HEADER MEMBRANE PROTEIN 16-NOV-10 3AQP
TITLE CRYSTAL STRUCTURE OF SECDF, A TRANSLOCON-ASSOCIATED MEMBRANE PROTEIN,
TITLE 2 FROM THERMUS THRMOPHILUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE SECDF PROTEIN-EXPORT MEMBRANE PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 300852;
SOURCE 4 STRAIN: HB8;
SOURCE 5 GENE: SECDF, TTHA0697;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: AD202;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PTV118N
KEYWDS MEMBRANE PROTEIN, SECDF, SEC, TRANSLOCON, CELL MEMBRANE, MEMBRANE,
KEYWDS 2 PROTEIN TRANSPORT, TRANSLOCATION, TRANSMEMBRANE, TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR T.TSUKAZAKI,H.MORI,Y.ECHIZEN,R.ISHITANI,S.FUKAI,T.TANAKA,
AUTHOR 2 A.PEREDERINA,D.G.VASSYLYEV,T.KOHNO,K.ITO,O.NUREKI
REVDAT 3 13-MAR-24 3AQP 1 SEQADV
REVDAT 2 22-JAN-14 3AQP 1 JRNL VERSN
REVDAT 1 18-MAY-11 3AQP 0
JRNL AUTH T.TSUKAZAKI,H.MORI,Y.ECHIZEN,R.ISHITANI,S.FUKAI,T.TANAKA,
JRNL AUTH 2 A.PEREDERINA,D.G.VASSYLYEV,T.KOHNO,A.D.MATURANA,K.ITO,
JRNL AUTH 3 O.NUREKI
JRNL TITL STRUCTURE AND FUNCTION OF A MEMBRANE COMPONENT SECDF THAT
JRNL TITL 2 ENHANCES PROTEIN EXPORT
JRNL REF NATURE V. 474 235 2011
JRNL REFN ISSN 0028-0836
JRNL PMID 21562494
JRNL DOI 10.1038/NATURE09980
REMARK 2
REMARK 2 RESOLUTION. 3.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6_289)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : TWIN_LSQ_F
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.88
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.700
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.0
REMARK 3 NUMBER OF REFLECTIONS : 41834
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.299
REMARK 3 R VALUE (WORKING SET) : 0.298
REMARK 3 FREE R VALUE : 0.319
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.510
REMARK 3 FREE R VALUE TEST SET COUNT : 2304
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 23.1941 - 8.0297 0.88 2805 157 0.2691 0.2957
REMARK 3 2 8.0297 - 6.4179 0.95 2969 139 0.3039 0.3591
REMARK 3 3 6.4179 - 5.6198 0.93 2929 155 0.3546 0.3703
REMARK 3 4 5.6198 - 5.1120 0.92 2869 143 0.3244 0.3281
REMARK 3 5 5.1120 - 4.7489 0.92 2878 148 0.2995 0.2963
REMARK 3 6 4.7489 - 4.4710 0.89 2793 144 0.2726 0.3048
REMARK 3 7 4.4710 - 4.2486 0.89 2761 146 0.2743 0.2584
REMARK 3 8 4.2486 - 4.0646 0.87 2724 160 0.2765 0.3256
REMARK 3 9 4.0646 - 3.9089 0.82 2542 141 0.2735 0.2839
REMARK 3 10 3.9089 - 3.7746 0.80 2516 132 0.2865 0.3466
REMARK 3 11 3.7746 - 3.6571 0.79 2460 134 0.2951 0.3365
REMARK 3 12 3.6571 - 3.5529 0.75 2337 141 0.3026 0.3284
REMARK 3 13 3.5529 - 3.4597 0.76 2379 126 0.3063 0.3238
REMARK 3 14 3.4597 - 3.3755 0.76 2363 127 0.3337 0.3550
REMARK 3 15 3.3755 - 3.2990 0.76 2354 134 0.3412 0.3923
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.00
REMARK 3 B_SOL : 0.00
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.570
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.69460
REMARK 3 B22 (A**2) : -2.69460
REMARK 3 B33 (A**2) : 5.38910
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 TWINNING INFORMATION.
REMARK 3 FRACTION: 0.5010
REMARK 3 OPERATOR: H,-K,-L
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.015 11280
REMARK 3 ANGLE : 1.298 15244
REMARK 3 CHIRALITY : 0.074 1852
REMARK 3 PLANARITY : 0.005 1936
REMARK 3 DIHEDRAL : 18.111 4080
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 2:515 OR RESSEQ
REMARK 3 522:726 )
REMARK 3 SELECTION : CHAIN B AND (RESSEQ 2:515 OR RESSEQ
REMARK 3 522:726 )
REMARK 3 ATOM PAIRS NUMBER : 5514
REMARK 3 RMSD : 0.013
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3AQP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-NOV-10.
REMARK 100 THE DEPOSITION ID IS D_1000029576.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-OCT-08
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 : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41841
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: SAD
REMARK 200 SOFTWARE USED: MLPHARE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 75.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 26% PEG 400, 0.2M SODIUM ACETETE,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+3/4
REMARK 290 4555 Y,-X,Z+1/4
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 80.28150
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 120.42225
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 40.14075
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 GLN A 516
REMARK 465 ALA A 517
REMARK 465 PRO A 518
REMARK 465 THR A 519
REMARK 465 ALA A 520
REMARK 465 ALA A 521
REMARK 465 ARG A 727
REMARK 465 LYS A 728
REMARK 465 ALA A 729
REMARK 465 GLN A 730
REMARK 465 GLU A 731
REMARK 465 ALA A 732
REMARK 465 SER A 733
REMARK 465 LYS A 734
REMARK 465 ALA A 735
REMARK 465 HIS A 736
REMARK 465 HIS A 737
REMARK 465 HIS A 738
REMARK 465 HIS A 739
REMARK 465 HIS A 740
REMARK 465 HIS A 741
REMARK 465 MET B 1
REMARK 465 GLN B 516
REMARK 465 ALA B 517
REMARK 465 PRO B 518
REMARK 465 THR B 519
REMARK 465 ALA B 520
REMARK 465 ALA B 521
REMARK 465 ARG B 727
REMARK 465 LYS B 728
REMARK 465 ALA B 729
REMARK 465 GLN B 730
REMARK 465 GLU B 731
REMARK 465 ALA B 732
REMARK 465 SER B 733
REMARK 465 LYS B 734
REMARK 465 ALA B 735
REMARK 465 HIS B 736
REMARK 465 HIS B 737
REMARK 465 HIS B 738
REMARK 465 HIS B 739
REMARK 465 HIS B 740
REMARK 465 HIS B 741
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 ASN B 342 OG SER B 345 2.11
REMARK 500 O ASN A 342 OG SER A 345 2.11
REMARK 500 O VAL A 343 N GLU A 347 2.11
REMARK 500 O VAL B 343 N GLU B 347 2.12
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 B 264 C - N - CA ANGL. DEV. = 9.4 DEGREES
REMARK 500 PRO B 295 C - N - CA ANGL. DEV. = 9.1 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 PHE A 10 -75.57 -40.11
REMARK 500 LYS A 24 137.92 -39.94
REMARK 500 PRO A 28 -65.61 -100.80
REMARK 500 ARG A 34 144.19 -36.85
REMARK 500 ASP A 38 5.14 -69.62
REMARK 500 VAL A 65 -70.55 -48.02
REMARK 500 ALA A 76 -90.60 -48.44
REMARK 500 PRO A 93 -176.83 -53.79
REMARK 500 ASP A 101 -78.68 -43.12
REMARK 500 ARG A 102 -62.67 -15.29
REMARK 500 ILE A 117 47.50 -94.39
REMARK 500 ALA A 122 4.04 -60.95
REMARK 500 ILE A 150 151.15 -44.56
REMARK 500 THR A 185 134.72 -36.60
REMARK 500 ARG A 203 129.42 -35.44
REMARK 500 ALA A 215 60.70 -156.56
REMARK 500 VAL A 235 -65.91 -91.36
REMARK 500 VAL A 244 -33.88 -35.35
REMARK 500 ALA A 270 -78.66 -39.14
REMARK 500 ARG A 276 -73.99 -46.74
REMARK 500 ALA A 278 -77.92 -42.28
REMARK 500 ILE A 280 -76.79 -44.04
REMARK 500 PHE A 286 -61.37 -28.88
REMARK 500 LEU A 287 -74.04 -46.95
REMARK 500 HIS A 296 -80.13 -48.82
REMARK 500 VAL A 300 -74.05 -35.73
REMARK 500 ALA A 310 -72.29 -35.13
REMARK 500 LEU A 313 -36.95 -36.04
REMARK 500 LEU A 323 98.33 -60.90
REMARK 500 LEU A 325 -62.50 -26.39
REMARK 500 LEU A 331 -87.28 -36.63
REMARK 500 VAL A 332 -64.06 -29.68
REMARK 500 LEU A 344 -73.08 -40.55
REMARK 500 SER A 345 -70.67 -37.06
REMARK 500 ARG A 368 -79.10 -42.68
REMARK 500 MET A 375 -75.64 -29.26
REMARK 500 ASP A 376 -79.30 -28.79
REMARK 500 VAL A 377 -56.11 -27.01
REMARK 500 ALA A 386 -81.30 -40.17
REMARK 500 ILE A 402 -72.00 -34.74
REMARK 500 ALA A 404 -79.91 -35.28
REMARK 500 VAL A 408 -79.49 -48.47
REMARK 500 SER A 410 -85.19 -33.81
REMARK 500 PHE A 412 -72.08 -37.29
REMARK 500 ASN A 414 -72.77 -55.82
REMARK 500 VAL A 416 -85.13 -99.46
REMARK 500 PRO A 440 138.32 -34.93
REMARK 500 ARG A 441 -169.07 -123.00
REMARK 500 PRO A 447 -7.07 -58.67
REMARK 500 TYR A 450 -76.24 -44.20
REMARK 500
REMARK 500 THIS ENTRY HAS 169 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3AQO RELATED DB: PDB
REMARK 900 RELATED ID: 2RRN RELATED DB: PDB
DBREF 3AQP A 1 735 UNP Q5SKE6 Q5SKE6_THET8 1 735
DBREF 3AQP B 1 735 UNP Q5SKE6 Q5SKE6_THET8 1 735
SEQADV 3AQP ASP A 2 UNP Q5SKE6 ASN 2 ENGINEERED MUTATION
SEQADV 3AQP HIS A 736 UNP Q5SKE6 EXPRESSION TAG
SEQADV 3AQP HIS A 737 UNP Q5SKE6 EXPRESSION TAG
SEQADV 3AQP HIS A 738 UNP Q5SKE6 EXPRESSION TAG
SEQADV 3AQP HIS A 739 UNP Q5SKE6 EXPRESSION TAG
SEQADV 3AQP HIS A 740 UNP Q5SKE6 EXPRESSION TAG
SEQADV 3AQP HIS A 741 UNP Q5SKE6 EXPRESSION TAG
SEQADV 3AQP ASP B 2 UNP Q5SKE6 ASN 2 ENGINEERED MUTATION
SEQADV 3AQP HIS B 736 UNP Q5SKE6 EXPRESSION TAG
SEQADV 3AQP HIS B 737 UNP Q5SKE6 EXPRESSION TAG
SEQADV 3AQP HIS B 738 UNP Q5SKE6 EXPRESSION TAG
SEQADV 3AQP HIS B 739 UNP Q5SKE6 EXPRESSION TAG
SEQADV 3AQP HIS B 740 UNP Q5SKE6 EXPRESSION TAG
SEQADV 3AQP HIS B 741 UNP Q5SKE6 EXPRESSION TAG
SEQRES 1 A 741 MET ASP ARG LYS ASN LEU THR SER LEU PHE LEU LEU GLY
SEQRES 2 A 741 VAL PHE LEU LEU ALA LEU LEU PHE VAL TRP LYS PRO TRP
SEQRES 3 A 741 ALA PRO GLU GLU PRO LYS VAL ARG LEU GLY LEU ASP LEU
SEQRES 4 A 741 LYS GLY GLY LEU ARG ILE VAL LEU GLU ALA ASP VAL GLU
SEQRES 5 A 741 ASN PRO THR LEU ASP ASP LEU GLU LYS ALA ARG THR VAL
SEQRES 6 A 741 LEU GLU ASN ARG ILE ASN ALA LEU GLY VAL ALA GLU PRO
SEQRES 7 A 741 LEU ILE GLN ILE GLN GLY GLN LYS ARG ILE VAL VAL GLU
SEQRES 8 A 741 LEU PRO GLY LEU SER GLN ALA ASP GLN ASP ARG ALA LEU
SEQRES 9 A 741 LYS LEU ILE GLY GLN ARG ALA VAL LEU GLU PHE ARG ILE
SEQRES 10 A 741 VAL LYS GLU GLY ALA THR GLY THR THR VAL ALA GLN ILE
SEQRES 11 A 741 ASN GLN ALA LEU ARG GLU ASN PRO ARG LEU ASN ARG GLU
SEQRES 12 A 741 GLU LEU GLU LYS ASP LEU ILE LYS PRO GLU ASP LEU GLY
SEQRES 13 A 741 PRO PRO LEU LEU THR GLY ALA ASP LEU ALA ASP ALA ARG
SEQRES 14 A 741 ALA VAL PHE ASP GLN PHE GLY ARG PRO GLN VAL SER LEU
SEQRES 15 A 741 THR PHE THR PRO GLU GLY ALA LYS LYS PHE GLU GLU VAL
SEQRES 16 A 741 THR ARG GLN ASN ILE GLY LYS ARG LEU ALA ILE VAL LEU
SEQRES 17 A 741 ASP GLY ARG VAL TYR THR ALA PRO VAL ILE ARG GLN ALA
SEQRES 18 A 741 ILE THR GLY GLY GLN ALA VAL ILE GLU GLY LEU SER SER
SEQRES 19 A 741 VAL GLU GLU ALA SER GLU ILE ALA LEU VAL LEU ARG SER
SEQRES 20 A 741 GLY SER LEU PRO VAL PRO LEU LYS VAL ALA GLU ILE ARG
SEQRES 21 A 741 ALA ILE GLY PRO THR LEU GLY GLN ASP ALA ILE GLN ALA
SEQRES 22 A 741 GLY ILE ARG SER ALA LEU ILE GLY THR LEU ALA ILE PHE
SEQRES 23 A 741 LEU LEU ILE PHE ALA TYR TYR GLY PRO HIS LEU GLY LEU
SEQRES 24 A 741 VAL ALA SER LEU GLY LEU LEU TYR THR SER ALA LEU ILE
SEQRES 25 A 741 LEU GLY LEU LEU SER GLY LEU GLY ALA THR LEU THR LEU
SEQRES 26 A 741 PRO GLY ILE ALA GLY LEU VAL LEU THR LEU GLY ALA ALA
SEQRES 27 A 741 VAL ASP GLY ASN VAL LEU SER PHE GLU ARG ILE LYS GLU
SEQRES 28 A 741 GLU LEU ARG ALA GLY LYS LYS LEU ARG GLN ALA ILE PRO
SEQRES 29 A 741 GLU GLY PHE ARG HIS SER THR LEU THR ILE MET ASP VAL
SEQRES 30 A 741 ASN ILE ALA HIS LEU LEU ALA ALA ALA ALA LEU TYR GLN
SEQRES 31 A 741 TYR ALA THR GLY PRO VAL ARG GLY PHE ALA VAL ILE LEU
SEQRES 32 A 741 ALA ILE GLY VAL VAL ALA SER VAL PHE SER ASN LEU VAL
SEQRES 33 A 741 PHE SER ARG HIS LEU LEU GLU ARG LEU ALA ASP ARG GLY
SEQRES 34 A 741 GLU ILE ARG PRO PRO MET TRP LEU VAL ASP PRO ARG PHE
SEQRES 35 A 741 ASN PHE MET GLY PRO ALA ARG TYR VAL THR ALA ALA THR
SEQRES 36 A 741 LEU LEU LEU ALA ALA LEU ALA ALA GLY VAL VAL PHE ALA
SEQRES 37 A 741 LYS GLY PHE ASN TYR SER ILE ASP PHE THR GLY GLY THR
SEQRES 38 A 741 ALA TYR THR LEU ARG ALA GLU PRO ASN VAL GLU VAL GLU
SEQRES 39 A 741 THR LEU ARG ARG PHE LEU GLU GLU LYS GLY PHE PRO GLY
SEQRES 40 A 741 LYS GLU ALA VAL ILE THR GLN VAL GLN ALA PRO THR ALA
SEQRES 41 A 741 ALA TYR ARG GLU PHE LEU VAL LYS LEU PRO PRO LEU SER
SEQRES 42 A 741 ASP GLU ARG ARG LEU GLU LEU GLU ARG LEU PHE ALA SER
SEQRES 43 A 741 GLU LEU LYS ALA THR VAL LEU ALA SER GLU THR VAL GLY
SEQRES 44 A 741 PRO ALA ILE GLY GLU GLU LEU ARG ARG ASN ALA VAL MET
SEQRES 45 A 741 ALA VAL LEU VAL GLY LEU GLY LEU ILE LEU LEU TYR VAL
SEQRES 46 A 741 ALA PHE ARG PHE ASP TRP THR PHE GLY VAL ALA SER ILE
SEQRES 47 A 741 LEU ALA VAL ALA HIS ASP VAL ALA ILE VAL ALA GLY MET
SEQRES 48 A 741 TYR SER LEU LEU GLY LEU GLU PHE SER ILE PRO THR ILE
SEQRES 49 A 741 ALA ALA LEU LEU THR ILE VAL GLY TYR SER ILE ASN ASP
SEQRES 50 A 741 SER ILE VAL VAL SER ASP ARG ILE ARG GLU ASN GLN LYS
SEQRES 51 A 741 LEU LEU ARG HIS LEU PRO TYR ALA GLU LEU VAL ASN ARG
SEQRES 52 A 741 SER ILE ASN GLN THR LEU SER ARG THR VAL MET THR SER
SEQRES 53 A 741 LEU THR THR LEU LEU PRO ILE LEU ALA LEU LEU PHE LEU
SEQRES 54 A 741 GLY GLY SER VAL LEU ARG ASP PHE ALA LEU ALA ILE PHE
SEQRES 55 A 741 VAL GLY ILE PHE VAL GLY THR TYR SER SER ILE TYR VAL
SEQRES 56 A 741 VAL SER ALA LEU VAL VAL ALA TRP LYS ASN ARG ARG LYS
SEQRES 57 A 741 ALA GLN GLU ALA SER LYS ALA HIS HIS HIS HIS HIS HIS
SEQRES 1 B 741 MET ASP ARG LYS ASN LEU THR SER LEU PHE LEU LEU GLY
SEQRES 2 B 741 VAL PHE LEU LEU ALA LEU LEU PHE VAL TRP LYS PRO TRP
SEQRES 3 B 741 ALA PRO GLU GLU PRO LYS VAL ARG LEU GLY LEU ASP LEU
SEQRES 4 B 741 LYS GLY GLY LEU ARG ILE VAL LEU GLU ALA ASP VAL GLU
SEQRES 5 B 741 ASN PRO THR LEU ASP ASP LEU GLU LYS ALA ARG THR VAL
SEQRES 6 B 741 LEU GLU ASN ARG ILE ASN ALA LEU GLY VAL ALA GLU PRO
SEQRES 7 B 741 LEU ILE GLN ILE GLN GLY GLN LYS ARG ILE VAL VAL GLU
SEQRES 8 B 741 LEU PRO GLY LEU SER GLN ALA ASP GLN ASP ARG ALA LEU
SEQRES 9 B 741 LYS LEU ILE GLY GLN ARG ALA VAL LEU GLU PHE ARG ILE
SEQRES 10 B 741 VAL LYS GLU GLY ALA THR GLY THR THR VAL ALA GLN ILE
SEQRES 11 B 741 ASN GLN ALA LEU ARG GLU ASN PRO ARG LEU ASN ARG GLU
SEQRES 12 B 741 GLU LEU GLU LYS ASP LEU ILE LYS PRO GLU ASP LEU GLY
SEQRES 13 B 741 PRO PRO LEU LEU THR GLY ALA ASP LEU ALA ASP ALA ARG
SEQRES 14 B 741 ALA VAL PHE ASP GLN PHE GLY ARG PRO GLN VAL SER LEU
SEQRES 15 B 741 THR PHE THR PRO GLU GLY ALA LYS LYS PHE GLU GLU VAL
SEQRES 16 B 741 THR ARG GLN ASN ILE GLY LYS ARG LEU ALA ILE VAL LEU
SEQRES 17 B 741 ASP GLY ARG VAL TYR THR ALA PRO VAL ILE ARG GLN ALA
SEQRES 18 B 741 ILE THR GLY GLY GLN ALA VAL ILE GLU GLY LEU SER SER
SEQRES 19 B 741 VAL GLU GLU ALA SER GLU ILE ALA LEU VAL LEU ARG SER
SEQRES 20 B 741 GLY SER LEU PRO VAL PRO LEU LYS VAL ALA GLU ILE ARG
SEQRES 21 B 741 ALA ILE GLY PRO THR LEU GLY GLN ASP ALA ILE GLN ALA
SEQRES 22 B 741 GLY ILE ARG SER ALA LEU ILE GLY THR LEU ALA ILE PHE
SEQRES 23 B 741 LEU LEU ILE PHE ALA TYR TYR GLY PRO HIS LEU GLY LEU
SEQRES 24 B 741 VAL ALA SER LEU GLY LEU LEU TYR THR SER ALA LEU ILE
SEQRES 25 B 741 LEU GLY LEU LEU SER GLY LEU GLY ALA THR LEU THR LEU
SEQRES 26 B 741 PRO GLY ILE ALA GLY LEU VAL LEU THR LEU GLY ALA ALA
SEQRES 27 B 741 VAL ASP GLY ASN VAL LEU SER PHE GLU ARG ILE LYS GLU
SEQRES 28 B 741 GLU LEU ARG ALA GLY LYS LYS LEU ARG GLN ALA ILE PRO
SEQRES 29 B 741 GLU GLY PHE ARG HIS SER THR LEU THR ILE MET ASP VAL
SEQRES 30 B 741 ASN ILE ALA HIS LEU LEU ALA ALA ALA ALA LEU TYR GLN
SEQRES 31 B 741 TYR ALA THR GLY PRO VAL ARG GLY PHE ALA VAL ILE LEU
SEQRES 32 B 741 ALA ILE GLY VAL VAL ALA SER VAL PHE SER ASN LEU VAL
SEQRES 33 B 741 PHE SER ARG HIS LEU LEU GLU ARG LEU ALA ASP ARG GLY
SEQRES 34 B 741 GLU ILE ARG PRO PRO MET TRP LEU VAL ASP PRO ARG PHE
SEQRES 35 B 741 ASN PHE MET GLY PRO ALA ARG TYR VAL THR ALA ALA THR
SEQRES 36 B 741 LEU LEU LEU ALA ALA LEU ALA ALA GLY VAL VAL PHE ALA
SEQRES 37 B 741 LYS GLY PHE ASN TYR SER ILE ASP PHE THR GLY GLY THR
SEQRES 38 B 741 ALA TYR THR LEU ARG ALA GLU PRO ASN VAL GLU VAL GLU
SEQRES 39 B 741 THR LEU ARG ARG PHE LEU GLU GLU LYS GLY PHE PRO GLY
SEQRES 40 B 741 LYS GLU ALA VAL ILE THR GLN VAL GLN ALA PRO THR ALA
SEQRES 41 B 741 ALA TYR ARG GLU PHE LEU VAL LYS LEU PRO PRO LEU SER
SEQRES 42 B 741 ASP GLU ARG ARG LEU GLU LEU GLU ARG LEU PHE ALA SER
SEQRES 43 B 741 GLU LEU LYS ALA THR VAL LEU ALA SER GLU THR VAL GLY
SEQRES 44 B 741 PRO ALA ILE GLY GLU GLU LEU ARG ARG ASN ALA VAL MET
SEQRES 45 B 741 ALA VAL LEU VAL GLY LEU GLY LEU ILE LEU LEU TYR VAL
SEQRES 46 B 741 ALA PHE ARG PHE ASP TRP THR PHE GLY VAL ALA SER ILE
SEQRES 47 B 741 LEU ALA VAL ALA HIS ASP VAL ALA ILE VAL ALA GLY MET
SEQRES 48 B 741 TYR SER LEU LEU GLY LEU GLU PHE SER ILE PRO THR ILE
SEQRES 49 B 741 ALA ALA LEU LEU THR ILE VAL GLY TYR SER ILE ASN ASP
SEQRES 50 B 741 SER ILE VAL VAL SER ASP ARG ILE ARG GLU ASN GLN LYS
SEQRES 51 B 741 LEU LEU ARG HIS LEU PRO TYR ALA GLU LEU VAL ASN ARG
SEQRES 52 B 741 SER ILE ASN GLN THR LEU SER ARG THR VAL MET THR SER
SEQRES 53 B 741 LEU THR THR LEU LEU PRO ILE LEU ALA LEU LEU PHE LEU
SEQRES 54 B 741 GLY GLY SER VAL LEU ARG ASP PHE ALA LEU ALA ILE PHE
SEQRES 55 B 741 VAL GLY ILE PHE VAL GLY THR TYR SER SER ILE TYR VAL
SEQRES 56 B 741 VAL SER ALA LEU VAL VAL ALA TRP LYS ASN ARG ARG LYS
SEQRES 57 B 741 ALA GLN GLU ALA SER LYS ALA HIS HIS HIS HIS HIS HIS
HELIX 1 1 ASP A 2 LYS A 24 1 23
HELIX 2 2 PRO A 28 VAL A 33 1 6
HELIX 3 3 THR A 55 GLY A 74 1 20
HELIX 4 4 SER A 96 GLN A 109 1 14
HELIX 5 5 THR A 126 ASN A 137 1 12
HELIX 6 6 ASN A 141 LEU A 149 1 9
HELIX 7 7 THR A 185 ASN A 199 1 15
HELIX 8 8 GLU A 236 LEU A 250 1 15
HELIX 9 9 GLY A 263 GLY A 294 1 32
HELIX 10 10 GLY A 294 GLY A 320 1 27
HELIX 11 11 THR A 324 ARG A 354 1 31
HELIX 12 12 LYS A 358 TYR A 391 1 34
HELIX 13 13 GLY A 394 GLY A 429 1 36
HELIX 14 14 PRO A 447 GLY A 470 1 24
HELIX 15 15 SER A 474 GLY A 479 1 6
HELIX 16 16 GLU A 492 GLU A 502 1 11
HELIX 17 17 SER A 533 LEU A 548 1 16
HELIX 18 18 GLY A 559 PHE A 589 1 31
HELIX 19 19 ASP A 590 GLY A 616 1 27
HELIX 20 20 SER A 620 LEU A 652 1 33
HELIX 21 21 PRO A 656 GLY A 690 1 35
HELIX 22 22 GLY A 691 ARG A 726 1 36
HELIX 23 23 ASP B 2 LYS B 24 1 23
HELIX 24 24 PRO B 28 VAL B 33 1 6
HELIX 25 25 THR B 55 GLY B 74 1 20
HELIX 26 26 SER B 96 GLN B 109 1 14
HELIX 27 27 THR B 126 ASN B 137 1 12
HELIX 28 28 ASN B 141 LEU B 149 1 9
HELIX 29 29 THR B 185 ASN B 199 1 15
HELIX 30 30 GLU B 236 LEU B 250 1 15
HELIX 31 31 GLY B 263 GLY B 294 1 32
HELIX 32 32 GLY B 294 GLY B 320 1 27
HELIX 33 33 THR B 324 ALA B 355 1 32
HELIX 34 34 LYS B 358 TYR B 391 1 34
HELIX 35 35 GLY B 394 GLY B 429 1 36
HELIX 36 36 PRO B 447 GLY B 470 1 24
HELIX 37 37 SER B 474 GLY B 479 1 6
HELIX 38 38 GLU B 492 GLU B 502 1 11
HELIX 39 39 SER B 533 LEU B 548 1 16
HELIX 40 40 GLY B 559 PHE B 589 1 31
HELIX 41 41 ASP B 590 GLY B 616 1 27
HELIX 42 42 SER B 620 LEU B 652 1 33
HELIX 43 43 PRO B 656 GLY B 690 1 35
HELIX 44 44 GLY B 691 ARG B 726 1 36
SHEET 1 A 8 LEU A 79 GLN A 83 0
SHEET 2 A 8 ARG A 87 GLY A 94 -1 O GLU A 91 N LEU A 79
SHEET 3 A 8 GLY A 42 GLU A 48 -1 N LEU A 43 O LEU A 92
SHEET 4 A 8 LYS A 255 ILE A 262 -1 O ARG A 260 N ARG A 44
SHEET 5 A 8 ALA A 554 VAL A 558 -1 O THR A 557 N ILE A 259
SHEET 6 A 8 GLY A 480 ALA A 487 -1 N THR A 484 O ALA A 554
SHEET 7 A 8 ARG A 523 LEU A 529 -1 O LEU A 529 N THR A 481
SHEET 8 A 8 VAL A 511 VAL A 515 -1 N VAL A 511 O LYS A 528
SHEET 1 B 4 LEU A 160 THR A 161 0
SHEET 2 B 4 LEU A 113 PHE A 115 -1 N PHE A 115 O LEU A 160
SHEET 3 B 4 ILE A 206 LEU A 208 -1 O VAL A 207 N GLU A 114
SHEET 4 B 4 ARG A 211 THR A 214 -1 O ARG A 211 N LEU A 208
SHEET 1 C 3 LEU A 165 ASP A 173 0
SHEET 2 C 3 ARG A 177 PHE A 184 -1 O ARG A 177 N ASP A 173
SHEET 3 C 3 GLN A 226 VAL A 228 -1 O ALA A 227 N LEU A 182
SHEET 1 D 2 LEU B 35 GLY B 36 0
SHEET 2 D 2 THR B 322 LEU B 323 1 O LEU B 323 N LEU B 35
SHEET 1 E 8 LEU B 79 GLN B 83 0
SHEET 2 E 8 ARG B 87 GLY B 94 -1 O GLU B 91 N LEU B 79
SHEET 3 E 8 GLY B 42 GLU B 48 -1 N LEU B 43 O LEU B 92
SHEET 4 E 8 LYS B 255 ILE B 262 -1 O ARG B 260 N ARG B 44
SHEET 5 E 8 ALA B 554 VAL B 558 -1 O THR B 557 N ILE B 259
SHEET 6 E 8 GLY B 480 ALA B 487 -1 N THR B 484 O ALA B 554
SHEET 7 E 8 ARG B 523 LEU B 529 -1 O LEU B 529 N THR B 481
SHEET 8 E 8 VAL B 511 VAL B 515 -1 N VAL B 511 O LYS B 528
SHEET 1 F 4 LEU B 160 THR B 161 0
SHEET 2 F 4 LEU B 113 PHE B 115 -1 N PHE B 115 O LEU B 160
SHEET 3 F 4 ILE B 206 LEU B 208 -1 O VAL B 207 N GLU B 114
SHEET 4 F 4 ARG B 211 THR B 214 -1 O ARG B 211 N LEU B 208
SHEET 1 G 3 LEU B 165 ASP B 173 0
SHEET 2 G 3 ARG B 177 PHE B 184 -1 O ARG B 177 N ASP B 173
SHEET 3 G 3 GLN B 226 VAL B 228 -1 O ALA B 227 N LEU B 182
CRYST1 140.636 140.636 160.563 90.00 90.00 90.00 P 43 8
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 0.007111 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007111 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006228 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
