HEADER TRANSLATION 15-DEC-14 4UE4
TITLE STRUCTURAL BASIS FOR TARGETING AND ELONGATION ARREST OF BACILLUS
TITLE 2 SIGNAL RECOGNITION PARTICLE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 6S RNA;
COMPND 3 CHAIN: A;
COMPND 4 MOL_ID: 2;
COMPND 5 MOLECULE: FTSQ SIGNAL SEQUENCE;
COMPND 6 CHAIN: B;
COMPND 7 MOL_ID: 3;
COMPND 8 MOLECULE: SIGNAL RECOGNITION PARTICLE PROTEIN;
COMPND 9 CHAIN: C;
COMPND 10 FRAGMENT: M DOMAIN;
COMPND 11 SYNONYM: FIFTY-FOUR HOMOLOG, FFH;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS SUBSP. SUBTILIS STR. 168;
SOURCE 3 ORGANISM_TAXID: 224308;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS SUBSP. SUBTILIS STR. 168;
SOURCE 6 ORGANISM_TAXID: 224308;
SOURCE 7 MOL_ID: 3;
SOURCE 8 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS SUBSP. SUBTILIS STR. 168;
SOURCE 9 ORGANISM_TAXID: 224308;
SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 11 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 12 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 13 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 14 EXPRESSION_SYSTEM_VECTOR: PETRSF
KEYWDS SIGNAL RECOGNITION PARTICLE (SRP), STALLED-RIBOSOME, TRANSLATION,
KEYWDS 2 TRANSLOCATION, MIFM STALLING
EXPDTA ELECTRON MICROSCOPY
AUTHOR B.BECKERT,A.KEDROV,D.SOHMEN,G.KEMPF,K.WILD,I.SINNING,H.STAHLBERG,
AUTHOR 2 D.N.WILSON,R.BECKMANN
REVDAT 5 03-OCT-18 4UE4 1 REMARK
REVDAT 4 30-AUG-17 4UE4 1 REMARK
REVDAT 3 21-OCT-15 4UE4 1 JRNL
REVDAT 2 23-SEP-15 4UE4 1 JRNL
REVDAT 1 09-SEP-15 4UE4 0
JRNL AUTH B.BECKERT,A.KEDROV,D.SOHMEN,G.KEMPF,K.WILD,I.SINNING,
JRNL AUTH 2 H.STAHLBERG,D.N.WILSON,R.BECKMANN
JRNL TITL TRANSLATIONAL ARREST BY A PROKARYOTIC SIGNAL RECOGNITION
JRNL TITL 2 PARTICLE IS MEDIATED BY RNA INTERACTIONS.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 22 767 2015
JRNL REFN ISSN 1545-9993
JRNL PMID 26344568
JRNL DOI 10.1038/NSMB.3086
REMARK 2
REMARK 2 RESOLUTION. 7.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : SPIDER
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : NULL
REMARK 3 REFINEMENT SPACE : NULL
REMARK 3 REFINEMENT PROTOCOL : RIGID BODY FIT
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : METHOD--RIGID BODY
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 7.000
REMARK 3 NUMBER OF PARTICLES : 75900
REMARK 3 CTF CORRECTION METHOD : NULL
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: SUBMISSION BASED ON EXPERIMENTAL DATA FROM EMDB EMD
REMARK 3 -2843. (DEPOSITION ID: 12993).
REMARK 4
REMARK 4 4UE4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE.
REMARK 100 THE DEPOSITION ID IS D_1290062579.
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE
REMARK 245 SPECIMEN TYPE : VITREOUS ICE
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE TYPE : PARTICLE
REMARK 245 PARTICLE TYPE : POINT
REMARK 245 NAME OF SAMPLE : BACILLUS SUBTILIS MIFM STALLED
REMARK 245 RIBOSOME IN COMPLEX WITH SIGNAL
REMARK 245 RECOGNITION PARTICLE (SRP)
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL
REMARK 245 SAMPLE SUPPORT DETAILS : CARBON
REMARK 245 SAMPLE VITRIFICATION DETAILS : VITRIFICATION 1 -- CRYOGEN-
REMARK 245 ETHANE, INSTRUMENT- FEI
REMARK 245 VITROBOT MARK IV,
REMARK 245 SAMPLE BUFFER : HEPERS 20 MM, KOAC 150 MM,
REMARK 245 MG(OAC)2 10MM, NIKKOL 0.005%,
REMARK 245 DTT 1MM, 2% GLYCEROL
REMARK 245 PH : 7.60
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : 10-DEC-13
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS
REMARK 245 DETECTOR TYPE : TVIPS TEMCAM-F816 (8K X 8K)
REMARK 245 MINIMUM DEFOCUS (NM) : 800.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 4000.00
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : 2.70
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 20.00
REMARK 245 ILLUMINATION MODE : SPOT SCAN
REMARK 245 NOMINAL MAGNIFICATION : NULL
REMARK 245 CALIBRATED MAGNIFICATION : NULL
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 300
REMARK 245 IMAGING DETAILS : NULL
REMARK 247
REMARK 247 ELECTRON MICROSCOPY
REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON
REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE
REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES
REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION
REMARK 247 OF THE STRUCTURE FACTORS.
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: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LEU B 10 CB CG CD1 CD2
REMARK 470 PHE B 11 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU B 12 CB CG CD1 CD2
REMARK 470 LEU B 13 CB CG CD1 CD2
REMARK 470 THR B 14 CB OG1 CG2
REMARK 470 VAL B 15 CB CG1 CG2
REMARK 470 CYS B 16 CB SG
REMARK 470 THR B 17 CB OG1 CG2
REMARK 470 THR B 18 CB OG1 CG2
REMARK 470 VAL B 19 CB CG1 CG2
REMARK 470 LEU B 20 CB CG CD1 CD2
REMARK 470 VAL B 21 CB CG1 CG2
REMARK 470 SER B 22 CB OG
REMARK 470 TRP B 24 CB CG CD1 CD2 NE1 CE2 CE3
REMARK 470 TRP B 24 CZ2 CZ3 CH2
REMARK 470 VAL B 25 CB CG1 CG2
REMARK 470 VAL B 26 CB CG1 CG2
REMARK 470 LEU B 27 CB CG CD1 CD2
REMARK 470 TRP B 29 CB CG CD1 CD2 NE1 CE2 CE3
REMARK 470 TRP B 29 CZ2 CZ3 CH2
REMARK 470 MET B 30 CB CG SD CE
REMARK 470 GLU B 31 CB CG CD OE1 OE2
REMARK 470 THR C 330 CB OG1 CG2
REMARK 470 LEU C 331 CB CG CD1 CD2
REMARK 470 ASP C 332 CB CG OD1 OD2
REMARK 470 ASP C 333 CB CG OD1 OD2
REMARK 470 PHE C 334 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU C 335 CB CG CD1 CD2
REMARK 470 GLU C 336 CB CG CD OE1 OE2
REMARK 470 GLN C 337 CB CG CD OE1 NE2
REMARK 470 LEU C 338 CB CG CD1 CD2
REMARK 470 GLN C 340 CB CG CD OE1 NE2
REMARK 470 VAL C 341 CB CG1 CG2
REMARK 470 ARG C 342 CB CG CD NE CZ NH1 NH2
REMARK 470 ASN C 343 CB CG OD1 ND2
REMARK 470 MET C 344 CB CG SD CE
REMARK 470 PRO C 346 CB CG CD
REMARK 470 LEU C 347 CB CG CD1 CD2
REMARK 470 ASP C 348 CB CG OD1 OD2
REMARK 470 GLU C 349 CB CG CD OE1 OE2
REMARK 470 LEU C 350 CB CG CD1 CD2
REMARK 470 LEU C 351 CB CG CD1 CD2
REMARK 470 GLN C 352 CB CG CD OE1 NE2
REMARK 470 MET C 353 CB CG SD CE
REMARK 470 MET C 354 CB CG SD CE
REMARK 470 PRO C 355 CB CG CD
REMARK 470 ALA C 357 CB
REMARK 470 LYS C 359 CB CG CD CE NZ
REMARK 470 MET C 360 CB CG SD CE
REMARK 470 LYS C 361 CB CG CD CE NZ
REMARK 470 LEU C 363 CB CG CD1 CD2
REMARK 470 LYS C 364 CB CG CD CE NZ
REMARK 470 ASN C 365 CB CG OD1 ND2
REMARK 470 ILE C 366 CB CG1 CG2 CD1
REMARK 470 GLN C 367 CB CG CD OE1 NE2
REMARK 470 VAL C 368 CB CG1 CG2
REMARK 470 ASP C 369 CB CG OD1 OD2
REMARK 470 GLU C 370 CB CG CD OE1 OE2
REMARK 470 LYS C 371 CB CG CD CE NZ
REMARK 470 GLN C 372 CB CG CD OE1 NE2
REMARK 470 LEU C 373 CB CG CD1 CD2
REMARK 470 ASN C 374 CB CG OD1 ND2
REMARK 470 HIS C 375 CB CG ND1 CD2 CE1 NE2
REMARK 470 VAL C 376 CB CG1 CG2
REMARK 470 GLU C 377 CB CG CD OE1 OE2
REMARK 470 ALA C 378 CB
REMARK 470 ILE C 379 CB CG1 CG2 CD1
REMARK 470 ILE C 380 CB CG1 CG2 CD1
REMARK 470 LYS C 381 CB CG CD CE NZ
REMARK 470 SER C 382 CB OG
REMARK 470 MET C 383 CB CG SD CE
REMARK 470 THR C 384 CB OG1 CG2
REMARK 470 VAL C 385 CB CG1 CG2
REMARK 470 LEU C 386 CB CG CD1 CD2
REMARK 470 GLU C 387 CB CG CD OE1 OE2
REMARK 470 LYS C 388 CB CG CD CE NZ
REMARK 470 GLU C 389 CB CG CD OE1 OE2
REMARK 470 GLN C 390 CB CG CD OE1 NE2
REMARK 470 PRO C 391 CB CG CD
REMARK 470 ASP C 392 CB CG OD1 OD2
REMARK 470 ILE C 393 CB CG1 CG2 CD1
REMARK 470 ILE C 394 CB CG1 CG2 CD1
REMARK 470 ASN C 395 CB CG OD1 ND2
REMARK 470 ALA C 396 CB
REMARK 470 SER C 397 CB OG
REMARK 470 ARG C 398 CB CG CD NE CZ NH1 NH2
REMARK 470 ARG C 399 CB CG CD NE CZ NH1 NH2
REMARK 470 LYS C 400 CB CG CD CE NZ
REMARK 470 ARG C 401 CB CG CD NE CZ NH1 NH2
REMARK 470 ILE C 402 CB CG1 CG2 CD1
REMARK 470 ALA C 403 CB
REMARK 470 LYS C 404 CB CG CD CE NZ
REMARK 470 SER C 406 CB OG
REMARK 470 THR C 408 CB OG1 CG2
REMARK 470 SER C 409 CB OG
REMARK 470 VAL C 410 CB CG1 CG2
REMARK 470 GLN C 411 CB CG CD OE1 NE2
REMARK 470 GLU C 412 CB CG CD OE1 OE2
REMARK 470 VAL C 413 CB CG1 CG2
REMARK 470 ASN C 414 CB CG OD1 ND2
REMARK 470 ARG C 415 CB CG CD NE CZ NH1 NH2
REMARK 470 LEU C 416 CB CG CD1 CD2
REMARK 470 LEU C 417 CB CG CD1 CD2
REMARK 470 LYS C 418 CB CG CD CE NZ
REMARK 470 GLN C 419 CB CG CD OE1 NE2
REMARK 470 PHE C 420 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP C 421 CB CG OD1 OD2
REMARK 470 GLU C 422 CB CG CD OE1 OE2
REMARK 470 MET C 423 CB CG SD CE
REMARK 470 LYS C 424 CB CG CD CE NZ
REMARK 470 LYS C 425 CB CG CD CE NZ
REMARK 470 MET C 426 CB CG SD CE
REMARK 470 MET C 427 CB CG SD CE
REMARK 470 LYS C 428 CB CG CD CE NZ
REMARK 470 GLN C 429 CB CG CD OE1 NE2
REMARK 470 MET C 430 CB CG SD CE
REMARK 470 THR C 431 CB OG1 CG2
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 C SER C 409 CA VAL C 410 1.44
REMARK 500 O2' A A 170 O LYS C 404 1.47
REMARK 500 O SER C 409 CA VAL C 410 1.60
REMARK 500 CA SER C 409 N VAL C 410 1.68
REMARK 500 N3 A A 135 O2 U A 196 1.94
REMARK 500 O2' G A 195 OP2 G A 197 2.00
REMARK 500 O2 C A 150 CA ARG C 398 2.09
REMARK 500 N3 U A 136 N1 A A 193 2.15
REMARK 500 O HIS C 375 N GLU C 377 2.15
REMARK 500 O2 U A 153 N1 A A 176 2.18
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 A A 44 O3' U A 45 P -0.082
REMARK 500 C A 51 P C A 51 O5' 0.060
REMARK 500 A A 235 O3' C A 236 P -0.083
REMARK 500 A A 250 O3' U A 251 P 0.083
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 U A 8 C2 - N3 - C4 ANGL. DEV. = -3.8 DEGREES
REMARK 500 U A 8 N3 - C4 - C5 ANGL. DEV. = 4.2 DEGREES
REMARK 500 U A 11 C2 - N3 - C4 ANGL. DEV. = -4.6 DEGREES
REMARK 500 U A 11 N3 - C4 - C5 ANGL. DEV. = 4.6 DEGREES
REMARK 500 A A 12 C6 - N1 - C2 ANGL. DEV. = 3.6 DEGREES
REMARK 500 A A 12 N1 - C2 - N3 ANGL. DEV. = -3.3 DEGREES
REMARK 500 A A 12 C5 - C6 - N1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 G A 14 O4' - C1' - N9 ANGL. DEV. = 4.4 DEGREES
REMARK 500 G A 14 C5 - C6 - N1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 C A 15 O4' - C1' - N1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 G A 17 C5 - C6 - N1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 A A 20 N1 - C2 - N3 ANGL. DEV. = -3.1 DEGREES
REMARK 500 U A 23 C2 - N3 - C4 ANGL. DEV. = -4.7 DEGREES
REMARK 500 U A 23 N3 - C4 - C5 ANGL. DEV. = 4.6 DEGREES
REMARK 500 A A 24 N1 - C2 - N3 ANGL. DEV. = -3.1 DEGREES
REMARK 500 G A 25 O4' - C1' - N9 ANGL. DEV. = 4.4 DEGREES
REMARK 500 G A 25 C3' - O3' - P ANGL. DEV. = 9.6 DEGREES
REMARK 500 C A 26 O4' - C1' - N1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 U A 29 C2 - N3 - C4 ANGL. DEV. = -4.9 DEGREES
REMARK 500 U A 29 N3 - C4 - C5 ANGL. DEV. = 4.8 DEGREES
REMARK 500 G A 30 O4' - C1' - N9 ANGL. DEV. = 4.9 DEGREES
REMARK 500 U A 34 C2 - N3 - C4 ANGL. DEV. = -4.6 DEGREES
REMARK 500 U A 34 N3 - C4 - C5 ANGL. DEV. = 4.6 DEGREES
REMARK 500 G A 35 O4' - C1' - N9 ANGL. DEV. = 4.8 DEGREES
REMARK 500 U A 36 O4' - C1' - N1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 U A 36 C2 - N3 - C4 ANGL. DEV. = -4.7 DEGREES
REMARK 500 U A 36 N3 - C4 - C5 ANGL. DEV. = 4.6 DEGREES
REMARK 500 U A 36 C3' - O3' - P ANGL. DEV. = 8.1 DEGREES
REMARK 500 A A 37 N1 - C2 - N3 ANGL. DEV. = -3.1 DEGREES
REMARK 500 C A 38 O4' - C1' - N1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 C A 39 O4' - C1' - N1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 U A 40 C2 - N3 - C4 ANGL. DEV. = -3.9 DEGREES
REMARK 500 U A 40 N3 - C4 - C5 ANGL. DEV. = 4.3 DEGREES
REMARK 500 A A 43 C4' - C3' - O3' ANGL. DEV. = 26.5 DEGREES
REMARK 500 A A 43 C2' - C3' - O3' ANGL. DEV. = -15.5 DEGREES
REMARK 500 A A 44 C4' - C3' - O3' ANGL. DEV. = -32.4 DEGREES
REMARK 500 U A 45 O5' - C5' - C4' ANGL. DEV. = 13.9 DEGREES
REMARK 500 U A 45 O4' - C4' - C3' ANGL. DEV. = -14.4 DEGREES
REMARK 500 U A 45 C5' - C4' - O4' ANGL. DEV. = 9.7 DEGREES
REMARK 500 U A 45 C4' - C3' - O3' ANGL. DEV. = 14.0 DEGREES
REMARK 500 U A 45 C2' - C3' - O3' ANGL. DEV. = -24.2 DEGREES
REMARK 500 U A 45 C4' - C3' - C2' ANGL. DEV. = -8.1 DEGREES
REMARK 500 U A 45 N1 - C1' - C2' ANGL. DEV. = -17.9 DEGREES
REMARK 500 U A 45 O4' - C1' - N1 ANGL. DEV. = 11.7 DEGREES
REMARK 500 C A 46 C2 - N3 - C4 ANGL. DEV. = 3.4 DEGREES
REMARK 500 C A 46 N3 - C4 - C5 ANGL. DEV. = -2.6 DEGREES
REMARK 500 C A 49 C3' - O3' - P ANGL. DEV. = 10.9 DEGREES
REMARK 500 U A 50 C2 - N3 - C4 ANGL. DEV. = -4.7 DEGREES
REMARK 500 U A 50 N3 - C4 - C5 ANGL. DEV. = 4.7 DEGREES
REMARK 500 U A 50 C3' - O3' - P ANGL. DEV. = 11.4 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 309 ANGLE DEVIATIONS.
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 LEU C 351 42.01 129.26
REMARK 500 LEU C 363 -65.61 162.29
REMARK 500 LYS C 364 -67.48 -143.04
REMARK 500 GLU C 370 157.95 171.31
REMARK 500 GLN C 372 -38.39 -139.55
REMARK 500 VAL C 376 -33.68 -12.95
REMARK 500 THR C 408 -155.13 -106.78
REMARK 500 MET C 430 -85.64 -108.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ALA C 357 GLY C 358 -35.39
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4UE5 RELATED DB: PDB
REMARK 900 STRUCTURAL BASIS FOR TARGETING AND ELONGATION ARREST OF BACILLUS
REMARK 900 SIGNAL RECOGNITION PARTICLE
REMARK 900 RELATED ID: EMD-2843 RELATED DB: EMDB
DBREF 4UE4 A 4 269 GB 40130 X14796.1 290 556
DBREF 4UE4 B 10 31 PDB 4UE4 4UE4 10 31
DBREF 4UE4 C 330 431 UNP P37105 SRP54_BACSU 330 431
SEQADV 4UE4 A GB 40130 U 525 DELETION
SEQRES 1 A 266 G C C G U G C U A A G C G
SEQRES 2 A 266 G G G A G G U A G C G G U
SEQRES 3 A 266 G C C C U G U A C C U G C
SEQRES 4 A 266 A A U C C G C U C U A G C
SEQRES 5 A 266 A G G G C C G A A U C C C
SEQRES 6 A 266 U U C U C G A G G U U C G
SEQRES 7 A 266 U U U A C U U U A A G G C
SEQRES 8 A 266 C U G C C U U A A G U A A
SEQRES 9 A 266 G U G G U G U U G A C G U
SEQRES 10 A 266 U U G G G U C C U G C G C
SEQRES 11 A 266 A A U G G G A A U U C A U
SEQRES 12 A 266 G A A C C A U G U C A G G
SEQRES 13 A 266 U C C G G A A G G A A G C
SEQRES 14 A 266 A G C A U U A A G U G A A
SEQRES 15 A 266 A C C U C U C A U G U G C
SEQRES 16 A 266 C G C A G G G U U G C C U
SEQRES 17 A 266 G G G C C G A G C U A A C
SEQRES 18 A 266 U G C U U A A G U A A C G
SEQRES 19 A 266 C U A G G G U A G C G A A
SEQRES 20 A 266 U C G A C A G A A G G U G
SEQRES 21 A 266 C A C G G U
SEQRES 1 B 22 LEU PHE LEU LEU THR VAL CYS THR THR VAL LEU VAL SER
SEQRES 2 B 22 GLY TRP VAL VAL LEU GLY TRP MET GLU
SEQRES 1 C 102 THR LEU ASP ASP PHE LEU GLU GLN LEU GLY GLN VAL ARG
SEQRES 2 C 102 ASN MET GLY PRO LEU ASP GLU LEU LEU GLN MET MET PRO
SEQRES 3 C 102 GLY ALA GLY LYS MET LYS GLY LEU LYS ASN ILE GLN VAL
SEQRES 4 C 102 ASP GLU LYS GLN LEU ASN HIS VAL GLU ALA ILE ILE LYS
SEQRES 5 C 102 SER MET THR VAL LEU GLU LYS GLU GLN PRO ASP ILE ILE
SEQRES 6 C 102 ASN ALA SER ARG ARG LYS ARG ILE ALA LYS GLY SER GLY
SEQRES 7 C 102 THR SER VAL GLN GLU VAL ASN ARG LEU LEU LYS GLN PHE
SEQRES 8 C 102 ASP GLU MET LYS LYS MET MET LYS GLN MET THR
HELIX 1 1 LEU B 10 GLY B 28 1 19
HELIX 2 2 THR C 330 GLY C 345 1 16
HELIX 3 3 HIS C 375 MET C 383 1 9
HELIX 4 4 THR C 384 GLN C 390 1 7
HELIX 5 5 PRO C 391 ILE C 394 5 4
HELIX 6 6 ASN C 395 GLY C 407 1 13
HELIX 7 7 SER C 409 MET C 430 1 22
CISPEP 1 GLU C 349 LEU C 350 0 4.51
CISPEP 2 GLY C 358 LYS C 359 0 0.31
CISPEP 3 LEU C 363 LYS C 364 0 -25.74
CISPEP 4 LYS C 364 ASN C 365 0 -11.59
CISPEP 5 ASN C 365 ILE C 366 0 -27.33
CISPEP 6 GLN C 367 VAL C 368 0 -13.53
CISPEP 7 ASP C 369 GLU C 370 0 0.59
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
