HEADER PROTEIN TRANSPORT 21-NOV-13 4CG7
TITLE CRYO-EM OF THE SEC61-COMPLEX BOUND TO THE IDLE 80S RIBOSOME
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN TRANSPORT PROTEIN SEC61 SUBUNIT ALPHA ISOFORM 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SEC61 ALPHA-1;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: PROTEIN TRANSPORT PROTEIN SEC61 SUBUNIT GAMMA;
COMPND 7 CHAIN: B;
COMPND 8 MOL_ID: 3;
COMPND 9 MOLECULE: TRANSPORT PROTEIN SEC61 SUBUNIT BETA;
COMPND 10 CHAIN: C
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CANIS LUPUS FAMILIARIS;
SOURCE 3 ORGANISM_COMMON: DOG;
SOURCE 4 ORGANISM_TAXID: 9615;
SOURCE 5 ORGAN: PANCREAS;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: CANIS LUPUS FAMILIARIS;
SOURCE 8 ORGANISM_COMMON: DOG;
SOURCE 9 ORGANISM_TAXID: 9615;
SOURCE 10 ORGAN: PANCREAS;
SOURCE 11 MOL_ID: 3;
SOURCE 12 ORGANISM_SCIENTIFIC: CANIS LUPUS FAMILIARIS;
SOURCE 13 ORGANISM_COMMON: DOG;
SOURCE 14 ORGANISM_TAXID: 9615;
SOURCE 15 ORGAN: PANCREAS
KEYWDS PROTEIN TRANSPORT, CO-TRANSLATIONAL PROTEIN TRANSLOCATION
EXPDTA ELECTRON MICROSCOPY
AUTHOR M.GOGALA,T.BECKER,B.BEATRIX,C.BARRIO-GARCIA,O.BERNINGHAUSEN,
AUTHOR 2 R.BECKMANN
REVDAT 4 30-AUG-17 4CG7 1 REMARK
REVDAT 3 19-FEB-14 4CG7 1 JRNL
REVDAT 2 12-FEB-14 4CG7 1 JRNL
REVDAT 1 05-FEB-14 4CG7 0
JRNL AUTH M.GOGALA,T.BECKER,B.BEATRIX,J.ARMACHE,C.BARRIO-GARCIA,
JRNL AUTH 2 O.BERNINGHAUSEN,R.BECKMANN
JRNL TITL STRUCTURES OF THE SEC61 COMPLEX ENGAGED IN NASCENT PEPTIDE
JRNL TITL 2 TRANSLOCATION OR MEMBRANE INSERTION.
JRNL REF NATURE V. 506 107 2014
JRNL REFN ISSN 0028-0836
JRNL PMID 24499919
JRNL DOI 10.1038/NATURE12950
REMARK 2
REMARK 2 RESOLUTION. 6.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : MAPPOS, COOT, MDFF, UCSF CHIMERA,
REMARK 3 SIGNATURE, 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 : NULL
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) : 1.238
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 6.900
REMARK 3 NUMBER OF PARTICLES : 162655
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 -2510. (DEPOSITION ID: 12120).
REMARK 4
REMARK 4 4CG7 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_1290059036.
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 : IDLE SEC61 BOUND TO AN EMPTY
REMARK 245 WHEAT GERM 80S-RIBOSOME
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, HUMIDITY- 95,
REMARK 245 INSTRUMENT- FEI VITROBOT MARK
REMARK 245 IV, METHOD- BLOT FOR 3 SECONDS
REMARK 245 BEFORE PLUNGING,
REMARK 245 SAMPLE BUFFER : 30 MM HEPES/KOH 7.6, 10 MM
REMARK 245 MG(OAC)2, 180 MM KOAC/HAC PH
REMARK 245 7.6, 0.3 % DIGITONIN, 1 MM DTT
REMARK 245 PH : 7.60
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : 17-JUL-11
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-F416 (4K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : 1300.00
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) : 25.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : NULL
REMARK 245 CALIBRATED MAGNIFICATION : 148721
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 200
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 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 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 ALA A 2
REMARK 465 ILE A 3
REMARK 465 LYS A 4
REMARK 465 PHE A 5
REMARK 465 LEU A 6
REMARK 465 GLU A 7
REMARK 465 VAL A 8
REMARK 465 ILE A 9
REMARK 465 LYS A 10
REMARK 465 PRO A 11
REMARK 465 PHE A 12
REMARK 465 CYS A 13
REMARK 465 VAL A 14
REMARK 465 ILE A 15
REMARK 465 LEU A 16
REMARK 465 PRO A 17
REMARK 465 GLU A 18
REMARK 465 ILE A 19
REMARK 465 GLN A 20
REMARK 465 LYS A 21
REMARK 465 PRO A 22
REMARK 465 GLU A 23
REMARK 465 ARG A 24
REMARK 465 MET B 1
REMARK 465 ASP B 2
REMARK 465 GLN B 3
REMARK 465 VAL B 4
REMARK 465 MET B 5
REMARK 465 GLN B 6
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 NE ARG A 402 O MET A 409 1.88
REMARK 500 NH2 ARG A 402 O MET A 409 1.93
REMARK 500 CZ ARG A 402 O MET A 409 2.05
REMARK 500 CB ARG A 405 OG SER A 408 2.08
REMARK 500 O VAL A 410 OD1 ASN A 414 2.16
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 PHE A 476 C PHE A 476 O -0.230
REMARK 500 GLY B 68 C GLY B 68 O -0.232
REMARK 500 SER C 96 C SER C 96 O -0.229
REMARK 500 SER C 96 C SER C 96 OXT -0.229
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 GLN A 27 N - CA - CB ANGL. DEV. = 11.1 DEGREES
REMARK 500 PRO A 49 C - N - CA ANGL. DEV. = 9.9 DEGREES
REMARK 500 PRO A 49 C - N - CD ANGL. DEV. = -27.1 DEGREES
REMARK 500 PRO A 49 CA - N - CD ANGL. DEV. = -17.6 DEGREES
REMARK 500 SER A 55 N - CA - CB ANGL. DEV. = 9.4 DEGREES
REMARK 500 SER A 56 N - CA - CB ANGL. DEV. = 9.9 DEGREES
REMARK 500 SER A 71 N - CA - CB ANGL. DEV. = 10.0 DEGREES
REMARK 500 SER A 128 N - CA - CB ANGL. DEV. = 10.0 DEGREES
REMARK 500 TYR A 173 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 TYR A 173 CB - CG - CD1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 TYR A 257 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 TYR A 257 CB - CG - CD1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 TYR A 272 N - CA - CB ANGL. DEV. = 10.8 DEGREES
REMARK 500 TYR A 276 CB - CG - CD2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 TYR A 276 CB - CG - CD1 ANGL. DEV. = 5.3 DEGREES
REMARK 500 TYR A 336 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 TYR A 364 CB - CG - CD2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 TYR A 364 CB - CG - CD1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 PHE A 375 CB - CG - CD1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ASN A 414 N - CA - CB ANGL. DEV. = 10.8 DEGREES
REMARK 500 GLY B 68 CA - C - O ANGL. DEV. = -11.6 DEGREES
REMARK 500 PHE C 80 CB - CG - CD1 ANGL. DEV. = 4.4 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 GLN A 27 124.90 148.00
REMARK 500 PRO A 49 -19.64 100.47
REMARK 500 PHE A 51 -24.11 94.25
REMARK 500 MET A 54 -50.82 156.17
REMARK 500 SER A 55 161.38 143.15
REMARK 500 SER A 56 -147.44 115.78
REMARK 500 ASP A 57 -6.74 -143.81
REMARK 500 ALA A 59 169.05 155.48
REMARK 500 PHE A 62 -158.75 13.92
REMARK 500 ALA A 70 99.00 90.30
REMARK 500 SER A 71 -144.64 115.74
REMARK 500 ARG A 73 -19.41 -148.15
REMARK 500 THR A 75 -124.16 58.06
REMARK 500 ILE A 81 20.37 -57.92
REMARK 500 VAL A 102 9.02 84.69
REMARK 500 GLN A 127 -36.14 -137.06
REMARK 500 GLU A 142 9.31 88.19
REMARK 500 ALA A 145 153.24 94.77
REMARK 500 ILE A 147 -66.15 7.08
REMARK 500 LEU A 149 -59.79 14.64
REMARK 500 LYS A 171 26.04 -155.73
REMARK 500 TYR A 173 129.38 156.41
REMARK 500 LEU A 175 -135.41 148.99
REMARK 500 THR A 199 -144.58 166.03
REMARK 500 VAL A 201 141.54 -172.84
REMARK 500 PHE A 209 -136.10 53.64
REMARK 500 ALA A 212 -96.94 -107.82
REMARK 500 ILE A 213 52.29 -142.79
REMARK 500 ILE A 214 -136.26 -14.80
REMARK 500 THR A 222 -93.53 -21.00
REMARK 500 THR A 224 -131.27 55.45
REMARK 500 LYS A 226 -160.90 77.11
REMARK 500 VAL A 227 3.04 86.86
REMARK 500 ARG A 231 -170.24 168.23
REMARK 500 TYR A 235 -45.35 -156.82
REMARK 500 ARG A 236 -74.17 -52.31
REMARK 500 GLN A 237 -67.80 -11.37
REMARK 500 ASP A 264 -113.06 -97.51
REMARK 500 LYS A 268 9.53 88.44
REMARK 500 ALA A 270 15.65 94.26
REMARK 500 ARG A 271 -35.96 87.35
REMARK 500 TYR A 272 -83.42 151.95
REMARK 500 ARG A 273 131.51 -20.82
REMARK 500 LEU A 283 -122.42 48.97
REMARK 500 ASN A 315 93.40 -177.58
REMARK 500 LEU A 316 -137.72 -52.07
REMARK 500 LEU A 317 139.92 -29.42
REMARK 500 TRP A 324 -12.93 92.41
REMARK 500 ALA A 335 62.75 -35.25
REMARK 500 VAL A 338 72.44 -109.63
REMARK 500
REMARK 500 THIS ENTRY HAS 81 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 GLN A 47 ILE A 48 -146.25
REMARK 500 ILE A 48 PRO A 49 -134.08
REMARK 500 ALA A 59 ASP A 60 -147.87
REMARK 500 TRP A 64 MET A 65 -149.34
REMARK 500 ALA A 70 SER A 71 146.24
REMARK 500 MET A 133 THR A 134 -145.71
REMARK 500 GLY A 176 SER A 177 -144.92
REMARK 500 PRO A 266 ILE A 267 -134.62
REMARK 500 ARG A 273 GLY A 274 -123.93
REMARK 500 ASP A 357 PRO A 358 -105.12
REMARK 500 PRO A 358 VAL A 359 142.76
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 ARG A 73 0.15 SIDE CHAIN
REMARK 500 TYR A 285 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-2510 RELATED DB: EMDB
REMARK 900 CRYO-EM OF THE SEC61-COMPLEX BOUND TO THE IDLE 80S RIBOSOME
REMARK 900 RELATED ID: 4CG5 RELATED DB: PDB
REMARK 900 CRYO-EM OF THE SEC61-COMPLEX BOUND TO THE 80S RIBOSOME TRANSLATING
REMARK 900 A SECRETORY SUBSTRATE
REMARK 900 RELATED ID: 4CG6 RELATED DB: PDB
REMARK 900 CRYO-EM OF THE SEC61-COMPLEX BOUND TO THE IDLE 80S RIBOSOME
DBREF 4CG7 A 1 476 UNP P38377 S61A1_CANFA 1 476
DBREF 4CG7 B 1 68 UNP P60058 SC61G_CANFA 1 68
DBREF 4CG7 C 61 96 PDB 4CG7 4CG7 61 96
SEQRES 1 A 476 MET ALA ILE LYS PHE LEU GLU VAL ILE LYS PRO PHE CYS
SEQRES 2 A 476 VAL ILE LEU PRO GLU ILE GLN LYS PRO GLU ARG LYS ILE
SEQRES 3 A 476 GLN PHE LYS GLU LYS VAL LEU TRP THR ALA ILE THR LEU
SEQRES 4 A 476 PHE ILE PHE LEU VAL CYS CYS GLN ILE PRO LEU PHE GLY
SEQRES 5 A 476 ILE MET SER SER ASP SER ALA ASP PRO PHE TYR TRP MET
SEQRES 6 A 476 ARG VAL ILE LEU ALA SER ASN ARG GLY THR LEU MET GLU
SEQRES 7 A 476 LEU GLY ILE SER PRO ILE VAL THR SER GLY LEU ILE MET
SEQRES 8 A 476 GLN LEU LEU ALA GLY ALA LYS ILE ILE GLU VAL GLY ASP
SEQRES 9 A 476 THR PRO LYS ASP ARG ALA LEU PHE ASN GLY ALA GLN LYS
SEQRES 10 A 476 LEU PHE GLY MET ILE ILE THR ILE GLY GLN SER ILE VAL
SEQRES 11 A 476 TYR VAL MET THR GLY MET TYR GLY ASP PRO SER GLU MET
SEQRES 12 A 476 GLY ALA GLY ILE CYS LEU LEU ILE THR ILE GLN LEU PHE
SEQRES 13 A 476 VAL ALA GLY LEU ILE VAL LEU LEU LEU ASP GLU LEU LEU
SEQRES 14 A 476 GLN LYS GLY TYR GLY LEU GLY SER GLY ILE SER LEU PHE
SEQRES 15 A 476 ILE ALA THR ASN ILE CYS GLU THR ILE VAL TRP LYS ALA
SEQRES 16 A 476 PHE SER PRO THR THR VAL ASN THR GLY ARG GLY MET GLU
SEQRES 17 A 476 PHE GLU GLY ALA ILE ILE ALA LEU PHE HIS LEU LEU ALA
SEQRES 18 A 476 THR ARG THR ASP LYS VAL ARG ALA LEU ARG GLU ALA PHE
SEQRES 19 A 476 TYR ARG GLN ASN LEU PRO ASN LEU MET ASN LEU ILE ALA
SEQRES 20 A 476 THR ILE PHE VAL PHE ALA VAL VAL ILE TYR PHE GLN GLY
SEQRES 21 A 476 PHE ARG VAL ASP LEU PRO ILE LYS SER ALA ARG TYR ARG
SEQRES 22 A 476 GLY GLN TYR ASN THR TYR PRO ILE LYS LEU PHE TYR THR
SEQRES 23 A 476 SER ASN ILE PRO ILE ILE LEU GLN SER ALA LEU VAL SER
SEQRES 24 A 476 ASN LEU TYR VAL ILE SER GLN MET LEU SER ALA ARG PHE
SEQRES 25 A 476 SER GLY ASN LEU LEU VAL SER LEU LEU GLY THR TRP SER
SEQRES 26 A 476 ASP THR SER SER GLY GLY PRO ALA ARG ALA TYR PRO VAL
SEQRES 27 A 476 GLY GLY LEU CYS HIS TYR LEU SER PRO PRO GLU SER PHE
SEQRES 28 A 476 GLY SER VAL LEU GLU ASP PRO VAL HIS ALA VAL VAL TYR
SEQRES 29 A 476 ILE VAL PHE MET LEU GLY SER CYS ALA PHE PHE SER LYS
SEQRES 30 A 476 THR TRP ILE GLU VAL SER GLY SER SER ALA LYS ASP VAL
SEQRES 31 A 476 ALA LYS GLN LEU LYS GLU GLN GLN MET VAL MET ARG GLY
SEQRES 32 A 476 HIS ARG GLU THR SER MET VAL HIS GLU LEU ASN ARG TYR
SEQRES 33 A 476 ILE PRO THR ALA ALA ALA PHE GLY GLY LEU CYS ILE GLY
SEQRES 34 A 476 ALA LEU SER VAL LEU ALA ASP PHE LEU GLY ALA ILE GLY
SEQRES 35 A 476 SER GLY THR GLY ILE LEU LEU ALA VAL THR ILE ILE TYR
SEQRES 36 A 476 GLN TYR PHE GLU ILE PHE VAL LYS GLU GLN SER GLU VAL
SEQRES 37 A 476 GLY SER MET GLY ALA LEU LEU PHE
SEQRES 1 B 68 MET ASP GLN VAL MET GLN PHE VAL GLU PRO SER ARG GLN
SEQRES 2 B 68 PHE VAL LYS ASP SER ILE ARG LEU VAL LYS ARG CYS THR
SEQRES 3 B 68 LYS PRO ASP ARG LYS GLU PHE GLN LYS ILE ALA MET ALA
SEQRES 4 B 68 THR ALA ILE GLY PHE ALA ILE MET GLY PHE ILE GLY PHE
SEQRES 5 B 68 PHE VAL LYS LEU ILE HIS ILE PRO ILE ASN ASN ILE ILE
SEQRES 6 B 68 VAL GLY GLY
SEQRES 1 C 36 GLU ASP SER PRO GLY LEU LYS VAL GLY PRO VAL PRO VAL
SEQRES 2 C 36 LEU VAL MET SER LEU LEU PHE ILE ALA SER VAL PHE MET
SEQRES 3 C 36 LEU HIS ILE TRP GLY LYS TYR THR ARG SER
HELIX 1 1 GLN A 27 CYS A 46 1 20
HELIX 2 2 TRP A 64 ALA A 70 1 7
HELIX 3 3 SER A 82 LYS A 98 1 17
HELIX 4 4 GLY A 103 GLN A 127 1 25
HELIX 5 5 GLN A 127 GLY A 135 1 9
HELIX 6 6 ALA A 145 CYS A 148 5 4
HELIX 7 7 LEU A 149 GLN A 170 1 22
HELIX 8 8 GLY A 178 PHE A 196 1 19
HELIX 9 9 ALA A 215 ALA A 221 1 7
HELIX 10 10 TYR A 235 GLN A 237 5 3
HELIX 11 11 ASN A 238 PHE A 261 1 24
HELIX 12 12 LYS A 282 SER A 313 1 32
HELIX 13 13 LEU A 317 GLY A 322 1 6
HELIX 14 14 GLY A 340 LEU A 345 1 6
HELIX 15 15 VAL A 359 TRP A 379 1 21
HELIX 16 16 SER A 386 GLN A 398 1 13
HELIX 17 17 HIS A 411 ALA A 440 1 30
HELIX 18 18 THR A 445 GLU A 464 1 20
HELIX 19 19 PHE B 7 CYS B 25 1 19
HELIX 20 20 ARG B 30 ILE B 59 1 30
HELIX 21 21 PRO B 60 ASN B 62 5 3
HELIX 22 22 VAL C 71 HIS C 88 1 18
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
