQRES 17 A 375 CYS VAL TYR ALA PHE PHE SER GLY GLY GLY ALA LEU LYS
SEQRES 18 A 375 PHE ILE LYS ASP TYR ALA ALA ALA ASN LEU GLY ILE PRO
SEQRES 19 A 375 LEU TRP GLY PRO GLY PHE LEU THR ASP GLY VAL GLU ALA
SEQRES 20 A 375 ALA ALA GLY PRO ALA GLY ASP GLY ILE LYS THR VAL LEU
SEQRES 21 A 375 HIS TYR VAL SER ASP LEU ASP ASN ALA GLU ASN GLN ALA
SEQRES 22 A 375 PHE VAL LYS SER PHE GLU ALA ALA TYR LYS ILE PRO PRO
SEQRES 23 A 375 ASP VAL PHE ALA VAL GLN GLY TRP ASP ALA GLY GLN LEU
SEQRES 24 A 375 LEU ASP ALA GLY VAL LYS ALA VAL GLY GLY ASP VAL ALA
SEQRES 25 A 375 LYS ARG LYS GLU LEU ASN ALA ALA MSE ALA ALA ALA SER
SEQRES 26 A 375 PHE ALA SER PRO ARG GLY PRO PHE LYS LEU SER ALA ALA
SEQRES 27 A 375 HIS ASN PRO VAL GLN ASN PHE TYR LEU ARG GLU LEU LYS
SEQRES 28 A 375 GLY GLY LYS SER VAL ASN LEU GLY LEU ALA ALA PRO ALA
SEQRES 29 A 375 VAL ALA ASP GLU ALA ILE GLY CYS LYS LEU SER
MODRES 4EVR MSE A 113 MET SELENOMETHIONINE
MODRES 4EVR MSE A 115 MET SELENOMETHIONINE
MODRES 4EVR MSE A 140 MET SELENOMETHIONINE
MODRES 4EVR MSE A 163 MET SELENOMETHIONINE
MODRES 4EVR MSE A 184 MET SELENOMETHIONINE
MODRES 4EVR MSE A 338 MET SELENOMETHIONINE
HET MSE A 113 8
HET MSE A 115 8
HET MSE A 140 8
HET MSE A 163 8
HET MSE A 184 8
HET MSE A 338 8
HET BEZ A 401 9
HETNAM MSE SELENOMETHIONINE
HETNAM BEZ BENZOIC ACID
FORMUL 1 MSE 6(C5 H11 N O2 SE)
FORMUL 2 BEZ C7 H6 O2
FORMUL 3 HOH *174(H2 O)
HELIX 1 1 TYR A 46 GLN A 64 1 19
HELIX 2 2 ALA A 83 SER A 97 1 15
HELIX 3 3 HIS A 108 GLY A 123 1 16
HELIX 4 4 ALA A 133 ARG A 138 5 6
HELIX 5 5 ALA A 151 ALA A 166 1 16
HELIX 6 6 TYR A 178 GLY A 195 1 18
HELIX 7 7 PHE A 212 LYS A 223 1 12
HELIX 8 8 GLY A 233 ALA A 246 1 14
HELIX 9 9 PHE A 257 THR A 259 5 3
HELIX 10 10 VAL A 262 GLY A 267 1 6
HELIX 11 11 PRO A 268 ASP A 271 5 4
HELIX 12 12 ASN A 285 LYS A 300 1 16
HELIX 13 13 ASP A 304 VAL A 324 1 21
HELIX 14 14 LYS A 330 ALA A 340 1 11
SHEET 1 A 6 LYS A 67 LEU A 68 0
SHEET 2 A 6 ARG A 71 ASP A 79 -1 O ARG A 71 N LEU A 68
SHEET 3 A 6 LEU A 34 LEU A 40 1 N LEU A 38 O VAL A 76
SHEET 4 A 6 VAL A 102 GLY A 105 1 O VAL A 102 N GLY A 37
SHEET 5 A 6 THR A 126 VAL A 128 1 O ILE A 127 N LEU A 103
SHEET 6 A 6 VAL A 145 ARG A 147 1 O PHE A 146 N VAL A 128
SHEET 1 B 7 GLU A 198 ILE A 205 0
SHEET 2 B 7 LYS A 170 TRP A 176 1 N THR A 173 O ILE A 203
SHEET 3 B 7 CYS A 226 PHE A 230 1 O TYR A 228 N VAL A 174
SHEET 4 B 7 LEU A 252 PRO A 255 1 O TRP A 253 N VAL A 227
SHEET 5 B 7 LYS A 274 LEU A 277 1 O LYS A 274 N LEU A 252
SHEET 6 B 7 PHE A 362 LYS A 368 -1 O ARG A 365 N THR A 275
SHEET 7 B 7 LYS A 371 ALA A 379 -1 O VAL A 373 N GLU A 366
SHEET 1 C 2 PHE A 343 SER A 345 0
SHEET 2 C 2 GLY A 348 PHE A 350 -1 O PHE A 350 N PHE A 343
SSBOND 1 CYS A 141 CYS A 389 1555 1555 2.05
LINK C ALA A 112 N MSE A 113 1555 1555 1.30
LINK C MSE A 113 N ALA A 114 1555 1555 1.35
LINK C ALA A 114 N MSE A 115 1555 1555 1.34
LINK C MSE A 115 N VAL A 116 1555 1555 1.34
LINK C ALA A 139 N MSE A 140 1555 1555 1.32
LINK C MSE A 140 N CYS A 141 1555 1555 1.38
LINK C ALA A 162 N MSE A 163 1555 1555 1.35
LINK C MSE A 163 N ILE A 164 1555 1555 1.33
LINK C GLU A 183 N MSE A 184 1555 1555 1.32
LINK C MSE A 184 N VAL A 185 1555 1555 1.36
LINK C ALA A 337 N MSE A 338 1555 1555 1.33
LINK C MSE A 338 N ALA A 339 1555 1555 1.36
CISPEP 1 GLY A 105 THR A 106 0 -2.34
CISPEP 2 PHE A 207 PRO A 208 0 -2.74
SITE 1 AC1 11 TYR A 46 LEU A 49 VAL A 107 HIS A 108
SITE 2 AC1 11 SER A 109 ASN A 130 ALA A 131 GLY A 132
SITE 3 AC1 11 TYR A 178 ALA A 180 MSE A 184
CRYST1 42.306 57.778 133.889 90.00 90.00 90.00 P 21 21 21 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 0.023637 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017308 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007469 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
