HEADER TRANSLATION 17-AUG-18 6HD5
TITLE CRYO-EM STRUCTURE OF THE RIBOSOME-NATA COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: N-TERMINAL ACETYLTRANSFERASE A COMPLEX SUBUNIT NAT1;
COMPND 3 CHAIN: t;
COMPND 4 SYNONYM: NATA COMPLEX SUBUNIT NAT1,AMINO-TERMINAL,ALPHA-AMINO,
COMPND 5 ACETYLTRANSFERASE 1;
COMPND 6 OTHER_DETAILS: RIBOSOME BINDING SUBUNIT;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: N-TERMINAL ACETYLTRANSFERASE A COMPLEX CATALYTIC SUBUNIT
COMPND 9 ARD1;
COMPND 10 CHAIN: u;
COMPND 11 SYNONYM: NATA COMPLEX SUBUNIT ARD1,ARREST-DEFECTIVE PROTEIN 1;
COMPND 12 EC: 2.3.1.255;
COMPND 13 OTHER_DETAILS: CATALYTIC SUBUNIT;
COMPND 14 MOL_ID: 3;
COMPND 15 MOLECULE: N-ALPHA-ACETYLTRANSFERASE NAT5;
COMPND 16 CHAIN: v;
COMPND 17 SYNONYM: NATA COMPLEX SUBUNIT NAT5;
COMPND 18 EC: 2.3.1.258;
COMPND 19 OTHER_DETAILS: RIBOSOME BINDING SUBUNIT
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 3 S288C);
SOURCE 4 ORGANISM_TAXID: 559292;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 7 S288C);
SOURCE 8 ORGANISM_TAXID: 559292;
SOURCE 9 MOL_ID: 3;
SOURCE 10 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 11 S288C);
SOURCE 12 ORGANISM_TAXID: 559292
KEYWDS N-TERMINAL ACETYLATION, PROTEIN MODIFICATION, RIBOSOME, EXPANSION
KEYWDS 2 SEGMENTS, TRANSLATION
EXPDTA ELECTRON MICROSCOPY
AUTHOR A.G.KNORR,T.BECKER,R.BECKMANN
REVDAT 3 16-JAN-19 6HD5 1 JRNL
REVDAT 2 26-DEC-18 6HD5 1 JRNL
REVDAT 1 19-DEC-18 6HD5 0
JRNL AUTH A.G.KNORR,C.SCHMIDT,P.TESINA,O.BERNINGHAUSEN,T.BECKER,
JRNL AUTH 2 B.BEATRIX,R.BECKMANN
JRNL TITL RIBOSOME-NATA ARCHITECTURE REVEALS THAT RRNA EXPANSION
JRNL TITL 2 SEGMENTS COORDINATE N-TERMINAL ACETYLATION.
JRNL REF NAT. STRUCT. MOL. BIOL. V. 26 35 2019
JRNL REFN ESSN 1545-9985
JRNL PMID 30559462
JRNL DOI 10.1038/S41594-018-0165-Y
REMARK 2
REMARK 2 RESOLUTION. 4.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : GAUTOMATCH, GCTF, RELION, RELION,
REMARK 3 RELION
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 : NULL
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) : 4.800
REMARK 3 NUMBER OF PARTICLES : 262507
REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE
REMARK 3 CORRECTION
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: NULL
REMARK 4
REMARK 4 6HD5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-AUG-18.
REMARK 100 THE DEPOSITION ID IS D_1200011427.
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE
REMARK 245 SPECIMEN TYPE : NULL
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE TYPE : PARTICLE
REMARK 245 PARTICLE TYPE : POINT
REMARK 245 NAME OF SAMPLE : RIBOSOME-NATA COMPLEX
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 7.50
REMARK 245 SAMPLE DETAILS : MAP WAS REFINED ON NATA.
REMARK 245 COORDINATES ARE DEPOSITED FOR NATA ONLY.
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS
REMARK 245 DETECTOR TYPE : FEI FALCON II (4K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : NULL
REMARK 245 MAXIMUM DEFOCUS (NM) : NULL
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : NULL
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 2.50
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
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 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 61800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: t, u, v
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 t 1
REMARK 465 SER t 2
REMARK 465 ARG t 3
REMARK 465 LYS t 4
REMARK 465 ARG t 5
REMARK 465 SER t 6
REMARK 465 THR t 7
REMARK 465 LYS t 8
REMARK 465 PRO t 9
REMARK 465 LYS t 10
REMARK 465 PRO t 11
REMARK 465 ALA t 12
REMARK 465 ALA t 13
REMARK 465 LYS t 14
REMARK 465 ILE t 15
REMARK 465 ALA t 16
REMARK 465 MET u 1
REMARK 465 ILE u 237
REMARK 465 VAL u 238
REMARK 465 MET v 1
REMARK 465 GLY v 2
REMARK 465 ASP v 43
REMARK 465 SER v 44
REMARK 465 LEU v 45
REMARK 465 VAL v 46
REMARK 465 ALA v 47
REMARK 465 LYS v 48
REMARK 465 ASN v 49
REMARK 465 LYS v 50
REMARK 465 LYS v 51
REMARK 465 PRO v 52
REMARK 465 SER v 53
REMARK 465 SER v 54
REMARK 465 LYS v 55
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 t 17 CG CD1 CD2
REMARK 470 LYS t 18 CG CD CE NZ
REMARK 470 LYS t 19 CG CD CE NZ
REMARK 470 LEU t 25 CG CD1 CD2
REMARK 470 LEU t 28 CG CD1 CD2
REMARK 470 GLN t 35 CG CD OE1 NE2
REMARK 470 LYS t 38 CG CD CE NZ
REMARK 470 LEU t 40 CG CD1 CD2
REMARK 470 LYS t 41 CG CD CE NZ
REMARK 470 LEU t 42 CG CD1 CD2
REMARK 470 LYS t 48 CG CD CE NZ
REMARK 470 LYS t 49 CG CD CE NZ
REMARK 470 SER t 75 OG
REMARK 470 GLU t 85 CG CD OE1 OE2
REMARK 470 SER t 88 OG
REMARK 470 LYS t 516 CG CD CE NZ
REMARK 470 LYS t 517 CG CD CE NZ
REMARK 470 LYS t 525 CG CD CE NZ
REMARK 470 LYS t 526 CG CD CE NZ
REMARK 470 GLU t 527 CG CD OE1 OE2
REMARK 470 VAL t 528 CG1 CG2
REMARK 470 GLU t 529 CG CD OE1 OE2
REMARK 470 SER t 530 OG
REMARK 470 ASP t 531 CG OD1 OD2
REMARK 470 LYS t 532 CG CD CE NZ
REMARK 470 SER t 533 OG
REMARK 470 GLU t 534 CG CD OE1 OE2
REMARK 470 LYS t 541 CG CD CE NZ
REMARK 470 ARG t 625 CG CD NE CZ NH1 NH2
REMARK 470 LYS t 626 CG CD CE NZ
REMARK 470 SER t 627 OG
REMARK 470 ASP t 628 CG OD1 OD2
REMARK 470 SER t 629 OG
REMARK 470 LEU t 630 CG CD1 CD2
REMARK 470 ASP t 631 CG OD1 OD2
REMARK 470 GLU t 632 CG CD OE1 OE2
REMARK 470 ASN t 633 CG OD1 ND2
REMARK 470 SER t 634 OG
REMARK 470 ASP t 635 CG OD1 OD2
REMARK 470 GLU t 636 CG CD OE1 OE2
REMARK 470 ILE t 637 CG1 CG2 CD1
REMARK 470 GLN t 638 CG CD OE1 NE2
REMARK 470 ASN t 639 CG OD1 ND2
REMARK 470 ASN t 640 CG OD1 ND2
REMARK 470 GLN t 642 CG CD OE1 NE2
REMARK 470 ASN t 643 CG OD1 ND2
REMARK 470 SER t 644 OG
REMARK 470 SER t 645 OG
REMARK 470 GLN t 647 CG CD OE1 NE2
REMARK 470 LYS t 648 CG CD CE NZ
REMARK 470 LYS t 649 CG CD CE NZ
REMARK 470 LYS t 650 CG CD CE NZ
REMARK 470 LYS t 652 CG CD CE NZ
REMARK 470 LYS t 653 CG CD CE NZ
REMARK 470 GLU t 654 CG CD OE1 OE2
REMARK 470 MET t 658 CG SD CE
REMARK 470 ASN t 659 CG OD1 ND2
REMARK 470 LYS t 660 CG CD CE NZ
REMARK 470 LYS t 662 CG CD CE NZ
REMARK 470 GLU t 663 CG CD OE1 OE2
REMARK 470 THR t 664 OG1 CG2
REMARK 470 GLU t 709 CD OE1 OE2
REMARK 470 LYS t 807 CG CD CE NZ
REMARK 470 SER u 57 OG
REMARK 470 ASP u 58 CG OD1 OD2
REMARK 470 GLU u 59 CG CD OE1 OE2
REMARK 470 GLN u 60 CG CD OE1 NE2
REMARK 470 ASP u 61 CG OD1 OD2
REMARK 470 GLU u 62 CG CD OE1 OE2
REMARK 470 ASN u 63 CG OD1 ND2
REMARK 470 ASP u 64 CG OD1 OD2
REMARK 470 LYS u 65 CG CD CE NZ
REMARK 470 LEU u 66 CG CD1 CD2
REMARK 470 GLU u 67 CG CD OE1 OE2
REMARK 470 LEU u 68 CG CD1 CD2
REMARK 470 THR u 69 OG1 CG2
REMARK 470 LEU u 70 CG CD1 CD2
REMARK 470 ASP u 71 CG OD1 OD2
REMARK 470 THR u 73 OG1 CG2
REMARK 470 ASN u 74 CG OD1 ND2
REMARK 470 ASP u 75 CG OD1 OD2
REMARK 470 ASP u 105 CG OD1 OD2
REMARK 470 GLN u 106 CG CD OE1 NE2
REMARK 470 GLN u 107 CG CD OE1 NE2
REMARK 470 LEU u 209 CG CD1 CD2
REMARK 470 LYS u 210 CG CD CE NZ
REMARK 470 GLU u 211 CG CD OE1 OE2
REMARK 470 ASN u 212 CG OD1 ND2
REMARK 470 GLU u 213 CG CD OE1 OE2
REMARK 470 SER u 222 OG
REMARK 470 ASP u 227 CG OD1 OD2
REMARK 470 ILE u 228 CG1 CG2 CD1
REMARK 470 ILE u 229 CG1 CG2 CD1
REMARK 470 LYS u 230 CG CD CE NZ
REMARK 470 GLN u 231 CG CD OE1 NE2
REMARK 470 VAL u 233 CG1 CG2
REMARK 470 ASN u 234 CG OD1 ND2
REMARK 470 ASP u 235 CG OD1 OD2
REMARK 470 ILE u 236 CG1 CG2 CD1
REMARK 470 GLU v 42 CG CD OE1 OE2
REMARK 470 LYS v 56 CG CD CE NZ
REMARK 470 LYS v 82 CG CD CE NZ
REMARK 470 GLN v 83 CG CD OE1 NE2
REMARK 470 ASN v 84 CG OD1 ND2
REMARK 470 SER v 87 OG
REMARK 470 ASP v 164 CG OD1 OD2
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 LYS t 18 -58.79 -150.21
REMARK 500 TYR t 36 -44.65 -131.15
REMARK 500 SER t 52 37.41 -97.44
REMARK 500 GLU t 85 -63.66 -101.25
REMARK 500 ALA t 87 69.88 -107.06
REMARK 500 ASP t 140 95.41 -67.95
REMARK 500 LEU t 156 56.51 -115.03
REMARK 500 ASN t 172 -70.66 -67.23
REMARK 500 ALA t 189 56.33 -114.89
REMARK 500 LYS t 192 42.89 -98.19
REMARK 500 SER t 217 -131.48 59.19
REMARK 500 LEU t 254 -93.84 -100.41
REMARK 500 PRO t 342 28.53 -79.86
REMARK 500 ALA t 343 20.35 -143.07
REMARK 500 LYS t 356 -89.45 -157.69
REMARK 500 PHE t 400 -45.81 -130.12
REMARK 500 LEU t 449 76.16 -106.28
REMARK 500 GLN t 450 -18.40 -149.45
REMARK 500 LEU t 477 -60.34 -137.62
REMARK 500 ASP t 482 -83.91 -126.71
REMARK 500 ASP t 483 35.33 -94.04
REMARK 500 ASN t 486 -163.09 -129.09
REMARK 500 GLU t 495 71.94 58.90
REMARK 500 SER t 497 -51.03 -154.56
REMARK 500 VAL t 528 -123.17 58.19
REMARK 500 ALA t 537 -16.11 -142.72
REMARK 500 ALA t 560 -49.60 -147.00
REMARK 500 SER t 629 -151.90 59.32
REMARK 500 ASP t 631 75.86 56.01
REMARK 500 GLN t 638 -139.78 57.39
REMARK 500 ASN t 639 -131.35 -110.34
REMARK 500 ASN t 643 -119.43 56.07
REMARK 500 SER t 645 39.86 -156.28
REMARK 500 SER t 646 75.18 55.29
REMARK 500 ALA t 671 -46.13 -134.25
REMARK 500 ARG t 708 -145.47 -84.86
REMARK 500 ARG t 723 34.90 -92.30
REMARK 500 PHE t 765 -134.34 -144.62
REMARK 500 GLU t 780 -71.99 -87.10
REMARK 500 ASN t 784 -50.99 -131.37
REMARK 500 LYS t 804 -76.44 -82.44
REMARK 500 TYR t 819 71.79 -108.11
REMARK 500 SER t 827 -58.76 -151.36
REMARK 500 LEU t 841 -159.10 -140.50
REMARK 500 ASN u 23 -108.43 -136.72
REMARK 500 GLU u 42 54.07 -95.95
REMARK 500 ALA u 43 -46.97 -156.60
REMARK 500 THR u 48 -164.21 -123.80
REMARK 500 CYS u 54 84.16 -156.05
REMARK 500 GLU u 55 80.10 54.38
REMARK 500
REMARK 500 THIS ENTRY HAS 98 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4XNH RELATED DB: PDB
REMARK 900 S. CEREVISIAE NATA COMPLEX
REMARK 900 RELATED ID: 4KVM RELATED DB: PDB
REMARK 900 S. POMBE NATA COMPLEX
REMARK 900 RELATED ID: EMD-0201 RELATED DB: EMDB
REMARK 900 CRYO-EM STRUCTURE OF THE RIBOSOME-NATA COMPLEX
DBREF 6HD5 t 1 854 UNP P12945 NAT1_YEAST 1 854
DBREF 6HD5 u 1 238 UNP P07347 ARD1_YEAST 1 238
DBREF 6HD5 v 1 176 UNP Q08689 NAT5_YEAST 1 176
SEQRES 1 t 854 MET SER ARG LYS ARG SER THR LYS PRO LYS PRO ALA ALA
SEQRES 2 t 854 LYS ILE ALA LEU LYS LYS GLU ASN ASP GLN PHE LEU GLU
SEQRES 3 t 854 ALA LEU LYS LEU TYR GLU GLY LYS GLN TYR LYS LYS SER
SEQRES 4 t 854 LEU LYS LEU LEU ASP ALA ILE LEU LYS LYS ASP GLY SER
SEQRES 5 t 854 HIS VAL ASP SER LEU ALA LEU LYS GLY LEU ASP LEU TYR
SEQRES 6 t 854 SER VAL GLY GLU LYS ASP ASP ALA ALA SER TYR VAL ALA
SEQRES 7 t 854 ASN ALA ILE ARG LYS ILE GLU GLY ALA SER ALA SER PRO
SEQRES 8 t 854 ILE CYS CYS HIS VAL LEU GLY ILE TYR MET ARG ASN THR
SEQRES 9 t 854 LYS GLU TYR LYS GLU SER ILE LYS TRP PHE THR ALA ALA
SEQRES 10 t 854 LEU ASN ASN GLY SER THR ASN LYS GLN ILE TYR ARG ASP
SEQRES 11 t 854 LEU ALA THR LEU GLN SER GLN ILE GLY ASP PHE LYS ASN
SEQRES 12 t 854 ALA LEU VAL SER ARG LYS LYS TYR TRP GLU ALA PHE LEU
SEQRES 13 t 854 GLY TYR ARG ALA ASN TRP THR SER LEU ALA VAL ALA GLN
SEQRES 14 t 854 ASP VAL ASN GLY GLU ARG GLN GLN ALA ILE ASN THR LEU
SEQRES 15 t 854 SER GLN PHE GLU LYS LEU ALA GLU GLY LYS ILE SER ASP
SEQRES 16 t 854 SER GLU LYS TYR GLU HIS SER GLU CYS LEU MET TYR LYS
SEQRES 17 t 854 ASN ASP ILE MET TYR LYS ALA ALA SER ASP ASN GLN ASP
SEQRES 18 t 854 LYS LEU GLN ASN VAL LEU LYS HIS LEU ASN ASP ILE GLU
SEQRES 19 t 854 PRO CYS VAL PHE ASP LYS PHE GLY LEU LEU GLU ARG LYS
SEQRES 20 t 854 ALA THR ILE TYR MET LYS LEU GLY GLN LEU LYS ASP ALA
SEQRES 21 t 854 SER ILE VAL TYR ARG THR LEU ILE LYS ARG ASN PRO ASP
SEQRES 22 t 854 ASN PHE LYS TYR TYR LYS LEU LEU GLU VAL SER LEU GLY
SEQRES 23 t 854 ILE GLN GLY ASP ASN LYS LEU LYS LYS ALA LEU TYR GLY
SEQRES 24 t 854 LYS LEU GLU GLN PHE TYR PRO ARG CYS GLU PRO PRO LYS
SEQRES 25 t 854 PHE ILE PRO LEU THR PHE LEU GLN ASP LYS GLU GLU LEU
SEQRES 26 t 854 SER LYS LYS LEU ARG GLU TYR VAL LEU PRO GLN LEU GLU
SEQRES 27 t 854 ARG GLY VAL PRO ALA THR PHE SER ASN VAL LYS PRO LEU
SEQRES 28 t 854 TYR GLN ARG ARG LYS SER LYS VAL SER PRO LEU LEU GLU
SEQRES 29 t 854 LYS ILE VAL LEU ASP TYR LEU SER GLY LEU ASP PRO THR
SEQRES 30 t 854 GLN ASP PRO ILE PRO PHE ILE TRP THR ASN TYR TYR LEU
SEQRES 31 t 854 SER GLN HIS PHE LEU PHE LEU LYS ASP PHE PRO LYS ALA
SEQRES 32 t 854 GLN GLU TYR ILE ASP ALA ALA LEU ASP HIS THR PRO THR
SEQRES 33 t 854 LEU VAL GLU PHE TYR ILE LEU LYS ALA ARG ILE LEU LYS
SEQRES 34 t 854 HIS LEU GLY LEU MET ASP THR ALA ALA GLY ILE LEU GLU
SEQRES 35 t 854 GLU GLY ARG GLN LEU ASP LEU GLN ASP ARG PHE ILE ASN
SEQRES 36 t 854 CYS LYS THR VAL LYS TYR PHE LEU ARG ALA ASN ASN ILE
SEQRES 37 t 854 ASP LYS ALA VAL GLU VAL ALA SER LEU PHE THR LYS ASN
SEQRES 38 t 854 ASP ASP SER VAL ASN GLY ILE LYS ASP LEU HIS LEU VAL
SEQRES 39 t 854 GLU ALA SER TRP PHE ILE VAL GLU GLN ALA GLU ALA TYR
SEQRES 40 t 854 TYR ARG LEU TYR LEU ASP ARG LYS LYS LYS LEU ASP ASP
SEQRES 41 t 854 LEU ALA SER LEU LYS LYS GLU VAL GLU SER ASP LYS SER
SEQRES 42 t 854 GLU GLN ILE ALA ASN ASP ILE LYS GLU ASN GLN TRP LEU
SEQRES 43 t 854 VAL ARG LYS TYR LYS GLY LEU ALA LEU LYS ARG PHE ASN
SEQRES 44 t 854 ALA ILE PRO LYS PHE TYR LYS GLN PHE GLU ASP ASP GLN
SEQRES 45 t 854 LEU ASP PHE HIS SER TYR CYS MET ARG LYS GLY THR PRO
SEQRES 46 t 854 ARG ALA TYR LEU GLU MET LEU GLU TRP GLY LYS ALA LEU
SEQRES 47 t 854 TYR THR LYS PRO MET TYR VAL ARG ALA MET LYS GLU ALA
SEQRES 48 t 854 SER LYS LEU TYR PHE GLN MET HIS ASP ASP ARG LEU LYS
SEQRES 49 t 854 ARG LYS SER ASP SER LEU ASP GLU ASN SER ASP GLU ILE
SEQRES 50 t 854 GLN ASN ASN GLY GLN ASN SER SER SER GLN LYS LYS LYS
SEQRES 51 t 854 ALA LYS LYS GLU ALA ALA ALA MET ASN LYS ARG LYS GLU
SEQRES 52 t 854 THR GLU ALA LYS SER VAL ALA ALA TYR PRO SER ASP GLN
SEQRES 53 t 854 ASP ASN ASP VAL PHE GLY GLU LYS LEU ILE GLU THR SER
SEQRES 54 t 854 THR PRO MET GLU ASP PHE ALA THR GLU PHE TYR ASN ASN
SEQRES 55 t 854 TYR SER MET GLN VAL ARG GLU ASP GLU ARG ASP TYR ILE
SEQRES 56 t 854 LEU ASP PHE GLU PHE ASN TYR ARG ILE GLY LYS LEU ALA
SEQRES 57 t 854 LEU CYS PHE ALA SER LEU ASN LYS PHE ALA LYS ARG PHE
SEQRES 58 t 854 GLY THR THR SER GLY LEU PHE GLY SER MET ALA ILE VAL
SEQRES 59 t 854 LEU LEU HIS ALA THR ARG ASN ASP THR PRO PHE ASP PRO
SEQRES 60 t 854 ILE LEU LYS LYS VAL VAL THR LYS SER LEU GLU LYS GLU
SEQRES 61 t 854 TYR SER GLU ASN PHE PRO LEU ASN GLU ILE SER ASN ASN
SEQRES 62 t 854 SER PHE ASP TRP LEU ASN PHE TYR GLN GLU LYS PHE GLY
SEQRES 63 t 854 LYS ASN ASP ILE ASN GLY LEU LEU PHE LEU TYR ARG TYR
SEQRES 64 t 854 ARG ASP ASP VAL PRO ILE GLY SER SER ASN LEU LYS GLU
SEQRES 65 t 854 MET ILE ILE SER SER LEU SER PRO LEU GLU PRO HIS SER
SEQRES 66 t 854 GLN ASN GLU ILE LEU GLN TYR TYR LEU
SEQRES 1 u 238 MET PRO ILE ASN ILE ARG ARG ALA THR ILE ASN ASP ILE
SEQRES 2 u 238 ILE CYS MET GLN ASN ALA ASN LEU HIS ASN LEU PRO GLU
SEQRES 3 u 238 ASN TYR MET MET LYS TYR TYR MET TYR HIS ILE LEU SER
SEQRES 4 u 238 TRP PRO GLU ALA SER PHE VAL ALA THR THR THR THR LEU
SEQRES 5 u 238 ASP CYS GLU ASP SER ASP GLU GLN ASP GLU ASN ASP LYS
SEQRES 6 u 238 LEU GLU LEU THR LEU ASP GLY THR ASN ASP GLY ARG THR
SEQRES 7 u 238 ILE LYS LEU ASP PRO THR TYR LEU ALA PRO GLY GLU LYS
SEQRES 8 u 238 LEU VAL GLY TYR VAL LEU VAL LYS MET ASN ASP ASP PRO
SEQRES 9 u 238 ASP GLN GLN ASN GLU PRO PRO ASN GLY HIS ILE THR SER
SEQRES 10 u 238 LEU SER VAL MET ARG THR TYR ARG ARG MET GLY ILE ALA
SEQRES 11 u 238 GLU ASN LEU MET ARG GLN ALA LEU PHE ALA LEU ARG GLU
SEQRES 12 u 238 VAL HIS GLN ALA GLU TYR VAL SER LEU HIS VAL ARG GLN
SEQRES 13 u 238 SER ASN ARG ALA ALA LEU HIS LEU TYR ARG ASP THR LEU
SEQRES 14 u 238 ALA PHE GLU VAL LEU SER ILE GLU LYS SER TYR TYR GLN
SEQRES 15 u 238 ASP GLY GLU ASP ALA TYR ALA MET LYS LYS VAL LEU LYS
SEQRES 16 u 238 LEU GLU GLU LEU GLN ILE SER ASN PHE THR HIS ARG ARG
SEQRES 17 u 238 LEU LYS GLU ASN GLU GLU LYS LEU GLU ASP ASP LEU GLU
SEQRES 18 u 238 SER ASP LEU LEU GLU ASP ILE ILE LYS GLN GLY VAL ASN
SEQRES 19 u 238 ASP ILE ILE VAL
SEQRES 1 v 176 MET GLY ARG ASP ILE CYS THR LEU ASP ASN VAL TYR ALA
SEQRES 2 v 176 ASN ASN LEU GLY MET LEU THR LYS LEU ALA HIS VAL THR
SEQRES 3 v 176 VAL PRO ASN LEU TYR GLN ASP ALA PHE PHE SER ALA LEU
SEQRES 4 v 176 PHE ALA GLU ASP SER LEU VAL ALA LYS ASN LYS LYS PRO
SEQRES 5 v 176 SER SER LYS LYS ASP VAL HIS PHE THR GLN MET ALA TYR
SEQRES 6 v 176 TYR SER GLU ILE PRO VAL GLY GLY LEU VAL ALA LYS LEU
SEQRES 7 v 176 VAL PRO LYS LYS GLN ASN GLU LEU SER LEU LYS GLY ILE
SEQRES 8 v 176 GLN ILE GLU PHE LEU GLY VAL LEU PRO ASN TYR ARG HIS
SEQRES 9 v 176 LYS SER ILE GLY SER LYS LEU LEU LYS PHE ALA GLU ASP
SEQRES 10 v 176 LYS CYS SER GLU CYS HIS GLN HIS ASN VAL PHE VAL TYR
SEQRES 11 v 176 LEU PRO ALA VAL ASP ASP LEU THR LYS GLN TRP PHE ILE
SEQRES 12 v 176 ALA HIS GLY PHE GLU GLN VAL GLY GLU THR VAL ASN ASN
SEQRES 13 v 176 PHE ILE LYS GLY VAL ASN GLY ASP GLU GLN ASP ALA ILE
SEQRES 14 v 176 LEU LEU LYS LYS HIS ILE SER
HELIX 1 AA1 LYS t 18 GLY t 33 1 16
HELIX 2 AA2 TYR t 36 ASP t 50 1 15
HELIX 3 AA3 HIS t 53 GLY t 68 1 16
HELIX 4 AA4 LYS t 70 LYS t 83 1 14
HELIX 5 AA5 SER t 90 THR t 104 1 15
HELIX 6 AA6 TYR t 107 SER t 122 1 16
HELIX 7 AA7 LYS t 125 GLY t 139 1 15
HELIX 8 AA8 PHE t 141 PHE t 155 1 15
HELIX 9 AA9 TYR t 158 GLY t 173 1 16
HELIX 10 AB1 GLU t 174 ALA t 189 1 16
HELIX 11 AB2 ASP t 195 ALA t 215 1 21
HELIX 12 AB3 ASN t 219 GLU t 234 1 16
HELIX 13 AB4 LYS t 240 GLY t 255 1 16
HELIX 14 AB5 GLN t 256 ASN t 271 1 16
HELIX 15 AB6 ASN t 274 GLY t 286 1 13
HELIX 16 AB7 ASP t 290 GLN t 303 1 14
HELIX 17 AB8 GLU t 309 ILE t 314 1 6
HELIX 18 AB9 PRO t 315 PHE t 318 5 4
HELIX 19 AC1 ASP t 321 GLY t 340 1 20
HELIX 20 AC2 ALA t 343 VAL t 348 1 6
HELIX 21 AC3 VAL t 348 ARG t 355 1 8
HELIX 22 AC4 VAL t 359 SER t 372 1 14
HELIX 23 AC5 ASP t 379 LEU t 397 1 19
HELIX 24 AC6 PHE t 400 THR t 414 1 15
HELIX 25 AC7 LEU t 417 LEU t 431 1 15
HELIX 26 AC8 LEU t 433 GLN t 446 1 14
HELIX 27 AC9 ARG t 452 ARG t 464 1 13
HELIX 28 AD1 ILE t 468 SER t 476 1 9
HELIX 29 AD2 GLY t 487 VAL t 494 1 8
HELIX 30 AD3 SER t 497 LYS t 525 1 29
HELIX 31 AD4 ASP t 531 ILE t 536 1 6
HELIX 32 AD5 ALA t 537 ASN t 559 1 23
HELIX 33 AD6 ALA t 560 ASP t 571 1 12
HELIX 34 AD7 ASP t 574 LYS t 582 1 9
HELIX 35 AD8 THR t 584 LEU t 598 1 15
HELIX 36 AD9 LYS t 601 SER t 627 1 27
HELIX 37 AE1 SER t 646 VAL t 669 1 24
HELIX 38 AE2 THR t 690 PHE t 699 1 10
HELIX 39 AE3 TYR t 700 GLN t 706 1 7
HELIX 40 AE4 ASP t 713 ARG t 723 1 11
HELIX 41 AE5 LEU t 727 PHE t 741 1 15
HELIX 42 AE6 SER t 745 THR t 759 1 15
HELIX 43 AE7 ASP t 766 TYR t 781 1 16
HELIX 44 AE8 ASP t 796 PHE t 805 1 10
HELIX 45 AE9 ILE t 810 TYR t 819 1 10
HELIX 46 AF1 SER t 827 LEU t 838 1 12
HELIX 47 AF2 GLU t 842 TYR t 852 1 11
HELIX 48 AF3 THR u 9 ASN u 11 5 3
HELIX 49 AF4 ASP u 12 HIS u 22 1 11
HELIX 50 AF5 MET u 29 SER u 39 1 11
HELIX 51 AF6 ILE u 129 HIS u 145 1 17
HELIX 52 AF7 ASN u 158 ARG u 166 1 9
HELIX 53 AF8 ILE u 201 THR u 205 5 5
HELIX 54 AF9 ASN v 15 ALA v 23 1 9
HELIX 55 AG1 ASP v 33 ALA v 38 1 6
HELIX 56 AG2 SER v 106 CYS v 122 1 17
HELIX 57 AG3 ASP v 136 PHE v 147 1 12
SHEET 1 AA1 4 ASN u 4 ARG u 7 0
SHEET 2 AA1 4 PHE u 45 THR u 48 -1 O VAL u 46 N ARG u 6
SHEET 3 AA1 4 GLU u 90 MET u 100 -1 O GLY u 94 N ALA u 47
SHEET 4 AA1 4 TYR u 85 ALA u 87 -1 N LEU u 86 O GLU u 90
SHEET 1 AA2 7 ASN u 4 ARG u 7 0
SHEET 2 AA2 7 PHE u 45 THR u 48 -1 O VAL u 46 N ARG u 6
SHEET 3 AA2 7 GLU u 90 MET u 100 -1 O GLY u 94 N ALA u 47
SHEET 4 AA2 7 GLY u 113 VAL u 120 -1 O SER u 117 N LEU u 97
SHEET 5 AA2 7 TYR u 149 VAL u 154 1 O TYR u 149 N GLY u 113
SHEET 6 AA2 7 ALA u 187 VAL u 193 -1 O TYR u 188 N VAL u 154
SHEET 7 AA2 7 VAL u 173 GLU u 177 -1 N GLU u 177 O ALA u 187
SHEET 1 AA3 7 CYS v 6 ASP v 9 0
SHEET 2 AA3 7 VAL v 58 TYR v 66 -1 O MET v 63 N ASP v 9
SHEET 3 AA3 7 PRO v 70 LEU v 78 -1 O LEU v 78 N VAL v 58
SHEET 4 AA3 7 ILE v 91 VAL v 98 -1 O GLN v 92 N LYS v 77
SHEET 5 AA3 7 VAL v 127 PRO v 132 1 O PHE v 128 N ILE v 93
SHEET 6 AA3 7 GLU v 165 LYS v 173 -1 O ILE v 169 N LEU v 131
SHEET 7 AA3 7 GLU v 148 GLN v 149 -1 N GLU v 148 O LYS v 172
SHEET 1 AA4 7 CYS v 6 ASP v 9 0
SHEET 2 AA4 7 VAL v 58 TYR v 66 -1 O MET v 63 N ASP v 9
SHEET 3 AA4 7 PRO v 70 LEU v 78 -1 O LEU v 78 N VAL v 58
SHEET 4 AA4 7 ILE v 91 VAL v 98 -1 O GLN v 92 N LYS v 77
SHEET 5 AA4 7 VAL v 127 PRO v 132 1 O PHE v 128 N ILE v 93
SHEET 6 AA4 7 GLU v 165 LYS v 173 -1 O ILE v 169 N LEU v 131
SHEET 7 AA4 7 VAL v 154 LYS v 159 -1 N PHE v 157 O GLN v 166
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
