Header list of 1gwp.pdb file
Complete list - r 14 2 Bytes
HEADER VIRAL PROTEIN 22-MAR-02 1GWP
TITLE STRUCTURE OF THE N-TERMINAL DOMAIN OF THE MATURE HIV-1
TITLE 2 CAPSID PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GAG POLYPROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: AMINO-TERMINAL CORE DOMAIN RESIDUES 132 - 282;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS TYPE 1
SOURCE 3 (NEW YORK-5 ISOLATE);
SOURCE 4 ORGANISM_TAXID: 11698;
SOURCE 5 STRAIN: PNL4-3;
SOURCE 6 CELL_LINE: CLONE 12;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET11A
KEYWDS HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 CAPSID PROTEIN, AMIMO-
KEYWDS 2 TERMINAL CORE DOMAIN, HIV-1 CA-151, VIRUS CAPSID PROTEIN,
KEYWDS 3 VIRUS MATURATION, VIRAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR C.TANG,R.K.GITTI,B.M.LEE,J.WALKER,M.F.SUMMERS,S.YOO,
AUTHOR 2 W.I.SUNDQUIST
REVDAT 5 12-MAR-14 1GWP 1 SOURCE
REVDAT 4 05-FEB-14 1GWP 1 HEADER SOURCE KEYWDS REMARK
REVDAT 4 2 VERSN
REVDAT 3 24-FEB-09 1GWP 1 VERSN
REVDAT 2 26-MAR-04 1GWP 1 SPRSDE
REVDAT 1 21-JUN-02 1GWP 0
SPRSDE 26-MAR-04 1GWP 1GDS 1GDY 1GDZ
JRNL AUTH C.TANG,Y.NDASSA,M.F.SUMMERS
JRNL TITL STRUCTURE OF THE N-TERMINAL 283-RESIDUE FRAGMENT
JRNL TITL 2 OF THE IMMATURE HIV-1 GAG POLYPROTEIN
JRNL REF NAT.STRUCT.BIOL. V. 9 537 2002
JRNL REFN ISSN 1072-8368
JRNL PMID 12032547
JRNL DOI 10.1038/NSB806
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.K.GITTI,B.M.LEE,J.WALKER,M.F.SUMMERS,S.YOO,W.I.SUNDQUIST
REMARK 1 TITL STRUCTURE OF THE AMINO-TERMINAL CORE DOMAIN OF THE HIV-1
REMARK 1 TITL 2 CAPSID PROTEIN.
REMARK 1 REF SCIENCE V. 273 231 1996
REMARK 1 REFN ISSN 0036-8075
REMARK 1 PMID 8662505
REMARK 1 DOI 10.1126/SCIENCE.273.5272.231
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA
REMARK 3 AUTHORS : GUNTERT,WUTHRICH
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: TORSION ANGLE DYNAMICS FOLLOWED BY
REMARK 3 ENERGY MINIMIZATION. GUNTERT, P., MUMENTHALER, C. WUTHRICH, K.
REMARK 3 (1997). TORSION ANGLE DYNAMICS FOR NMR STRUCTURE CALCULATION
REMARK 3 WITH THE NEW PROGRAM DYANA. J. MOL. BIOL. 273, 283-298.
REMARK 4
REMARK 4 1GWP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-MAR-02.
REMARK 100 THE PDBE ID CODE IS EBI-9544.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.5
REMARK 210 IONIC STRENGTH : 10
REMARK 210 PRESSURE : 1ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HMQC-NOESY-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: HSQC HNCA, HN(CO)CA, HNCO, HNHA HMQC-NOESY-HSQC,
REMARK 210 HSQC-NOESY-HSQC, HMQC-NOESY-HMQC
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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: 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 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 ASN A 5 177.08 -49.16
REMARK 500 1 ALA A 14 -174.64 47.10
REMARK 500 1 LYS A 30 -77.21 -119.07
REMARK 500 1 ALA A 31 61.06 84.38
REMARK 500 1 LEU A 83 -79.25 -71.12
REMARK 500 1 VAL A 86 131.23 -176.81
REMARK 500 1 ALA A 92 154.20 -40.20
REMARK 500 1 THR A 110 -146.77 -114.39
REMARK 500 1 PRO A 125 48.80 -75.00
REMARK 500 1 THR A 148 89.62 32.99
REMARK 500 1 SER A 149 77.39 -109.83
REMARK 500 2 ASN A 5 172.92 -49.38
REMARK 500 2 ALA A 14 -173.63 47.34
REMARK 500 2 LYS A 30 -72.79 -91.78
REMARK 500 2 ALA A 31 93.84 85.49
REMARK 500 2 PHE A 32 74.86 48.47
REMARK 500 2 LEU A 83 -87.10 -71.10
REMARK 500 2 PRO A 85 -167.10 -75.02
REMARK 500 2 MET A 96 165.18 -42.28
REMARK 500 2 PRO A 125 48.96 -75.03
REMARK 500 2 SER A 146 66.77 39.21
REMARK 500 2 THR A 148 61.71 -173.38
REMARK 500 3 ASN A 5 169.15 -45.45
REMARK 500 3 ALA A 14 -174.76 47.86
REMARK 500 3 LYS A 30 -79.68 -119.51
REMARK 500 3 ALA A 31 56.87 83.48
REMARK 500 3 SER A 44 -78.76 -77.90
REMARK 500 3 THR A 48 -179.12 -49.72
REMARK 500 3 LEU A 83 -81.29 -79.49
REMARK 500 3 HIS A 87 52.87 -152.43
REMARK 500 3 ARG A 97 -179.83 -66.36
REMARK 500 3 PRO A 99 -167.23 -75.03
REMARK 500 3 PRO A 125 47.50 -75.10
REMARK 500 3 SER A 149 157.92 60.59
REMARK 500 4 ASN A 5 176.17 -48.80
REMARK 500 4 ALA A 14 -173.26 46.54
REMARK 500 4 LYS A 30 -70.29 -91.47
REMARK 500 4 ALA A 31 76.40 89.22
REMARK 500 4 PHE A 32 79.07 58.50
REMARK 500 4 PRO A 85 -164.55 -74.98
REMARK 500 4 VAL A 86 114.92 61.80
REMARK 500 4 ILE A 91 -175.07 47.94
REMARK 500 4 PRO A 125 48.38 -74.95
REMARK 500 4 SER A 146 66.25 39.35
REMARK 500 4 THR A 148 59.05 -150.21
REMARK 500 4 SER A 149 107.17 68.20
REMARK 500 5 LEU A 6 -48.82 83.32
REMARK 500 5 GLN A 9 159.45 161.17
REMARK 500 5 ALA A 14 -173.38 45.80
REMARK 500 5 LYS A 30 -79.85 -120.23
REMARK 500 5 ALA A 31 59.46 85.09
REMARK 500 5 VAL A 86 141.65 -39.81
REMARK 500 5 HIS A 87 58.95 177.84
REMARK 500 5 MET A 96 82.01 36.04
REMARK 500 5 PRO A 125 49.43 -74.97
REMARK 500 5 SER A 146 79.97 42.19
REMARK 500 5 THR A 148 57.94 -118.91
REMARK 500 5 SER A 149 87.07 67.08
REMARK 500 6 ASN A 5 178.04 -49.54
REMARK 500 6 ALA A 14 -174.25 46.71
REMARK 500 6 LYS A 30 -76.15 -106.98
REMARK 500 6 ALA A 31 74.26 88.37
REMARK 500 6 SER A 44 -78.65 -76.93
REMARK 500 6 LEU A 83 -84.25 -75.41
REMARK 500 6 VAL A 86 56.52 -176.60
REMARK 500 6 HIS A 87 57.51 -149.93
REMARK 500 6 SER A 146 68.63 39.14
REMARK 500 6 THR A 148 58.39 -171.89
REMARK 500 7 ASN A 5 178.70 -50.19
REMARK 500 7 ALA A 14 -173.67 47.00
REMARK 500 7 LYS A 30 -85.68 -119.39
REMARK 500 7 ALA A 31 70.09 84.01
REMARK 500 7 PHE A 32 100.10 53.31
REMARK 500 7 SER A 44 -82.19 -84.68
REMARK 500 7 THR A 48 -178.31 -49.78
REMARK 500 7 LEU A 83 -70.47 -69.43
REMARK 500 7 VAL A 86 105.87 -171.11
REMARK 500 7 HIS A 87 50.14 -164.98
REMARK 500 7 ALA A 92 152.34 -43.22
REMARK 500 7 PRO A 125 48.47 -74.96
REMARK 500 7 SER A 146 77.71 41.56
REMARK 500 7 THR A 148 -60.79 -97.81
REMARK 500 7 SER A 149 117.34 -166.72
REMARK 500 7 ILE A 150 105.83 64.44
REMARK 500 8 ASN A 5 174.41 -56.20
REMARK 500 8 ALA A 14 -173.02 46.95
REMARK 500 8 LYS A 30 -76.49 -108.17
REMARK 500 8 ALA A 31 75.35 86.34
REMARK 500 8 SER A 44 -80.41 -79.59
REMARK 500 8 ARG A 97 -177.96 -60.90
REMARK 500 8 SER A 102 -54.87 151.25
REMARK 500 8 PRO A 125 46.77 -74.97
REMARK 500 8 SER A 146 80.94 39.49
REMARK 500 8 THR A 148 55.74 -163.67
REMARK 500 9 ASN A 5 177.37 -49.73
REMARK 500 9 ALA A 14 -174.04 48.31
REMARK 500 9 LYS A 30 -78.31 -118.99
REMARK 500 9 ALA A 31 93.05 87.37
REMARK 500 9 PHE A 32 93.52 49.70
REMARK 500 9 HIS A 87 52.78 -170.33
REMARK 500 9 SER A 102 -38.40 94.97
REMARK 500 9 PRO A 125 47.39 -75.00
REMARK 500 9 SER A 146 79.19 39.10
REMARK 500 9 THR A 148 57.70 -96.95
REMARK 500 10 ALA A 14 -173.25 47.47
REMARK 500 10 LYS A 30 -61.87 -92.83
REMARK 500 10 ALA A 31 77.48 75.44
REMARK 500 10 PHE A 32 73.39 56.40
REMARK 500 10 LEU A 83 -74.95 -68.22
REMARK 500 10 ARG A 97 -178.59 -68.10
REMARK 500 10 SER A 102 -55.17 153.10
REMARK 500 10 PRO A 125 45.75 -74.93
REMARK 500 10 SER A 146 78.70 38.97
REMARK 500 10 THR A 148 -58.50 -152.35
REMARK 500 10 ILE A 150 -52.18 -140.77
REMARK 500 11 ASN A 5 -168.61 -71.60
REMARK 500 11 LEU A 6 -73.50 -32.00
REMARK 500 11 ALA A 14 -173.98 47.06
REMARK 500 11 LYS A 30 -71.22 -95.04
REMARK 500 11 ALA A 31 81.26 85.66
REMARK 500 11 SER A 44 -76.03 -75.33
REMARK 500 11 MET A 96 147.64 66.18
REMARK 500 11 PRO A 125 49.81 -75.07
REMARK 500 11 PRO A 147 -169.92 -75.06
REMARK 500 11 SER A 149 130.68 -39.44
REMARK 500 12 ASN A 5 161.31 -41.48
REMARK 500 12 ALA A 14 165.66 -43.59
REMARK 500 12 ILE A 15 -172.86 -56.67
REMARK 500 12 LYS A 30 -70.49 -103.90
REMARK 500 12 ALA A 31 80.58 85.71
REMARK 500 12 PHE A 32 82.15 55.97
REMARK 500 12 LEU A 83 -71.42 -68.62
REMARK 500 12 VAL A 86 138.99 -176.23
REMARK 500 12 GLU A 98 79.68 -119.00
REMARK 500 12 PRO A 125 48.44 -74.96
REMARK 500 12 THR A 148 -69.02 67.52
REMARK 500 12 SER A 149 134.68 68.96
REMARK 500 13 LEU A 6 -56.07 77.97
REMARK 500 13 ALA A 14 164.85 -43.39
REMARK 500 13 LYS A 30 -76.14 -91.35
REMARK 500 13 ALA A 31 86.71 87.63
REMARK 500 13 SER A 44 -78.55 -75.58
REMARK 500 13 LEU A 83 -81.83 -68.23
REMARK 500 13 HIS A 87 73.29 -105.37
REMARK 500 13 SER A 102 -59.94 156.13
REMARK 500 13 PRO A 125 48.37 -75.03
REMARK 500 13 SER A 146 79.72 39.41
REMARK 500 13 THR A 148 58.97 -172.70
REMARK 500 13 SER A 149 167.33 179.00
REMARK 500 14 ASN A 5 178.60 -49.87
REMARK 500 14 ALA A 14 -174.26 47.57
REMARK 500 14 LYS A 30 -71.29 -92.32
REMARK 500 14 ALA A 31 79.62 86.95
REMARK 500 14 PHE A 32 84.67 58.08
REMARK 500 14 LEU A 83 -86.45 -69.58
REMARK 500 14 PRO A 125 44.89 -74.96
REMARK 500 14 SER A 146 66.85 39.09
REMARK 500 14 THR A 148 57.33 -168.33
REMARK 500 15 ALA A 14 -173.57 46.74
REMARK 500 15 LYS A 30 -77.11 -101.90
REMARK 500 15 ALA A 31 75.49 88.15
REMARK 500 15 LEU A 83 -80.55 -70.50
REMARK 500 15 PRO A 85 -166.34 -75.06
REMARK 500 15 HIS A 87 110.83 -160.42
REMARK 500 15 ALA A 92 153.46 -43.65
REMARK 500 15 SER A 102 -29.26 -39.50
REMARK 500 15 PRO A 125 49.17 -74.93
REMARK 500 15 SER A 146 81.96 40.43
REMARK 500 15 SER A 149 150.87 62.65
REMARK 500 15 ILE A 150 135.93 65.64
REMARK 500 16 ASN A 5 178.55 -49.97
REMARK 500 16 ALA A 14 -173.87 47.42
REMARK 500 16 LYS A 30 -84.03 -122.11
REMARK 500 16 ALA A 31 59.34 88.33
REMARK 500 16 SER A 44 -81.02 -82.48
REMARK 500 16 HIS A 62 79.45 177.42
REMARK 500 16 MET A 96 95.71 -50.19
REMARK 500 16 SER A 102 -57.00 153.94
REMARK 500 16 PRO A 125 49.57 -75.01
REMARK 500 16 THR A 148 140.61 62.54
REMARK 500 16 SER A 149 158.62 68.99
REMARK 500 16 ILE A 150 113.71 64.65
REMARK 500 17 LEU A 6 122.00 73.40
REMARK 500 17 ALA A 14 -173.10 46.69
REMARK 500 17 LYS A 30 -75.12 -92.28
REMARK 500 17 ALA A 31 88.50 86.28
REMARK 500 17 VAL A 86 66.17 -170.47
REMARK 500 17 GLN A 95 -84.05 -71.45
REMARK 500 17 MET A 96 83.91 179.38
REMARK 500 17 THR A 110 -169.74 -106.04
REMARK 500 17 PRO A 125 46.42 -74.97
REMARK 500 17 SER A 146 84.03 39.36
REMARK 500 17 THR A 148 -61.13 -136.72
REMARK 500 17 SER A 149 79.35 -163.01
REMARK 500 18 LEU A 6 -56.16 73.67
REMARK 500 18 ALA A 14 -174.14 47.14
REMARK 500 18 LYS A 30 -67.32 -103.39
REMARK 500 18 ALA A 31 63.68 88.40
REMARK 500 18 PHE A 32 75.58 60.85
REMARK 500 18 SER A 44 -80.96 -83.20
REMARK 500 18 LEU A 83 -80.16 -79.34
REMARK 500 18 PRO A 85 -169.82 -75.01
REMARK 500 18 SER A 102 -55.52 157.82
REMARK 500 18 PRO A 125 43.99 -75.04
REMARK 500 18 SER A 146 69.66 39.38
REMARK 500 19 ASN A 5 176.81 -49.10
REMARK 500 19 ALA A 14 -179.01 50.25
REMARK 500 19 LYS A 30 -83.41 -122.91
REMARK 500 19 ALA A 31 77.65 90.22
REMARK 500 19 PHE A 32 49.41 27.91
REMARK 500 19 SER A 44 -80.93 -84.71
REMARK 500 19 THR A 48 179.91 -48.95
REMARK 500 19 MET A 96 101.77 -53.09
REMARK 500 19 ARG A 97 -178.26 -68.13
REMARK 500 19 SER A 102 -39.94 99.24
REMARK 500 19 PRO A 125 47.22 -75.05
REMARK 500 19 SER A 146 79.90 40.08
REMARK 500 19 ILE A 150 86.76 66.18
REMARK 500 20 ALA A 14 -174.77 48.13
REMARK 500 20 LYS A 30 -71.60 -91.47
REMARK 500 20 ALA A 31 86.98 87.00
REMARK 500 20 PHE A 32 88.73 57.66
REMARK 500 20 SER A 44 -81.48 -81.47
REMARK 500 20 LEU A 83 -71.53 -73.83
REMARK 500 20 VAL A 86 88.91 -61.45
REMARK 500 20 HIS A 87 49.24 179.74
REMARK 500 20 GLN A 95 -164.16 -117.91
REMARK 500 20 PRO A 125 46.87 -75.05
REMARK 500 20 TRP A 133 -70.48 -62.24
REMARK 500 20 THR A 148 160.11 -48.35
REMARK 500 20 SER A 149 99.80 -179.47
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1A43 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE HIV-1 CAPSID PROTEIN
REMARK 900 DIMERIZATION DOMAINAT 2.6A RESOLUTION
REMARK 900 RELATED ID: 1A8O RELATED DB: PDB
REMARK 900 HIV CAPSID C-TERMINAL DOMAIN
REMARK 900 RELATED ID: 1AFV RELATED DB: PDB
REMARK 900 HIV-1 CAPSID PROTEIN (P24) COMPLEX WITH
REMARK 900 FAB25.3
REMARK 900 RELATED ID: 1AK4 RELATED DB: PDB
REMARK 900 HUMAN CYCLOPHILIN A BOUND TO THE AMINO-
REMARK 900 TERMINAL DOMAIN OF HIV-1 CAPSID
REMARK 900 RELATED ID: 1AUM RELATED DB: PDB
REMARK 900 HIV CAPSID C-TERMINAL DOMAIN (CAC146)
REMARK 900 RELATED ID: 1BAJ RELATED DB: PDB
REMARK 900 HIV-1 CAPSID PROTEIN C-TERMINAL FRAGMENT
REMARK 900 PLUS GAG P2 DOMAIN
REMARK 900 RELATED ID: 1HIW RELATED DB: PDB
REMARK 900 TRIMERIC HIV-1 MATRIX PROTEIN
REMARK 900 RELATED ID: 2HMX RELATED DB: PDB
REMARK 900 HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 MATRIX
REMARK 900 PROTEIN 2HMX 3
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 GENBANK PID G902799 FOR GAG POLYPROTEIN PRECURSOR
DBREF 1GWP A 1 151 UNP P12493 GAG_HV1N5 132 282
SEQRES 1 A 151 PRO ILE VAL GLN ASN LEU GLN GLY GLN MET VAL HIS GLN
SEQRES 2 A 151 ALA ILE SER PRO ARG THR LEU ASN ALA TRP VAL LYS VAL
SEQRES 3 A 151 VAL GLU GLU LYS ALA PHE SER PRO GLU VAL ILE PRO MET
SEQRES 4 A 151 PHE SER ALA LEU SER GLU GLY ALA THR PRO GLN ASP LEU
SEQRES 5 A 151 ASN THR MET LEU ASN THR VAL GLY GLY HIS GLN ALA ALA
SEQRES 6 A 151 MET GLN MET LEU LYS GLU THR ILE ASN GLU GLU ALA ALA
SEQRES 7 A 151 GLU TRP ASP ARG LEU HIS PRO VAL HIS ALA GLY PRO ILE
SEQRES 8 A 151 ALA PRO GLY GLN MET ARG GLU PRO ARG GLY SER ASP ILE
SEQRES 9 A 151 ALA GLY THR THR SER THR LEU GLN GLU GLN ILE GLY TRP
SEQRES 10 A 151 MET THR HIS ASN PRO PRO ILE PRO VAL GLY GLU ILE TYR
SEQRES 11 A 151 LYS ARG TRP ILE ILE LEU GLY LEU ASN LYS ILE VAL ARG
SEQRES 12 A 151 MET TYR SER PRO THR SER ILE LEU
HELIX 1 1 SER A 16 LYS A 30 1 15
HELIX 2 2 SER A 33 SER A 44 1 12
HELIX 3 3 THR A 48 VAL A 59 1 12
HELIX 4 4 HIS A 62 HIS A 84 1 23
HELIX 5 5 ARG A 100 ALA A 105 1 6
HELIX 6 6 THR A 110 THR A 119 1 10
HELIX 7 7 VAL A 126 SER A 146 1 21
SHEET 1 AA 2 PRO A 1 ASN A 5 0
SHEET 2 AA 2 GLN A 9 GLN A 13 -1 O VAL A 11 N VAL A 3
CISPEP 1 ASN A 121 PRO A 122 1 0.00
CISPEP 2 ASN A 121 PRO A 122 2 -0.02
CISPEP 3 ASN A 121 PRO A 122 3 -0.01
CISPEP 4 ASN A 121 PRO A 122 4 0.01
CISPEP 5 ASN A 121 PRO A 122 5 0.09
CISPEP 6 ASN A 121 PRO A 122 6 -0.04
CISPEP 7 ASN A 121 PRO A 122 7 -0.02
CISPEP 8 ASN A 121 PRO A 122 8 -0.02
CISPEP 9 ASN A 121 PRO A 122 9 -0.03
CISPEP 10 ASN A 121 PRO A 122 10 0.04
CISPEP 11 ASN A 121 PRO A 122 11 -0.04
CISPEP 12 ASN A 121 PRO A 122 12 -0.03
CISPEP 13 ASN A 121 PRO A 122 13 -0.02
CISPEP 14 ASN A 121 PRO A 122 14 -0.07
CISPEP 15 ASN A 121 PRO A 122 15 0.03
CISPEP 16 ASN A 121 PRO A 122 16 -0.06
CISPEP 17 ASN A 121 PRO A 122 17 0.07
CISPEP 18 ASN A 121 PRO A 122 18 -0.05
CISPEP 19 ASN A 121 PRO A 122 19 -0.10
CISPEP 20 ASN A 121 PRO A 122 20 0.00
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 14 2 Bytes