Header list of 1c17.pdb file
Complete list - b 16 2 Bytes
HEADER MEMBRANE PROTEIN 20-JUL-99 1C17
TITLE A1C12 SUBCOMPLEX OF F1FO ATP SYNTHASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ATP SYNTHASE SUBUNIT C;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: ATP SYNTHASE SUBUNIT A;
COMPND 7 CHAIN: M;
COMPND 8 FRAGMENT: CONSENSUS HELICES OF SUBUNIT A;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 8 ORGANISM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS MEMBRANE PROTEIN, HELIX, COMPLEX
EXPDTA SOLUTION NMR
AUTHOR V.K.RASTOGI,M.E.GIRVIN
REVDAT 3 16-FEB-22 1C17 1 REMARK
REVDAT 2 24-FEB-09 1C17 1 VERSN
REVDAT 1 24-NOV-99 1C17 0
JRNL AUTH V.K.RASTOGI,M.E.GIRVIN
JRNL TITL STRUCTURAL CHANGES LINKED TO PROTON TRANSLOCATION BY SUBUNIT
JRNL TITL 2 C OF THE ATP SYNTHASE.
JRNL REF NATURE V. 402 263 1999
JRNL REFN ISSN 0028-0836
JRNL PMID 10580496
JRNL DOI 10.1038/46224
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.5, CNS 0.5
REMARK 3 AUTHORS : BRUNGER (CNS), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1C17 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUL-99.
REMARK 100 THE DEPOSITION ID IS D_1000009366.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300; 300
REMARK 210 PH : 5.0; 8.0
REMARK 210 IONIC STRENGTH : 50 MM; 50 MM
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM SUBUNIT C
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK:
REMARK 210 THE STRUCTURES OF SUBUNIT C MONOMERS WERE DETERMINED BY TRIPLE
REMARK 210 RESONANCE
REMARK 210 TECHNIQUES THE MODELS OF SUBUNIT A, THE C12 SUBCOMPLEX, AND THE
REMARK 210 AC12
REMARK 210 SUBCOMPLEX USED DISLUFIDE CROSS-LINKS AS CONSTRAINTS IN
REMARK 210 CONJUCNTION WITH THE
REMARK 210 NMR SOLUTION STRUCTURES OF SUBUNIT C
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: TRIDECAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: K, L, M
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 RES C SSSEQI
REMARK 465 GLY M 170
REMARK 465 ILE M 171
REMARK 465 GLY M 172
REMARK 465 GLY M 173
REMARK 465 PHE M 174
REMARK 465 THR M 175
REMARK 465 LYS M 176
REMARK 465 GLU M 177
REMARK 465 LEU M 178
REMARK 465 THR M 179
REMARK 465 LEU M 180
REMARK 465 GLN M 181
REMARK 465 PRO M 182
REMARK 465 PHE M 183
REMARK 465 ASN M 184
REMARK 465 HIS M 185
REMARK 465 TRP M 186
REMARK 465 ALA M 187
REMARK 465 PHE M 188
REMARK 465 ILE M 189
REMARK 465 PRO M 190
REMARK 465 VAL M 191
REMARK 465 ASN M 192
REMARK 465 LEU M 193
REMARK 465 ILE M 194
REMARK 465 LEU M 195
REMARK 465 GLU M 196
REMARK 465 GLY M 197
REMARK 465 VAL M 198
REMARK 465 MET M 266
REMARK 465 ALA M 267
REMARK 465 SER M 268
REMARK 465 GLU M 269
REMARK 465 GLU M 270
REMARK 465 HIS M 271
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 ALA C 12 H MET C 16 1.51
REMARK 500 O ALA K 12 H MET K 16 1.51
REMARK 500 O ALA E 12 H MET E 16 1.51
REMARK 500 O ALA D 12 H MET D 16 1.51
REMARK 500 O ALA H 12 H MET H 16 1.51
REMARK 500 O ALA A 12 H MET A 16 1.51
REMARK 500 O ALA B 12 H MET B 16 1.51
REMARK 500 O ALA F 12 H MET F 16 1.51
REMARK 500 O ALA G 12 H MET G 16 1.51
REMARK 500 O ALA I 12 H MET I 16 1.51
REMARK 500 O ALA J 12 H MET J 16 1.51
REMARK 500 O PRO G 47 H THR G 51 1.56
REMARK 500 O PRO D 47 H THR D 51 1.56
REMARK 500 O PRO C 47 H THR C 51 1.56
REMARK 500 O PRO B 47 H THR B 51 1.56
REMARK 500 O PRO E 47 H THR E 51 1.56
REMARK 500 O PRO J 47 H THR J 51 1.56
REMARK 500 O PRO H 47 H THR H 51 1.56
REMARK 500 O PRO I 47 H THR I 51 1.56
REMARK 500 O PRO A 47 H THR A 51 1.56
REMARK 500 O PRO K 47 H THR K 51 1.56
REMARK 500 O PRO F 47 H THR F 51 1.56
REMARK 500 O MET D 17 H ALA D 21 1.58
REMARK 500 O MET K 17 H ALA K 21 1.58
REMARK 500 O MET A 17 H ALA A 21 1.58
REMARK 500 O MET G 17 H ALA G 21 1.58
REMARK 500 O MET J 17 H ALA J 21 1.58
REMARK 500 O MET F 17 H ALA F 21 1.58
REMARK 500 O MET H 17 H ALA H 21 1.58
REMARK 500 O MET E 17 H ALA E 21 1.58
REMARK 500 O MET C 17 H ALA C 21 1.58
REMARK 500 O MET I 17 H ALA I 21 1.58
REMARK 500 O MET B 17 H ALA B 21 1.59
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 ASN A 5 -71.78 -64.61
REMARK 500 ALA A 39 31.39 -179.27
REMARK 500 ASP A 44 30.89 -94.56
REMARK 500 LEU A 45 -60.66 -97.73
REMARK 500 ASN B 5 -71.66 -64.74
REMARK 500 ALA B 39 31.46 -179.25
REMARK 500 ASP B 44 30.90 -94.55
REMARK 500 LEU B 45 -60.57 -97.74
REMARK 500 ASN C 5 -71.79 -64.65
REMARK 500 ALA C 39 31.34 -179.20
REMARK 500 ASP C 44 30.84 -94.51
REMARK 500 LEU C 45 -60.61 -97.71
REMARK 500 ASN D 5 -71.75 -64.68
REMARK 500 ALA D 39 31.44 -179.23
REMARK 500 ASP D 44 30.91 -94.60
REMARK 500 LEU D 45 -60.67 -97.70
REMARK 500 ASN E 5 -71.75 -64.66
REMARK 500 ALA E 39 31.47 -179.28
REMARK 500 ASP E 44 30.87 -94.54
REMARK 500 LEU E 45 -60.63 -97.76
REMARK 500 ASN F 5 -71.71 -64.70
REMARK 500 ALA F 39 31.46 -179.28
REMARK 500 ASP F 44 30.93 -94.63
REMARK 500 LEU F 45 -60.63 -97.71
REMARK 500 ASN G 5 -71.78 -64.62
REMARK 500 ALA G 39 31.40 -179.27
REMARK 500 ASP G 44 30.82 -94.52
REMARK 500 LEU G 45 -60.60 -97.67
REMARK 500 ASN H 5 -71.77 -64.74
REMARK 500 ALA H 39 31.41 -179.24
REMARK 500 ASP H 44 30.84 -94.49
REMARK 500 LEU H 45 -60.62 -97.68
REMARK 500 ASN I 5 -71.67 -64.73
REMARK 500 ALA I 39 31.43 -179.25
REMARK 500 ASP I 44 30.92 -94.55
REMARK 500 LEU I 45 -60.65 -97.78
REMARK 500 ASN J 5 -71.71 -64.65
REMARK 500 ALA J 39 31.38 -179.25
REMARK 500 ASP J 44 30.86 -94.59
REMARK 500 LEU J 45 -60.62 -97.70
REMARK 500 ASN K 5 -71.69 -64.72
REMARK 500 ALA K 39 31.43 -179.28
REMARK 500 ASP K 44 30.92 -94.65
REMARK 500 LEU K 45 -60.59 -97.71
REMARK 500 ILE L 30 -70.39 -66.10
REMARK 500 ASP L 44 55.54 -146.74
REMARK 500 ILE L 63 -82.88 -62.14
REMARK 500 MET L 75 -87.09 -84.36
REMARK 500 ALA L 77 -80.65 -77.15
REMARK 500 LYS M 97 -79.67 -67.82
REMARK 500
REMARK 500 THIS ENTRY HAS 55 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1C99 RELATED DB: PDB
REMARK 900 1C99 CONTAINS THE DEPROTONATED SUBUNIT C MONOMER
REMARK 900 RELATED ID: 1C0V RELATED DB: PDB
REMARK 900 1C0V CONTAINS THE PROTONATED SUBUNIT C MONOMER
DBREF 1C17 A 1 79 UNP P68699 ATPL_ECOLI 1 79
DBREF 1C17 B 1 79 UNP P68699 ATPL_ECOLI 1 79
DBREF 1C17 C 1 79 UNP P68699 ATPL_ECOLI 1 79
DBREF 1C17 D 1 79 UNP P68699 ATPL_ECOLI 1 79
DBREF 1C17 E 1 79 UNP P68699 ATPL_ECOLI 1 79
DBREF 1C17 F 1 79 UNP P68699 ATPL_ECOLI 1 79
DBREF 1C17 G 1 79 UNP P68699 ATPL_ECOLI 1 79
DBREF 1C17 H 1 79 UNP P68699 ATPL_ECOLI 1 79
DBREF 1C17 I 1 79 UNP P68699 ATPL_ECOLI 1 79
DBREF 1C17 J 1 79 UNP P68699 ATPL_ECOLI 1 79
DBREF 1C17 K 1 79 UNP P68699 ATPL_ECOLI 1 79
DBREF 1C17 L 1 79 UNP P68699 ATPL_ECOLI 1 79
DBREF 1C17 M 95 271 UNP P0AB98 ATP6_ECOLI 95 271
SEQRES 1 A 79 MET GLU ASN LEU ASN MET ASP LEU LEU TYR MET ALA ALA
SEQRES 2 A 79 ALA VAL MET MET GLY LEU ALA ALA ILE GLY ALA ALA ILE
SEQRES 3 A 79 GLY ILE GLY ILE LEU GLY GLY LYS PHE LEU GLU GLY ALA
SEQRES 4 A 79 ALA ARG GLN PRO ASP LEU ILE PRO LEU LEU ARG THR GLN
SEQRES 5 A 79 PHE PHE ILE VAL MET GLY LEU VAL ASP ALA ILE PRO MET
SEQRES 6 A 79 ILE ALA VAL GLY LEU GLY LEU TYR VAL MET PHE ALA VAL
SEQRES 7 A 79 ALA
SEQRES 1 B 79 MET GLU ASN LEU ASN MET ASP LEU LEU TYR MET ALA ALA
SEQRES 2 B 79 ALA VAL MET MET GLY LEU ALA ALA ILE GLY ALA ALA ILE
SEQRES 3 B 79 GLY ILE GLY ILE LEU GLY GLY LYS PHE LEU GLU GLY ALA
SEQRES 4 B 79 ALA ARG GLN PRO ASP LEU ILE PRO LEU LEU ARG THR GLN
SEQRES 5 B 79 PHE PHE ILE VAL MET GLY LEU VAL ASP ALA ILE PRO MET
SEQRES 6 B 79 ILE ALA VAL GLY LEU GLY LEU TYR VAL MET PHE ALA VAL
SEQRES 7 B 79 ALA
SEQRES 1 C 79 MET GLU ASN LEU ASN MET ASP LEU LEU TYR MET ALA ALA
SEQRES 2 C 79 ALA VAL MET MET GLY LEU ALA ALA ILE GLY ALA ALA ILE
SEQRES 3 C 79 GLY ILE GLY ILE LEU GLY GLY LYS PHE LEU GLU GLY ALA
SEQRES 4 C 79 ALA ARG GLN PRO ASP LEU ILE PRO LEU LEU ARG THR GLN
SEQRES 5 C 79 PHE PHE ILE VAL MET GLY LEU VAL ASP ALA ILE PRO MET
SEQRES 6 C 79 ILE ALA VAL GLY LEU GLY LEU TYR VAL MET PHE ALA VAL
SEQRES 7 C 79 ALA
SEQRES 1 D 79 MET GLU ASN LEU ASN MET ASP LEU LEU TYR MET ALA ALA
SEQRES 2 D 79 ALA VAL MET MET GLY LEU ALA ALA ILE GLY ALA ALA ILE
SEQRES 3 D 79 GLY ILE GLY ILE LEU GLY GLY LYS PHE LEU GLU GLY ALA
SEQRES 4 D 79 ALA ARG GLN PRO ASP LEU ILE PRO LEU LEU ARG THR GLN
SEQRES 5 D 79 PHE PHE ILE VAL MET GLY LEU VAL ASP ALA ILE PRO MET
SEQRES 6 D 79 ILE ALA VAL GLY LEU GLY LEU TYR VAL MET PHE ALA VAL
SEQRES 7 D 79 ALA
SEQRES 1 E 79 MET GLU ASN LEU ASN MET ASP LEU LEU TYR MET ALA ALA
SEQRES 2 E 79 ALA VAL MET MET GLY LEU ALA ALA ILE GLY ALA ALA ILE
SEQRES 3 E 79 GLY ILE GLY ILE LEU GLY GLY LYS PHE LEU GLU GLY ALA
SEQRES 4 E 79 ALA ARG GLN PRO ASP LEU ILE PRO LEU LEU ARG THR GLN
SEQRES 5 E 79 PHE PHE ILE VAL MET GLY LEU VAL ASP ALA ILE PRO MET
SEQRES 6 E 79 ILE ALA VAL GLY LEU GLY LEU TYR VAL MET PHE ALA VAL
SEQRES 7 E 79 ALA
SEQRES 1 F 79 MET GLU ASN LEU ASN MET ASP LEU LEU TYR MET ALA ALA
SEQRES 2 F 79 ALA VAL MET MET GLY LEU ALA ALA ILE GLY ALA ALA ILE
SEQRES 3 F 79 GLY ILE GLY ILE LEU GLY GLY LYS PHE LEU GLU GLY ALA
SEQRES 4 F 79 ALA ARG GLN PRO ASP LEU ILE PRO LEU LEU ARG THR GLN
SEQRES 5 F 79 PHE PHE ILE VAL MET GLY LEU VAL ASP ALA ILE PRO MET
SEQRES 6 F 79 ILE ALA VAL GLY LEU GLY LEU TYR VAL MET PHE ALA VAL
SEQRES 7 F 79 ALA
SEQRES 1 G 79 MET GLU ASN LEU ASN MET ASP LEU LEU TYR MET ALA ALA
SEQRES 2 G 79 ALA VAL MET MET GLY LEU ALA ALA ILE GLY ALA ALA ILE
SEQRES 3 G 79 GLY ILE GLY ILE LEU GLY GLY LYS PHE LEU GLU GLY ALA
SEQRES 4 G 79 ALA ARG GLN PRO ASP LEU ILE PRO LEU LEU ARG THR GLN
SEQRES 5 G 79 PHE PHE ILE VAL MET GLY LEU VAL ASP ALA ILE PRO MET
SEQRES 6 G 79 ILE ALA VAL GLY LEU GLY LEU TYR VAL MET PHE ALA VAL
SEQRES 7 G 79 ALA
SEQRES 1 H 79 MET GLU ASN LEU ASN MET ASP LEU LEU TYR MET ALA ALA
SEQRES 2 H 79 ALA VAL MET MET GLY LEU ALA ALA ILE GLY ALA ALA ILE
SEQRES 3 H 79 GLY ILE GLY ILE LEU GLY GLY LYS PHE LEU GLU GLY ALA
SEQRES 4 H 79 ALA ARG GLN PRO ASP LEU ILE PRO LEU LEU ARG THR GLN
SEQRES 5 H 79 PHE PHE ILE VAL MET GLY LEU VAL ASP ALA ILE PRO MET
SEQRES 6 H 79 ILE ALA VAL GLY LEU GLY LEU TYR VAL MET PHE ALA VAL
SEQRES 7 H 79 ALA
SEQRES 1 I 79 MET GLU ASN LEU ASN MET ASP LEU LEU TYR MET ALA ALA
SEQRES 2 I 79 ALA VAL MET MET GLY LEU ALA ALA ILE GLY ALA ALA ILE
SEQRES 3 I 79 GLY ILE GLY ILE LEU GLY GLY LYS PHE LEU GLU GLY ALA
SEQRES 4 I 79 ALA ARG GLN PRO ASP LEU ILE PRO LEU LEU ARG THR GLN
SEQRES 5 I 79 PHE PHE ILE VAL MET GLY LEU VAL ASP ALA ILE PRO MET
SEQRES 6 I 79 ILE ALA VAL GLY LEU GLY LEU TYR VAL MET PHE ALA VAL
SEQRES 7 I 79 ALA
SEQRES 1 J 79 MET GLU ASN LEU ASN MET ASP LEU LEU TYR MET ALA ALA
SEQRES 2 J 79 ALA VAL MET MET GLY LEU ALA ALA ILE GLY ALA ALA ILE
SEQRES 3 J 79 GLY ILE GLY ILE LEU GLY GLY LYS PHE LEU GLU GLY ALA
SEQRES 4 J 79 ALA ARG GLN PRO ASP LEU ILE PRO LEU LEU ARG THR GLN
SEQRES 5 J 79 PHE PHE ILE VAL MET GLY LEU VAL ASP ALA ILE PRO MET
SEQRES 6 J 79 ILE ALA VAL GLY LEU GLY LEU TYR VAL MET PHE ALA VAL
SEQRES 7 J 79 ALA
SEQRES 1 K 79 MET GLU ASN LEU ASN MET ASP LEU LEU TYR MET ALA ALA
SEQRES 2 K 79 ALA VAL MET MET GLY LEU ALA ALA ILE GLY ALA ALA ILE
SEQRES 3 K 79 GLY ILE GLY ILE LEU GLY GLY LYS PHE LEU GLU GLY ALA
SEQRES 4 K 79 ALA ARG GLN PRO ASP LEU ILE PRO LEU LEU ARG THR GLN
SEQRES 5 K 79 PHE PHE ILE VAL MET GLY LEU VAL ASP ALA ILE PRO MET
SEQRES 6 K 79 ILE ALA VAL GLY LEU GLY LEU TYR VAL MET PHE ALA VAL
SEQRES 7 K 79 ALA
SEQRES 1 L 79 MET GLU ASN LEU ASN MET ASP LEU LEU TYR MET ALA ALA
SEQRES 2 L 79 ALA VAL MET MET GLY LEU ALA ALA ILE GLY ALA ALA ILE
SEQRES 3 L 79 GLY ILE GLY ILE LEU GLY GLY LYS PHE LEU GLU GLY ALA
SEQRES 4 L 79 ALA ARG GLN PRO ASP LEU ILE PRO LEU LEU ARG THR GLN
SEQRES 5 L 79 PHE PHE ILE VAL MET GLY LEU VAL ASP ALA ILE PRO MET
SEQRES 6 L 79 ILE ALA VAL GLY LEU GLY LEU TYR VAL MET PHE ALA VAL
SEQRES 7 L 79 ALA
SEQRES 1 M 177 HIS GLY LYS SER LYS LEU ILE ALA PRO LEU ALA LEU THR
SEQRES 2 M 177 ILE PHE VAL TRP VAL PHE LEU MET ASN LEU MET ASP LEU
SEQRES 3 M 177 LEU PRO ILE ASP LEU LEU PRO TYR ILE ALA GLU HIS VAL
SEQRES 4 M 177 LEU GLY LEU PRO ALA LEU ARG VAL VAL PRO SER ALA ASP
SEQRES 5 M 177 VAL ASN VAL THR LEU SER MET ALA LEU GLY VAL PHE ILE
SEQRES 6 M 177 LEU ILE LEU PHE TYR SER ILE LYS MET LYS GLY ILE GLY
SEQRES 7 M 177 GLY PHE THR LYS GLU LEU THR LEU GLN PRO PHE ASN HIS
SEQRES 8 M 177 TRP ALA PHE ILE PRO VAL ASN LEU ILE LEU GLU GLY VAL
SEQRES 9 M 177 SER LEU LEU SER LYS PRO VAL SER LEU GLY LEU ARG LEU
SEQRES 10 M 177 PHE GLY ASN MET TYR ALA GLY GLU LEU ILE PHE ILE LEU
SEQRES 11 M 177 ILE ALA GLY LEU LEU PRO TRP TRP SER GLN TRP ILE LEU
SEQRES 12 M 177 ASN VAL PRO TRP ALA ILE PHE HIS ILE LEU ILE ILE THR
SEQRES 13 M 177 LEU GLN ALA PHE ILE PHE MET VAL LEU THR ILE VAL TYR
SEQRES 14 M 177 LEU SER MET ALA SER GLU GLU HIS
HELIX 1 1 MET A 1 GLY A 38 1 38
HELIX 2 2 LEU A 45 VAL A 60 1 16
HELIX 3 3 ASP A 61 ALA A 79 1 19
HELIX 4 4 MET B 1 GLY B 38 1 38
HELIX 5 5 LEU B 45 VAL B 60 1 16
HELIX 6 6 ASP B 61 ALA B 79 1 19
HELIX 7 7 MET C 1 GLY C 38 1 38
HELIX 8 8 LEU C 45 VAL C 60 1 16
HELIX 9 9 ASP C 61 ALA C 79 1 19
HELIX 10 10 MET D 1 GLY D 38 1 38
HELIX 11 11 LEU D 45 VAL D 60 1 16
HELIX 12 12 ASP D 61 ALA D 79 1 19
HELIX 13 13 MET E 1 GLY E 38 1 38
HELIX 14 14 LEU E 45 VAL E 60 1 16
HELIX 15 15 ASP E 61 ALA E 79 1 19
HELIX 16 16 MET F 1 GLY F 38 1 38
HELIX 17 17 LEU F 45 VAL F 60 1 16
HELIX 18 18 ASP F 61 ALA F 79 1 19
HELIX 19 19 MET G 1 GLY G 38 1 38
HELIX 20 20 LEU G 45 VAL G 60 1 16
HELIX 21 21 ASP G 61 ALA G 79 1 19
HELIX 22 22 MET H 1 GLY H 38 1 38
HELIX 23 23 LEU H 45 VAL H 60 1 16
HELIX 24 24 ASP H 61 ALA H 79 1 19
HELIX 25 25 MET I 1 GLY I 38 1 38
HELIX 26 26 LEU I 45 VAL I 60 1 16
HELIX 27 27 ASP I 61 ALA I 79 1 19
HELIX 28 28 MET J 1 GLY J 38 1 38
HELIX 29 29 LEU J 45 VAL J 60 1 16
HELIX 30 30 ASP J 61 ALA J 79 1 19
HELIX 31 31 MET K 1 GLY K 38 1 38
HELIX 32 32 LEU K 45 VAL K 60 1 16
HELIX 33 33 ASP K 61 ALA K 79 1 19
HELIX 34 34 MET L 1 GLN L 42 1 42
HELIX 35 35 LEU L 45 MET L 75 1 31
HELIX 36 36 GLY M 96 LEU M 126 1 31
HELIX 37 37 LEU M 134 LYS M 167 1 34
HELIX 38 38 LEU M 201 LEU M 229 1 29
HELIX 39 39 TRP M 232 LEU M 264 1 33
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
Complete list - b 16 2 Bytes