Header list of 2ese.pdb file
Complete list - r 9 2 Bytes
HEADER PROTEIN/RNA COMPLEX 26-OCT-05 2ESE
TITLE STRUCTURE OF THE SAM DOMAIN OF VTS1P IN COMPLEX WITH RNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5'-R(*GP*GP*AP*GP*AP*GP*GP*CP*UP*CP*UP*GP*GP*CP*AP*GP*CP*UP
COMPND 3 *UP*UP*UP*CP*C)-3';
COMPND 4 CHAIN: B;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: SRE RNA;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: VTS1P;
COMPND 9 CHAIN: A;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: RNA WAS PREPARED BY IN VITRO TRANSCRIPTION;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 6 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 7 ORGANISM_TAXID: 4932;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)+RIL;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PET28
KEYWDS PROTEIN-RNA COMPLEX, SHAPE SPECIFIC RECOGNITION, SAM DOMAIN, STEM-
KEYWDS 2 LOOP, PROTEIN-RNA COMPLEX COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR F.H.T.ALLAIN
REVDAT 4 09-MAR-22 2ESE 1 REMARK SEQADV
REVDAT 3 24-FEB-09 2ESE 1 VERSN
REVDAT 2 30-OCT-07 2ESE 1 JRNL
REVDAT 1 24-JAN-06 2ESE 0
JRNL AUTH F.C.OBERSTRASS,A.LEE,R.STEFL,M.JANIS,G.CHANFREAU,F.H.ALLAIN
JRNL TITL SHAPE-SPECIFIC RECOGNITION IN THE STRUCTURE OF THE VTS1P SAM
JRNL TITL 2 DOMAIN WITH RNA.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 13 160 2006
JRNL REFN ISSN 1545-9993
JRNL PMID 16429156
JRNL DOI 10.1038/NSMB1038
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, AMBER 7.0
REMARK 3 AUTHORS : BRUKER (XWINNMR), CASE, DA (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINED WITH NOES, DIHEDRAL ANGLES, AND
REMARK 3 RESIDUAL DIPOLAR COUPLINGS
REMARK 4
REMARK 4 2ESE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-NOV-05.
REMARK 100 THE DEPOSITION ID IS D_1000035034.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 50MM NACL, 50MM PHOSPHATE-BUFFER
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 0.8MM PROTEIN, 0.8MM RNA
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 900 MHZ; 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : SPARKY, AMBER 7.0
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 MET A 423
REMARK 465 GLY A 424
REMARK 465 SER A 425
REMARK 465 SER A 426
REMARK 465 HIS A 427
REMARK 465 HIS A 428
REMARK 465 HIS A 429
REMARK 465 HIS A 430
REMARK 465 HIS A 431
REMARK 465 HIS A 432
REMARK 465 SER A 433
REMARK 465 SER A 434
REMARK 465 GLY A 435
REMARK 465 LEU A 436
REMARK 465 VAL A 437
REMARK 465 PRO A 438
REMARK 465 ARG A 439
REMARK 465 GLY A 440
REMARK 465 SER A 441
REMARK 465 HIS A 442
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 A B 526 C5 - C6 - N1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 1 A B 528 C5 - C6 - N1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 1 C B 531 N3 - C2 - O2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 1 C B 533 C5' - C4' - C3' ANGL. DEV. = -8.5 DEGREES
REMARK 500 1 C B 533 C5' - C4' - O4' ANGL. DEV. = 6.3 DEGREES
REMARK 500 1 C B 533 O4' - C1' - N1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 1 C B 533 N3 - C2 - O2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 1 C B 537 N1 - C2 - O2 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 C B 537 N3 - C2 - O2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 1 A B 538 C5 - C6 - N1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 1 C B 540 O4' - C1' - N1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 1 C B 540 N1 - C2 - O2 ANGL. DEV. = 3.8 DEGREES
REMARK 500 1 C B 540 N3 - C2 - O2 ANGL. DEV. = -5.3 DEGREES
REMARK 500 1 U B 541 O4' - C1' - N1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 1 C B 545 N3 - C2 - O2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 1 C B 546 N3 - C2 - O2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 1 ARG A 520 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 2 A B 526 C5 - C6 - N1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 2 A B 528 C5 - C6 - N1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 2 C B 531 N3 - C2 - O2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 2 C B 533 C5' - C4' - C3' ANGL. DEV. = -8.9 DEGREES
REMARK 500 2 C B 533 C5' - C4' - O4' ANGL. DEV. = 6.8 DEGREES
REMARK 500 2 C B 533 N3 - C2 - O2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 2 C B 537 N1 - C2 - O2 ANGL. DEV. = 4.4 DEGREES
REMARK 500 2 C B 537 N3 - C2 - O2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 2 C B 537 C3' - O3' - P ANGL. DEV. = 9.9 DEGREES
REMARK 500 2 A B 538 C4 - C5 - C6 ANGL. DEV. = -3.1 DEGREES
REMARK 500 2 A B 538 C5 - C6 - N1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 A B 538 N1 - C6 - N6 ANGL. DEV. = -3.7 DEGREES
REMARK 500 2 C B 540 O4' - C1' - N1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 2 C B 540 N1 - C2 - O2 ANGL. DEV. = 3.9 DEGREES
REMARK 500 2 C B 540 N3 - C2 - O2 ANGL. DEV. = -5.3 DEGREES
REMARK 500 2 U B 541 O4' - C1' - N1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 2 U B 542 O4' - C1' - N1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 2 C B 545 N3 - C2 - O2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 2 C B 546 N3 - C2 - O2 ANGL. DEV. = -5.1 DEGREES
REMARK 500 2 ILE A 481 CA - CB - CG1 ANGL. DEV. = 11.5 DEGREES
REMARK 500 3 A B 526 C5 - C6 - N1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 3 A B 528 C5 - C6 - N1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 3 C B 531 N1 - C2 - O2 ANGL. DEV. = 3.6 DEGREES
REMARK 500 3 C B 531 N3 - C2 - O2 ANGL. DEV. = -5.1 DEGREES
REMARK 500 3 C B 533 C5' - C4' - O4' ANGL. DEV. = 5.6 DEGREES
REMARK 500 3 C B 533 O4' - C1' - N1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 3 C B 537 N1 - C2 - O2 ANGL. DEV. = 4.4 DEGREES
REMARK 500 3 C B 537 N3 - C2 - O2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 3 A B 538 C5 - C6 - N1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 3 C B 540 O4' - C1' - N1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 3 C B 540 N1 - C2 - O2 ANGL. DEV. = 3.8 DEGREES
REMARK 500 3 C B 540 N3 - C2 - O2 ANGL. DEV. = -5.3 DEGREES
REMARK 500 3 C B 545 N3 - C2 - O2 ANGL. DEV. = -4.9 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 350 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 1 SER A 446 -80.33 -141.17
REMARK 500 1 LEU A 447 -37.65 63.40
REMARK 500 1 THR A 448 27.26 -68.63
REMARK 500 1 ARG A 464 16.39 57.99
REMARK 500 1 HIS A 466 6.15 -60.08
REMARK 500 1 ILE A 478 -26.83 -34.17
REMARK 500 1 VAL A 493 63.87 -102.39
REMARK 500 1 ILE A 508 -70.69 -70.73
REMARK 500 2 SER A 446 -26.84 -161.97
REMARK 500 2 LEU A 447 -33.39 65.36
REMARK 500 2 THR A 448 22.37 -73.50
REMARK 500 2 HIS A 466 19.07 -62.95
REMARK 500 2 ILE A 478 -27.22 -35.00
REMARK 500 2 VAL A 493 61.37 -109.92
REMARK 500 2 ILE A 508 -71.19 -70.39
REMARK 500 3 PRO A 444 106.15 -52.42
REMARK 500 3 LEU A 447 -64.44 -137.52
REMARK 500 3 HIS A 466 8.42 -62.27
REMARK 500 3 ILE A 478 -25.71 -36.08
REMARK 500 3 LEU A 483 175.01 -56.50
REMARK 500 3 VAL A 493 63.72 -102.50
REMARK 500 4 SER A 446 -75.86 -151.45
REMARK 500 4 LEU A 447 -47.92 63.00
REMARK 500 4 THR A 448 21.16 -66.44
REMARK 500 4 HIS A 466 10.79 -61.59
REMARK 500 4 ILE A 478 -25.11 -34.30
REMARK 500 4 LEU A 483 170.08 -58.92
REMARK 500 4 VAL A 493 64.12 -106.96
REMARK 500 4 ILE A 508 -71.66 -71.03
REMARK 500 4 ASP A 519 7.18 -69.13
REMARK 500 4 ARG A 520 -0.39 51.02
REMARK 500 5 LYS A 445 -85.96 57.67
REMARK 500 5 THR A 448 16.42 -65.99
REMARK 500 5 HIS A 466 18.35 -63.24
REMARK 500 5 ILE A 478 -26.64 -34.53
REMARK 500 5 LEU A 483 171.01 -56.59
REMARK 500 5 VAL A 493 62.64 -107.13
REMARK 500 5 ILE A 508 -70.17 -70.16
REMARK 500 6 LYS A 445 -38.17 -151.57
REMARK 500 6 THR A 448 32.38 -66.19
REMARK 500 6 HIS A 466 19.78 -63.75
REMARK 500 6 ILE A 478 -27.43 -35.38
REMARK 500 6 VAL A 493 64.60 -106.51
REMARK 500 6 ILE A 508 -70.92 -69.99
REMARK 500 7 THR A 448 17.03 -68.43
REMARK 500 7 HIS A 466 8.08 -58.13
REMARK 500 7 ILE A 478 -25.58 -33.88
REMARK 500 7 LEU A 483 170.73 -59.30
REMARK 500 7 VAL A 493 67.00 -101.22
REMARK 500 7 ILE A 508 -71.21 -69.28
REMARK 500
REMARK 500 THIS ENTRY HAS 148 RAMACHANDRAN OUTLIERS.
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 C B 531 0.07 SIDE CHAIN
REMARK 500 1 C B 533 0.06 SIDE CHAIN
REMARK 500 1 G B 535 0.07 SIDE CHAIN
REMARK 500 1 G B 536 0.07 SIDE CHAIN
REMARK 500 2 C B 531 0.06 SIDE CHAIN
REMARK 500 2 C B 533 0.09 SIDE CHAIN
REMARK 500 3 C B 531 0.08 SIDE CHAIN
REMARK 500 3 C B 533 0.06 SIDE CHAIN
REMARK 500 3 C B 537 0.10 SIDE CHAIN
REMARK 500 4 C B 531 0.07 SIDE CHAIN
REMARK 500 4 C B 533 0.10 SIDE CHAIN
REMARK 500 4 G B 536 0.07 SIDE CHAIN
REMARK 500 5 C B 531 0.07 SIDE CHAIN
REMARK 500 5 C B 533 0.07 SIDE CHAIN
REMARK 500 5 G B 536 0.08 SIDE CHAIN
REMARK 500 6 G B 535 0.05 SIDE CHAIN
REMARK 500 6 G B 536 0.08 SIDE CHAIN
REMARK 500 6 C B 537 0.09 SIDE CHAIN
REMARK 500 7 C B 531 0.08 SIDE CHAIN
REMARK 500 7 C B 533 0.07 SIDE CHAIN
REMARK 500 7 G B 536 0.07 SIDE CHAIN
REMARK 500 7 C B 537 0.07 SIDE CHAIN
REMARK 500 8 C B 531 0.06 SIDE CHAIN
REMARK 500 8 G B 536 0.09 SIDE CHAIN
REMARK 500 9 G B 529 0.06 SIDE CHAIN
REMARK 500 9 G B 536 0.08 SIDE CHAIN
REMARK 500 9 C B 537 0.08 SIDE CHAIN
REMARK 500 9 C B 540 0.06 SIDE CHAIN
REMARK 500 10 C B 533 0.09 SIDE CHAIN
REMARK 500 10 C B 537 0.08 SIDE CHAIN
REMARK 500 11 C B 531 0.07 SIDE CHAIN
REMARK 500 11 G B 536 0.10 SIDE CHAIN
REMARK 500 12 G B 529 0.06 SIDE CHAIN
REMARK 500 12 C B 533 0.07 SIDE CHAIN
REMARK 500 12 G B 536 0.10 SIDE CHAIN
REMARK 500 12 C B 540 0.06 SIDE CHAIN
REMARK 500 13 G B 525 0.06 SIDE CHAIN
REMARK 500 13 C B 531 0.06 SIDE CHAIN
REMARK 500 13 G B 536 0.09 SIDE CHAIN
REMARK 500 14 C B 531 0.08 SIDE CHAIN
REMARK 500 14 C B 533 0.10 SIDE CHAIN
REMARK 500 14 G B 536 0.06 SIDE CHAIN
REMARK 500 14 C B 537 0.08 SIDE CHAIN
REMARK 500 14 G B 539 0.06 SIDE CHAIN
REMARK 500 14 C B 540 0.06 SIDE CHAIN
REMARK 500 14 C B 546 0.06 SIDE CHAIN
REMARK 500 15 C B 533 0.07 SIDE CHAIN
REMARK 500 15 G B 536 0.09 SIDE CHAIN
REMARK 500 15 C B 537 0.08 SIDE CHAIN
REMARK 500 16 C B 533 0.06 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 66 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2ESE A 444 523 GB 6324935 NP_015004 444 523
DBREF 2ESE B 524 546 PDB 2ESE 2ESE 524 546
SEQADV 2ESE MET A 423 GB 6324935 EXPRESSION TAG
SEQADV 2ESE GLY A 424 GB 6324935 EXPRESSION TAG
SEQADV 2ESE SER A 425 GB 6324935 EXPRESSION TAG
SEQADV 2ESE SER A 426 GB 6324935 EXPRESSION TAG
SEQADV 2ESE HIS A 427 GB 6324935 EXPRESSION TAG
SEQADV 2ESE HIS A 428 GB 6324935 EXPRESSION TAG
SEQADV 2ESE HIS A 429 GB 6324935 EXPRESSION TAG
SEQADV 2ESE HIS A 430 GB 6324935 EXPRESSION TAG
SEQADV 2ESE HIS A 431 GB 6324935 EXPRESSION TAG
SEQADV 2ESE HIS A 432 GB 6324935 EXPRESSION TAG
SEQADV 2ESE SER A 433 GB 6324935 EXPRESSION TAG
SEQADV 2ESE SER A 434 GB 6324935 EXPRESSION TAG
SEQADV 2ESE GLY A 435 GB 6324935 EXPRESSION TAG
SEQADV 2ESE LEU A 436 GB 6324935 EXPRESSION TAG
SEQADV 2ESE VAL A 437 GB 6324935 EXPRESSION TAG
SEQADV 2ESE PRO A 438 GB 6324935 EXPRESSION TAG
SEQADV 2ESE ARG A 439 GB 6324935 EXPRESSION TAG
SEQADV 2ESE GLY A 440 GB 6324935 EXPRESSION TAG
SEQADV 2ESE SER A 441 GB 6324935 EXPRESSION TAG
SEQADV 2ESE HIS A 442 GB 6324935 EXPRESSION TAG
SEQADV 2ESE MET A 443 GB 6324935 EXPRESSION TAG
SEQRES 1 B 23 G G A G A G G C U C U G G
SEQRES 2 B 23 C A G C U U U U C C
SEQRES 1 A 101 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 101 LEU VAL PRO ARG GLY SER HIS MET PRO LYS SER LEU THR
SEQRES 3 A 101 ASP PRO LYS LEU LEU LYS ASN ILE PRO MET TRP LEU LYS
SEQRES 4 A 101 SER LEU ARG LEU HIS LYS TYR SER ASP ALA LEU SER GLY
SEQRES 5 A 101 THR PRO TRP ILE GLU LEU ILE TYR LEU ASP ASP GLU THR
SEQRES 6 A 101 LEU GLU LYS LYS GLY VAL LEU ALA LEU GLY ALA ARG ARG
SEQRES 7 A 101 LYS LEU LEU LYS ALA PHE GLY ILE VAL ILE ASP TYR LYS
SEQRES 8 A 101 GLU ARG ASP LEU ILE ASP ARG SER ALA TYR
HELIX 1 1 ASP A 449 ASN A 455 1 7
HELIX 2 2 ASN A 455 SER A 462 1 8
HELIX 3 3 TYR A 468 SER A 473 1 6
HELIX 4 4 PRO A 476 ILE A 481 1 6
HELIX 5 5 ASP A 484 GLY A 492 1 9
HELIX 6 6 ALA A 495 ASP A 516 1 22
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 - r 9 2 Bytes