Header list of 1pbu.pdb file
Complete list - t 27 2 Bytes
HEADER TRANSLATION 15-MAY-03 1PBU
TITLE SOLUTION STRUCTURE OF THE C-TERMINAL DOMAIN OF THE HUMAN EEF1BGAMMA
TITLE 2 SUBUNIT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ELONGATION FACTOR 1-GAMMA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN (RESIDUES 276-437);
COMPND 5 SYNONYM: EF-1-GAMMA, EEF-1B GAMMA, PRO1608;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: EEF1G OR EF1G;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET16B
KEYWDS ALPHA/BETA, TRANSLATION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.VANWETSWINKEL,J.KRIEK,G.R.ANDERSEN,P.GUNTERT,J.DIJK,G.W.CANTERS,
AUTHOR 2 G.SIEGAL
REVDAT 3 27-OCT-21 1PBU 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1PBU 1 VERSN
REVDAT 1 15-JUL-03 1PBU 0
JRNL AUTH S.VANWETSWINKEL,J.KRIEK,G.R.ANDERSEN,J.DIJK,G.SIEGAL
JRNL TITL 1H, (15)N AND (13)C RESONANCE ASSIGNMENTS OF THE HIGHLY
JRNL TITL 2 CONSERVED 19 KDA C-TERMINAL DOMAIN FROM HUMAN ELONGATION
JRNL TITL 3 FACTOR 1BGAMMA.
JRNL REF J.BIOMOL.NMR V. 26 189 2003
JRNL REFN ISSN 0925-2738
JRNL PMID 12766415
JRNL DOI 10.1023/A:1023504611632
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, OPALP
REMARK 3 AUTHORS : BRUKER (XWINNMR), KORADI, R. ET AL. (OPALP)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 3920 NOE-DERIVED DISTANCE CONSTRAINTS
REMARK 4
REMARK 4 1PBU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-MAY-03.
REMARK 100 THE DEPOSITION ID IS D_1000019219.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.5
REMARK 210 IONIC STRENGTH : 75MM KCL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM EEF1BGAMMA[276-437]U
REMARK 210 -15N,13C, 20MM TRIS-HCL PH7.5,
REMARK 210 75MM KCL, 1MM DTT, 0.02%NAN3 (W/
REMARK 210 V); 1MM EEF1BGAMMA[276-437]U-15N,
REMARK 210 20MM TRIS-HCL PH7.5, 75MM KCL,
REMARK 210 1MM DTT, 0.02%NAN3 (W/V)
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; STANDARD
REMARK 210 TRIPLE RESONANCE EXPERIMENTS;
REMARK 210 HCCH-TOCSY AND CCH-TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; AVANCE; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.1, XEASY 1.3.13, CYANA
REMARK 210 1.06, VNMR 5.1
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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 ARG A 414 HG SER A 418 1.58
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 1 ARG A 348 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 4 TYR A 297 CB - CG - CD1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 7 TYR A 323 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 9 TYR A 297 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 9 ARG A 378 CD - NE - CZ ANGL. DEV. = 8.7 DEGREES
REMARK 500 9 ARG A 378 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 10 TYR A 326 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 10 ARG A 327 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 10 ARG A 353 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 13 TYR A 323 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 15 ARG A 348 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 15 ARG A 378 NE - CZ - NH1 ANGL. DEV. = 3.3 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 1 ASP A 278 98.67 56.47
REMARK 500 1 PHE A 280 39.68 -87.53
REMARK 500 1 PRO A 284 -150.64 -81.85
REMARK 500 1 ARG A 295 -70.67 -77.14
REMARK 500 1 VAL A 305 -73.17 -120.80
REMARK 500 1 PHE A 314 -103.18 -68.06
REMARK 500 1 ASP A 315 39.70 171.27
REMARK 500 1 LYS A 316 -7.76 -58.05
REMARK 500 1 GLU A 325 39.33 -143.90
REMARK 500 1 TYR A 326 63.15 37.39
REMARK 500 1 ARG A 327 -19.19 -35.65
REMARK 500 1 PHE A 328 69.65 -115.50
REMARK 500 1 THR A 333 38.08 -152.21
REMARK 500 1 GLN A 334 -160.40 -160.55
REMARK 500 1 LEU A 349 38.58 -88.83
REMARK 500 1 LYS A 354 -8.57 -59.65
REMARK 500 1 ASN A 355 33.14 -153.81
REMARK 500 1 THR A 365 -164.19 -172.17
REMARK 500 1 SER A 368 88.17 -150.48
REMARK 500 1 ARG A 378 53.73 -101.64
REMARK 500 1 ALA A 383 -46.55 80.15
REMARK 500 1 PRO A 388 2.78 -65.82
REMARK 500 1 GLN A 391 45.58 -144.61
REMARK 500 1 VAL A 392 -95.82 -84.54
REMARK 500 1 SER A 406 -163.46 -77.24
REMARK 500 1 ALA A 422 -35.43 178.93
REMARK 500 1 LYS A 428 -139.59 -82.44
REMARK 500 1 ASN A 431 -59.63 -19.11
REMARK 500 1 PHE A 436 54.14 -101.91
REMARK 500 2 ASP A 278 114.00 67.81
REMARK 500 2 PHE A 280 38.31 -87.47
REMARK 500 2 PRO A 284 -160.90 -79.17
REMARK 500 2 LYS A 285 154.06 -47.94
REMARK 500 2 TYR A 297 -73.13 -44.65
REMARK 500 2 VAL A 305 -66.92 -120.10
REMARK 500 2 GLU A 312 -65.99 -91.02
REMARK 500 2 PHE A 314 -103.97 -64.29
REMARK 500 2 ASP A 315 48.22 174.43
REMARK 500 2 LYS A 316 -6.31 -57.89
REMARK 500 2 GLU A 325 64.32 -150.63
REMARK 500 2 TYR A 326 64.12 26.23
REMARK 500 2 PHE A 328 73.36 -108.75
REMARK 500 2 THR A 333 36.54 -148.96
REMARK 500 2 GLN A 334 99.74 -172.53
REMARK 500 2 LYS A 351 11.65 -66.88
REMARK 500 2 ALA A 383 -49.25 79.05
REMARK 500 2 TRP A 390 59.75 -105.14
REMARK 500 2 GLN A 391 52.26 -143.05
REMARK 500 2 VAL A 392 -87.62 -95.61
REMARK 500 2 SER A 406 -164.21 -104.01
REMARK 500
REMARK 500 THIS ENTRY HAS 462 RAMACHANDRAN OUTLIERS.
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 PHE A 430 ASN A 431 1 -149.91
REMARK 500 GLY A 318 TRP A 319 2 142.98
REMARK 500 GLY A 318 TRP A 319 4 142.30
REMARK 500 GLY A 318 TRP A 319 5 148.64
REMARK 500 SER A 369 SER A 370 7 149.03
REMARK 500 PHE A 430 ASN A 431 7 -149.41
REMARK 500 GLY A 318 TRP A 319 8 142.29
REMARK 500 PHE A 430 ASN A 431 9 -145.42
REMARK 500 ALA A 276 LYS A 277 10 138.45
REMARK 500 GLU A 420 GLY A 421 11 -137.57
REMARK 500 GLU A 420 GLY A 421 13 -149.23
REMARK 500 PHE A 430 ASN A 431 13 -149.22
REMARK 500 HIS A 313 PHE A 314 14 -134.25
REMARK 500 PHE A 430 ASN A 431 14 -144.04
REMARK 500 PHE A 430 ASN A 431 16 -143.59
REMARK 500 PHE A 430 ASN A 431 17 -147.48
REMARK 500 PRO A 284 LYS A 285 18 149.71
REMARK 500 GLY A 364 THR A 365 20 -147.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 TYR A 326 0.08 SIDE CHAIN
REMARK 500 1 ARG A 327 0.10 SIDE CHAIN
REMARK 500 1 PHE A 357 0.08 SIDE CHAIN
REMARK 500 1 ARG A 378 0.09 SIDE CHAIN
REMARK 500 1 TYR A 416 0.08 SIDE CHAIN
REMARK 500 3 ARG A 295 0.10 SIDE CHAIN
REMARK 500 3 ARG A 348 0.11 SIDE CHAIN
REMARK 500 3 ARG A 400 0.10 SIDE CHAIN
REMARK 500 4 PHE A 310 0.08 SIDE CHAIN
REMARK 500 4 ARG A 414 0.10 SIDE CHAIN
REMARK 500 5 TYR A 326 0.09 SIDE CHAIN
REMARK 500 6 ARG A 327 0.09 SIDE CHAIN
REMARK 500 7 ARG A 295 0.13 SIDE CHAIN
REMARK 500 7 TYR A 309 0.07 SIDE CHAIN
REMARK 500 7 ARG A 353 0.12 SIDE CHAIN
REMARK 500 10 ARG A 378 0.08 SIDE CHAIN
REMARK 500 10 TYR A 416 0.07 SIDE CHAIN
REMARK 500 11 TYR A 326 0.07 SIDE CHAIN
REMARK 500 13 TYR A 326 0.10 SIDE CHAIN
REMARK 500 13 ARG A 400 0.09 SIDE CHAIN
REMARK 500 13 TYR A 416 0.10 SIDE CHAIN
REMARK 500 14 TYR A 323 0.06 SIDE CHAIN
REMARK 500 14 ARG A 378 0.09 SIDE CHAIN
REMARK 500 14 TYR A 416 0.09 SIDE CHAIN
REMARK 500 16 ARG A 295 0.08 SIDE CHAIN
REMARK 500 16 TYR A 323 0.07 SIDE CHAIN
REMARK 500 16 TYR A 326 0.09 SIDE CHAIN
REMARK 500 16 ARG A 348 0.08 SIDE CHAIN
REMARK 500 16 ARG A 353 0.09 SIDE CHAIN
REMARK 500 17 ARG A 353 0.09 SIDE CHAIN
REMARK 500 17 TYR A 416 0.10 SIDE CHAIN
REMARK 500 18 TYR A 326 0.08 SIDE CHAIN
REMARK 500 18 ARG A 353 0.14 SIDE CHAIN
REMARK 500 19 TYR A 323 0.08 SIDE CHAIN
REMARK 500 19 TYR A 326 0.09 SIDE CHAIN
REMARK 500 19 ARG A 327 0.08 SIDE CHAIN
REMARK 500 20 ARG A 295 0.08 SIDE CHAIN
REMARK 500 20 TYR A 326 0.08 SIDE CHAIN
REMARK 500 20 ARG A 378 0.13 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5628 RELATED DB: BMRB
REMARK 900 CHEMICAL SHIFT ASSIGNMENTS
DBREF 1PBU A 276 437 UNP P26641 EF1G_HUMAN 276 437
SEQADV 1PBU ALA A 289 UNP P26641 VAL 289 ENGINEERED MUTATION
SEQRES 1 A 162 ALA LYS ASP PRO PHE ALA HIS LEU PRO LYS SER THR PHE
SEQRES 2 A 162 ALA LEU ASP GLU PHE LYS ARG LYS TYR SER ASN GLU ASP
SEQRES 3 A 162 THR LEU SER VAL ALA LEU PRO TYR PHE TRP GLU HIS PHE
SEQRES 4 A 162 ASP LYS ASP GLY TRP SER LEU TRP TYR SER GLU TYR ARG
SEQRES 5 A 162 PHE PRO GLU GLU LEU THR GLN THR PHE MET SER CYS ASN
SEQRES 6 A 162 LEU ILE THR GLY MET PHE GLN ARG LEU ASP LYS LEU ARG
SEQRES 7 A 162 LYS ASN ALA PHE ALA SER VAL ILE LEU PHE GLY THR ASN
SEQRES 8 A 162 ASN SER SER SER ILE SER GLY VAL TRP VAL PHE ARG GLY
SEQRES 9 A 162 GLN GLU LEU ALA PHE PRO LEU SER PRO ASP TRP GLN VAL
SEQRES 10 A 162 ASP TYR GLU SER TYR THR TRP ARG LYS LEU ASP PRO GLY
SEQRES 11 A 162 SER GLU GLU THR GLN THR LEU VAL ARG GLU TYR PHE SER
SEQRES 12 A 162 TRP GLU GLY ALA PHE GLN HIS VAL GLY LYS ALA PHE ASN
SEQRES 13 A 162 GLN GLY LYS ILE PHE LYS
HELIX 1 1 ASP A 278 HIS A 282 5 5
HELIX 2 2 ALA A 289 GLU A 300 1 12
HELIX 3 3 ASP A 301 SER A 304 5 4
HELIX 4 4 VAL A 305 GLU A 312 1 8
HELIX 5 5 PHE A 328 LEU A 332 5 5
HELIX 6 6 MET A 337 LEU A 349 1 13
HELIX 7 7 ASP A 350 LYS A 354 5 5
HELIX 8 8 ALA A 383 GLN A 391 5 9
HELIX 9 9 ASP A 393 TYR A 397 5 5
HELIX 10 10 GLU A 407 TRP A 419 1 13
SHEET 1 A 4 ALA A 356 ALA A 358 0
SHEET 2 A 4 SER A 370 PHE A 377 -1 O VAL A 376 N PHE A 357
SHEET 3 A 4 SER A 320 SER A 324 -1 N SER A 324 O GLY A 373
SHEET 4 A 4 ARG A 400 LYS A 401 -1 O ARG A 400 N TYR A 323
SHEET 1 B 4 ALA A 356 ALA A 358 0
SHEET 2 B 4 SER A 370 PHE A 377 -1 O VAL A 376 N PHE A 357
SHEET 3 B 4 ILE A 361 PHE A 363 -1 N PHE A 363 O SER A 370
SHEET 4 B 4 GLN A 432 GLY A 433 -1 O GLN A 432 N LEU A 362
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
MODEL 1
Complete list - t 27 2 Bytes