Header list of 1jfw.pdb file
Complete list - b 23 2 Bytes
HEADER VIRAL PROTEIN 22-JUN-01 1JFW
TITLE HOMONUCLEAR AND HETERONUCLEAR 1H-13C NUCLEAR MAGNETIC RESONANCE
TITLE 2 ASSIGNMENT AND STRUCTURAL CHARACTERIZATION OF A HIV-1 TAT PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TAT PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: TRANSACTIVATING REGULATORY PROTEIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THIS PEPTIDE WAS SYNTHESIZED (SOLID PHASE SYNTHESIS).
SOURCE 4 THE SEQUENCE OF THIS PEPTIDE OCCURS NATURALLY IN HUMAN
SOURCE 5 IMMUNODEFICIENCY VIRUS TYPE 1
KEYWDS TAT, HIV-1, HETERONUCLEAR, DRUG DESIGN, VIRAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 11
AUTHOR J.M.PELOPONESE,C.GREGOIRE,S.OPI,D.ESQUIEU
REVDAT 4 23-FEB-22 1JFW 1 REMARK
REVDAT 3 24-FEB-09 1JFW 1 VERSN
REVDAT 2 01-APR-03 1JFW 1 JRNL
REVDAT 1 15-AUG-01 1JFW 0
SPRSDE 15-AUG-01 1JFW 1FKU
JRNL AUTH J.M.PELOPONESE JR.,C.GREGOIRE,S.OPI,D.ESQUIEU,J.STURGIS,
JRNL AUTH 2 E.LEBRUN,E.MEURS,Y.COLLETTE,D.OLIVE,A.M.AUBERTIN,M.WITVROW,
JRNL AUTH 3 C.PANNECOUQUE,E.DE CLERCQ,C.BAILLY,J.LEBRETON,E.P.LORET
JRNL TITL 1H-13C NUCLEAR MAGNETIC RESONANCE ASSIGNMENT AND STRUCTURAL
JRNL TITL 2 CHARACTERIZATION OF HIV-1 TAT PROTEIN.
JRNL REF C.R.ACAD.SCI.III V. 323 883 2000
JRNL REFN ISSN 0764-4469
JRNL PMID 11098404
JRNL DOI 10.1016/S0764-4469(00)01228-2
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DISCOVER 95, 97
REMARK 3 AUTHORS : MSI
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 915 RESTRAINTS AND 272 ARE LONG-RANGE NOES.
REMARK 4
REMARK 4 1JFW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JUN-01.
REMARK 100 THE DEPOSITION ID IS D_1000013721.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298.00
REMARK 210 PH : 4.50
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : SPECIFIC 13C LABELLING OF
REMARK 210 GLYCINE 15,44,48,61,79,83
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; 2D NOESY; 3D_ 13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 95, 97 AND 98, NMR_REFINE
REMARK 210 97, HOMOLOGY 95
REMARK 210 METHOD USED : SIMULATED ANNEALING, RANDOM LOOP
REMARK 210 RESEARCH VALIDATED WITH NOE BACK-
REMARK 210 CALCULATION ENERGY MINIMIZATION
REMARK 210 AND MOLECULAR DYNAMIC
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 11
REMARK 210 CONFORMERS, SELECTION CRITERIA : BACK CALCULATED DATA AGREE WITH
REMARK 210 EXPERIMEN TAL NOESY SPECTRUM,
REMARK 210 STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY,STRUCTURES
REMARK 210 WITH FAVORABLE NON-BOND ENERGY,
REMARK 210 STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY, TARGET
REMARK 210 FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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: MONOMERIC
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: 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
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 1 GLU A 2 CD GLU A 2 OE2 0.105
REMARK 500 1 GLU A 9 CD GLU A 9 OE2 0.108
REMARK 500 1 HIS A 13 CG HIS A 13 CD2 0.054
REMARK 500 1 HIS A 33 CG HIS A 33 CD2 0.055
REMARK 500 1 GLU A 86 CD GLU A 86 OE2 0.110
REMARK 500 2 HIS A 13 CG HIS A 13 CD2 0.058
REMARK 500 3 GLU A 2 CD GLU A 2 OE2 0.106
REMARK 500 3 GLU A 9 CD GLU A 9 OE2 0.108
REMARK 500 3 HIS A 13 CG HIS A 13 CD2 0.054
REMARK 500 3 GLU A 86 CD GLU A 86 OE2 0.109
REMARK 500 4 GLU A 2 CD GLU A 2 OE2 0.106
REMARK 500 4 GLU A 9 CD GLU A 9 OE2 0.109
REMARK 500 4 HIS A 13 CG HIS A 13 CD2 0.059
REMARK 500 4 GLU A 86 CD GLU A 86 OE2 0.109
REMARK 500 5 HIS A 13 CG HIS A 13 CD2 0.056
REMARK 500 6 HIS A 13 CG HIS A 13 CD2 0.055
REMARK 500 7 HIS A 13 CG HIS A 13 CD2 0.055
REMARK 500 8 GLU A 2 CD GLU A 2 OE2 0.109
REMARK 500 8 GLU A 9 CD GLU A 9 OE2 0.108
REMARK 500 8 HIS A 13 CG HIS A 13 CD2 0.057
REMARK 500 8 HIS A 33 CG HIS A 33 CD2 0.055
REMARK 500 8 GLU A 86 CD GLU A 86 OE2 0.109
REMARK 500 9 GLU A 2 CD GLU A 2 OE2 0.109
REMARK 500 9 GLU A 9 CD GLU A 9 OE2 0.109
REMARK 500 9 HIS A 13 CG HIS A 13 CD2 0.059
REMARK 500 9 HIS A 33 CG HIS A 33 CD2 0.055
REMARK 500 9 GLU A 86 CD GLU A 86 OE2 0.109
REMARK 500 10 GLU A 2 CD GLU A 2 OE2 0.106
REMARK 500 10 GLU A 9 CD GLU A 9 OE2 0.108
REMARK 500 10 HIS A 13 CG HIS A 13 CD2 0.058
REMARK 500 10 HIS A 33 CG HIS A 33 CD2 0.054
REMARK 500 10 GLU A 86 CD GLU A 86 OE2 0.109
REMARK 500 11 GLU A 2 CD GLU A 2 OE2 0.106
REMARK 500 11 GLU A 9 CD GLU A 9 OE2 0.108
REMARK 500 11 GLU A 86 CD GLU A 86 OE2 0.109
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 1 ASP A 5 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 1 ASP A 5 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 1 ARG A 7 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 1 HIS A 13 ND1 - CE1 - NE2 ANGL. DEV. = 8.2 DEGREES
REMARK 500 1 HIS A 33 ND1 - CE1 - NE2 ANGL. DEV. = 8.4 DEGREES
REMARK 500 1 ARG A 49 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 1 ARG A 52 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 1 ARG A 53 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 1 ARG A 53 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 1 ARG A 55 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 1 ARG A 56 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 1 ARG A 56 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 1 ARG A 57 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 1 HIS A 65 ND1 - CE1 - NE2 ANGL. DEV. = 8.4 DEGREES
REMARK 500 1 ARG A 78 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 2 ARG A 7 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 2 HIS A 13 ND1 - CE1 - NE2 ANGL. DEV. = 8.3 DEGREES
REMARK 500 2 HIS A 33 ND1 - CE1 - NE2 ANGL. DEV. = 8.4 DEGREES
REMARK 500 2 TYR A 47 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 2 ARG A 49 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 2 ARG A 52 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 2 ARG A 53 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 2 ARG A 55 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 2 ARG A 56 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 2 ARG A 57 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 HIS A 65 ND1 - CE1 - NE2 ANGL. DEV. = 8.2 DEGREES
REMARK 500 2 ARG A 78 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 3 ASP A 5 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 3 ASP A 5 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 3 ARG A 7 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 3 HIS A 13 ND1 - CE1 - NE2 ANGL. DEV. = 8.1 DEGREES
REMARK 500 3 HIS A 33 ND1 - CE1 - NE2 ANGL. DEV. = 8.4 DEGREES
REMARK 500 3 ARG A 49 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 3 ARG A 49 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 3 ARG A 52 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 3 ARG A 53 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 3 ARG A 53 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 3 ARG A 55 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 3 ARG A 56 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 3 ARG A 56 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 3 ARG A 57 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 3 HIS A 65 ND1 - CE1 - NE2 ANGL. DEV. = 8.4 DEGREES
REMARK 500 3 ARG A 78 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 4 ARG A 7 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 4 ARG A 7 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 4 HIS A 13 ND1 - CE1 - NE2 ANGL. DEV. = 8.2 DEGREES
REMARK 500 4 HIS A 33 ND1 - CE1 - NE2 ANGL. DEV. = 8.3 DEGREES
REMARK 500 4 ARG A 49 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 4 ARG A 52 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 4 ARG A 52 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 171 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 GLU A 2 -70.59 -79.50
REMARK 500 1 VAL A 4 -60.17 -90.29
REMARK 500 1 LYS A 12 64.28 -150.52
REMARK 500 1 SER A 16 95.55 -165.56
REMARK 500 1 GLN A 17 -62.72 -134.82
REMARK 500 1 THR A 20 -81.98 -149.51
REMARK 500 1 CYS A 22 -70.18 60.31
REMARK 500 1 THR A 24 119.01 79.09
REMARK 500 1 TYR A 26 -24.19 78.64
REMARK 500 1 CYS A 27 -64.59 75.30
REMARK 500 1 LYS A 29 -69.90 -108.51
REMARK 500 1 PHE A 32 -36.51 76.38
REMARK 500 1 CYS A 37 -61.04 -94.50
REMARK 500 1 PHE A 38 -53.92 67.90
REMARK 500 1 ALA A 42 -63.07 -91.01
REMARK 500 1 ILE A 45 -69.52 -24.05
REMARK 500 1 LYS A 50 -56.89 68.51
REMARK 500 1 ARG A 55 -67.88 -137.15
REMARK 500 1 SER A 62 -79.47 -140.09
REMARK 500 1 HIS A 65 -98.93 50.86
REMARK 500 1 VAL A 67 -70.93 -120.15
REMARK 500 1 SER A 68 104.46 64.74
REMARK 500 1 SER A 70 -92.10 -163.64
REMARK 500 1 SER A 75 -89.55 64.94
REMARK 500 1 ASP A 80 80.45 69.16
REMARK 500 1 THR A 82 -83.16 -151.77
REMARK 500 2 LYS A 12 86.60 -151.93
REMARK 500 2 SER A 16 67.11 -164.88
REMARK 500 2 GLN A 17 -66.07 -95.08
REMARK 500 2 THR A 20 -87.81 -142.32
REMARK 500 2 CYS A 22 -76.67 64.86
REMARK 500 2 THR A 24 111.04 73.50
REMARK 500 2 CYS A 27 -82.70 68.94
REMARK 500 2 LYS A 28 46.77 -92.61
REMARK 500 2 LYS A 29 -65.57 -140.55
REMARK 500 2 PHE A 32 -39.98 75.24
REMARK 500 2 PHE A 38 -53.68 67.69
REMARK 500 2 ALA A 42 -52.65 -134.13
REMARK 500 2 LYS A 50 -55.65 65.91
REMARK 500 2 ARG A 55 -78.72 -139.02
REMARK 500 2 ARG A 57 81.91 53.39
REMARK 500 2 SER A 62 -73.42 -110.32
REMARK 500 2 HIS A 65 -120.41 27.94
REMARK 500 2 GLN A 66 65.45 -101.74
REMARK 500 2 VAL A 67 -72.05 -113.07
REMARK 500 2 SER A 68 108.44 62.94
REMARK 500 2 LEU A 69 107.23 -54.80
REMARK 500 2 SER A 70 -84.35 -155.84
REMARK 500 2 PRO A 73 83.27 -64.53
REMARK 500 2 SER A 75 -86.72 61.84
REMARK 500
REMARK 500 THIS ENTRY HAS 290 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 TRP A 11 LYS A 12 1 144.62
REMARK 500 ALA A 21 CYS A 22 1 -147.95
REMARK 500 PRO A 84 LYS A 85 1 131.38
REMARK 500 TRP A 11 LYS A 12 2 127.15
REMARK 500 GLY A 79 ASP A 80 2 -138.42
REMARK 500 ALA A 21 CYS A 22 3 -147.45
REMARK 500 LYS A 85 GLU A 86 3 123.83
REMARK 500 TRP A 11 LYS A 12 4 147.94
REMARK 500 ALA A 21 CYS A 22 5 -129.63
REMARK 500 ALA A 21 CYS A 22 7 -148.83
REMARK 500 LEU A 8 GLU A 9 11 149.46
REMARK 500 SER A 16 GLN A 17 11 -136.24
REMARK 500 ALA A 21 CYS A 22 11 -148.06
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1JFW A 1 86 UNP P04610 TAT_HV1BR 1 86
SEQRES 1 A 86 MET GLU PRO VAL ASP PRO ARG LEU GLU PRO TRP LYS HIS
SEQRES 2 A 86 PRO GLY SER GLN PRO LYS THR ALA CYS THR THR CYS TYR
SEQRES 3 A 86 CYS LYS LYS CYS CYS PHE HIS CYS GLN VAL CYS PHE THR
SEQRES 4 A 86 THR LYS ALA LEU GLY ILE SER TYR GLY ARG LYS LYS ARG
SEQRES 5 A 86 ARG GLN ARG ARG ARG PRO PRO GLN GLY SER GLN THR HIS
SEQRES 6 A 86 GLN VAL SER LEU SER LYS GLN PRO THR SER GLN PRO ARG
SEQRES 7 A 86 GLY ASP PRO THR GLY PRO LYS GLU
SHEET 1 A 2 LEU A 43 GLY A 44 0
SHEET 2 A 2 TYR A 47 GLY A 48 -1 N TYR A 47 O GLY A 44
CISPEP 1 PRO A 84 LYS A 85 3 10.01
CISPEP 2 PRO A 84 LYS A 85 4 3.12
CISPEP 3 LYS A 85 GLU A 86 4 14.02
CISPEP 4 PRO A 84 LYS A 85 5 1.47
CISPEP 5 LYS A 85 GLU A 86 5 13.16
CISPEP 6 PRO A 84 LYS A 85 6 -1.92
CISPEP 7 LYS A 85 GLU A 86 6 21.25
CISPEP 8 PRO A 84 LYS A 85 7 -1.36
CISPEP 9 LYS A 85 GLU A 86 7 21.04
CISPEP 10 PRO A 84 LYS A 85 8 1.52
CISPEP 11 LYS A 85 GLU A 86 8 21.23
CISPEP 12 PRO A 84 LYS A 85 9 1.31
CISPEP 13 LYS A 85 GLU A 86 9 17.08
CISPEP 14 PRO A 84 LYS A 85 10 0.96
CISPEP 15 LYS A 85 GLU A 86 10 17.74
CISPEP 16 PRO A 84 LYS A 85 11 -1.46
CISPEP 17 LYS A 85 GLU A 86 11 20.72
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 - b 23 2 Bytes