Header list of 1gxh.pdb file
Complete list - r 25 2 Bytes
HEADER INHIBITOR 05-APR-02 1GXH
TITLE COLICIN E8 DNASE IMMUNITY PROTEIN: IM8
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COLICIN E8 IMMUNITY PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: IMME8, MICROCIN E8 IMMUNITY PROTEIN;
COMPND 5 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: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS INHIBITOR, INHIBITOR PROTEIN OF DNASE COLICIN E8,
KEYWDS 2 BACTERIOCIN IMMUNITY, PLASMID, DNASE INHIBITOR
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR C.S.LEDUFF,H.VIDELER,R.BOETZEL,M.CZISCH,R.JAMES,
AUTHOR 2 C.KLEANTHOUS,G.R.MOORE
REVDAT 2 24-FEB-09 1GXH 1 VERSN
REVDAT 1 01-MAY-02 1GXH 0
SPRSDE 05-APR-02 1GXH 1IMY
JRNL AUTH C.S.LEDUFF,H.VIDELER,R.BOETZEL,M.CZISCH,R.JAMES,
JRNL AUTH 2 C.KLEANTHOUS,G.R.MOORE
JRNL TITL NON-COGNATE PROTEIN-PROTEIN INTERACTION: THE NMR
JRNL TITL 2 STRUCTURE OF THE COLICIN E8 INHIBITOR PROTEIN IM8
JRNL TITL 3 AND ITS INTERACTION WITH THE DNASE DOMAIN OF
JRNL TITL 4 COLICIN E9
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : OPAL
REMARK 3 AUTHORS : LUGINBUHL,GUNTERT,BILLETER,WUTHRICH
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT IN VACUO
REMARK 4
REMARK 4 1GXH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-APR-02.
REMARK 100 THE PDBE ID CODE IS EBI-9658.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.2
REMARK 210 IONIC STRENGTH : 0.05M
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 0.01M DT
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY, 2D NOESY,
REMARK 210 3D 15N-EDITED NOESY,
REMARK 210 3D 15N EDITED TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750
REMARK 210 SPECTROMETER MODEL : UNITY+
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA AND REFINEMENT IN
REMARK 210 OPAL
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 300
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : THE 30 LOWEST TARGET
REMARK 210 FUNCTION STRUCTURES FROM DYANA
REMARK 210 WERE ENERGY MINIMISED IN OPAL;
REMARK 210 THE 20 LOWEST ENERGY STRUCTURES
REMARK 210 WERE CHOSEN AS THE FINAL
REMARK 210 ENSEMBLE
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: STRUCTURE DETERMINED USING 15N-LABELLED IM8. THE BEST
REMARK 210 REPRESENTATIVE CONFORMER FOR THIS ENSEMBLE HAS BEEN SUBMITTED
REMARK 210 AS A SEPARATE PDB ENTRY, 1GXG.
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 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 O PHE A 39 - HG1 THR A 43 1.55
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 VAL A 42 CA - CB - CG2 ANGL. DEV. = 9.7 DEGREES
REMARK 500 2 TYR A 10 CB - CG - CD1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 2 ILE A 18 CA - CB - CG2 ANGL. DEV. = 12.4 DEGREES
REMARK 500 3 VAL A 42 CA - CB - CG2 ANGL. DEV. = 12.3 DEGREES
REMARK 500 4 TYR A 10 CB - CG - CD1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 4 VAL A 42 CA - CB - CG2 ANGL. DEV. = 9.9 DEGREES
REMARK 500 5 SER A 8 N - CA - CB ANGL. DEV. = -9.3 DEGREES
REMARK 500 5 ARG A 74 CD - NE - CZ ANGL. DEV. = 11.5 DEGREES
REMARK 500 7 VAL A 42 CA - CB - CG2 ANGL. DEV. = 10.2 DEGREES
REMARK 500 8 VAL A 42 CA - CB - CG1 ANGL. DEV. = 9.9 DEGREES
REMARK 500 9 VAL A 42 CA - CB - CG2 ANGL. DEV. = 13.0 DEGREES
REMARK 500 10 VAL A 42 CA - CB - CG2 ANGL. DEV. = 9.1 DEGREES
REMARK 500 12 THR A 11 CA - CB - CG2 ANGL. DEV. = 9.0 DEGREES
REMARK 500 13 VAL A 42 CA - CB - CG2 ANGL. DEV. = 10.2 DEGREES
REMARK 500 14 VAL A 42 CA - CB - CG2 ANGL. DEV. = 11.6 DEGREES
REMARK 500 15 ILE A 18 CA - CB - CG2 ANGL. DEV. = 12.5 DEGREES
REMARK 500 15 VAL A 42 CA - CB - CG2 ANGL. DEV. = 9.1 DEGREES
REMARK 500 17 TYR A 10 CB - CG - CD1 ANGL. DEV. = -4.2 DEGREES
REMARK 500 17 VAL A 42 CA - CB - CG2 ANGL. DEV. = 10.5 DEGREES
REMARK 500 19 TYR A 10 CB - CG - CD1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 19 VAL A 42 CA - CB - CG1 ANGL. DEV. = 9.4 DEGREES
REMARK 500 20 VAL A 42 CA - CB - CG2 ANGL. DEV. = 9.9 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 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 CYS A 25 56.22 104.24
REMARK 500 1 ASP A 28 17.51 -145.83
REMARK 500 1 GLU A 29 -43.30 66.26
REMARK 500 1 GLU A 44 2.83 58.94
REMARK 500 1 PHE A 82 -174.19 -67.06
REMARK 500 2 GLU A 2 54.45 -98.13
REMARK 500 2 GLU A 29 -36.23 63.83
REMARK 500 2 THR A 43 -159.29 -78.43
REMARK 500 2 GLU A 44 13.35 -150.37
REMARK 500 2 SER A 49 -13.53 173.89
REMARK 500 2 SER A 62 169.54 178.79
REMARK 500 2 PRO A 63 2.45 -64.12
REMARK 500 2 LYS A 83 128.91 -38.59
REMARK 500 3 GLU A 2 35.26 -78.73
REMARK 500 3 LEU A 3 -178.08 -67.14
REMARK 500 3 LYS A 4 117.40 -36.14
REMARK 500 3 CYS A 25 72.75 87.34
REMARK 500 3 ASP A 28 37.85 -148.93
REMARK 500 3 GLU A 29 -47.59 79.49
REMARK 500 3 GLU A 44 -0.25 65.54
REMARK 500 3 PHE A 82 -172.02 -60.83
REMARK 500 3 LYS A 83 156.80 -38.11
REMARK 500 4 GLU A 2 52.41 -93.55
REMARK 500 4 THR A 11 146.43 -28.07
REMARK 500 4 CYS A 25 64.16 62.95
REMARK 500 4 SER A 49 -39.36 72.38
REMARK 500 4 LYS A 68 -71.99 -38.29
REMARK 500 4 LYS A 79 124.52 -38.63
REMARK 500 5 GLU A 2 99.37 -31.14
REMARK 500 5 LEU A 3 -169.54 40.63
REMARK 500 5 THR A 11 140.25 -27.37
REMARK 500 5 ASP A 28 -153.79 -88.38
REMARK 500 5 SER A 49 -38.73 65.22
REMARK 500 5 ASN A 59 66.47 -105.65
REMARK 500 5 PHE A 82 -176.43 -67.29
REMARK 500 6 GLU A 2 -176.05 59.56
REMARK 500 6 CYS A 25 54.15 84.43
REMARK 500 6 ASP A 28 35.88 -142.36
REMARK 500 6 GLU A 29 -48.31 78.97
REMARK 500 6 LYS A 79 128.48 -34.05
REMARK 500 6 PHE A 82 -172.35 -67.08
REMARK 500 6 LYS A 83 164.72 -46.38
REMARK 500 7 GLU A 2 51.24 -95.95
REMARK 500 7 THR A 11 142.02 -30.74
REMARK 500 7 CYS A 25 56.23 88.14
REMARK 500 7 GLU A 44 2.04 58.47
REMARK 500 7 SER A 49 -20.27 72.31
REMARK 500 7 LYS A 79 108.67 17.34
REMARK 500 7 PHE A 82 -166.13 -61.65
REMARK 500 8 LEU A 3 -163.01 -67.47
REMARK 500 8 TYR A 10 53.87 -114.54
REMARK 500 8 THR A 11 141.60 -26.82
REMARK 500 8 ILE A 22 -76.83 -74.75
REMARK 500 8 CYS A 25 84.07 77.13
REMARK 500 8 LYS A 79 106.03 -20.32
REMARK 500 8 PHE A 82 -164.78 -63.82
REMARK 500 9 GLU A 2 175.80 60.66
REMARK 500 9 LEU A 3 43.83 -68.50
REMARK 500 9 LYS A 4 169.52 74.20
REMARK 500 9 ASN A 5 -2.42 -146.21
REMARK 500 9 THR A 11 133.49 -23.26
REMARK 500 9 CYS A 25 57.48 87.85
REMARK 500 9 SER A 49 -18.84 101.16
REMARK 500 9 ASN A 58 35.34 -79.25
REMARK 500 9 PHE A 82 -162.19 -65.26
REMARK 500 9 LYS A 83 164.70 -44.81
REMARK 500 10 CYS A 25 16.32 49.94
REMARK 500 10 GLU A 29 -29.08 65.75
REMARK 500 10 GLU A 44 3.33 56.38
REMARK 500 10 SER A 49 -32.17 79.94
REMARK 500 10 PRO A 63 2.81 -68.23
REMARK 500 10 LYS A 68 -73.00 -45.13
REMARK 500 10 LYS A 79 107.95 15.95
REMARK 500 10 PHE A 82 -179.14 -60.59
REMARK 500 10 LYS A 83 141.16 -33.82
REMARK 500 11 SER A 6 169.05 164.76
REMARK 500 11 THR A 11 139.66 -25.30
REMARK 500 11 CYS A 25 25.68 83.47
REMARK 500 11 GLU A 44 3.91 56.76
REMARK 500 11 LYS A 68 -78.43 -39.22
REMARK 500 11 ILE A 70 -71.84 -69.10
REMARK 500 11 PHE A 82 -167.26 -67.84
REMARK 500 11 LYS A 83 164.38 -49.92
REMARK 500 12 THR A 11 144.02 -31.63
REMARK 500 12 CYS A 25 59.85 98.65
REMARK 500 12 THR A 43 -176.92 -64.94
REMARK 500 12 SER A 49 -17.26 65.31
REMARK 500 12 LYS A 79 104.49 -19.78
REMARK 500 12 PHE A 82 -157.25 -66.02
REMARK 500 12 LYS A 83 164.25 -40.64
REMARK 500 13 GLU A 2 -164.37 59.51
REMARK 500 13 TYR A 10 56.97 -90.01
REMARK 500 13 THR A 11 146.70 -34.51
REMARK 500 13 CYS A 25 64.68 92.32
REMARK 500 13 LYS A 79 117.98 -3.55
REMARK 500 13 LYS A 83 153.02 -44.92
REMARK 500 14 GLU A 2 34.44 -79.15
REMARK 500 14 CYS A 25 72.54 65.27
REMARK 500 14 ASP A 28 -158.05 -93.19
REMARK 500 14 SER A 49 -11.93 -48.79
REMARK 500 14 ASN A 58 -37.36 138.24
REMARK 500 14 PRO A 63 -8.75 -56.93
REMARK 500 14 LYS A 79 107.19 23.39
REMARK 500 14 PHE A 82 -174.69 -68.56
REMARK 500 15 GLU A 2 30.63 -152.93
REMARK 500 15 LEU A 3 -168.68 -101.87
REMARK 500 15 TYR A 10 56.38 -94.16
REMARK 500 15 THR A 11 144.72 -32.77
REMARK 500 15 CYS A 25 44.04 90.73
REMARK 500 15 ASN A 59 71.65 -68.13
REMARK 500 15 PRO A 63 -9.92 -57.25
REMARK 500 15 LYS A 68 -77.89 -35.59
REMARK 500 15 LYS A 79 106.13 16.15
REMARK 500 16 GLU A 29 -57.59 81.16
REMARK 500 16 LYS A 31 1.02 -66.12
REMARK 500 16 SER A 49 -8.29 -58.44
REMARK 500 16 LYS A 83 131.76 -35.61
REMARK 500 17 THR A 11 145.99 -34.53
REMARK 500 17 CYS A 25 18.48 86.64
REMARK 500 17 ASP A 28 35.49 -78.16
REMARK 500 17 GLU A 29 -51.43 79.20
REMARK 500 17 GLU A 44 5.23 59.61
REMARK 500 17 ASN A 58 0.28 122.73
REMARK 500 17 LYS A 68 -75.66 -37.69
REMARK 500 18 LEU A 3 -179.89 41.50
REMARK 500 18 CYS A 25 55.44 89.24
REMARK 500 18 THR A 43 -151.59 -68.06
REMARK 500 18 GLU A 44 16.10 -156.32
REMARK 500 18 LYS A 68 -72.74 -48.24
REMARK 500 18 PHE A 82 -163.69 -74.17
REMARK 500 18 LYS A 83 141.22 -31.64
REMARK 500 19 LEU A 3 -160.90 -69.50
REMARK 500 19 LYS A 4 129.41 -37.06
REMARK 500 19 SER A 6 172.17 178.52
REMARK 500 19 THR A 11 141.36 -27.30
REMARK 500 19 CYS A 25 60.40 134.18
REMARK 500 19 GLU A 44 2.60 58.83
REMARK 500 19 SER A 49 -17.55 68.51
REMARK 500 19 PRO A 63 -1.34 -57.64
REMARK 500 19 LYS A 79 96.68 21.36
REMARK 500 19 PHE A 82 -163.94 -61.73
REMARK 500 19 LYS A 83 165.40 -49.75
REMARK 500 20 LYS A 79 108.78 -7.64
REMARK 500 20 PHE A 82 -176.25 -67.48
REMARK 500 20 LYS A 83 135.43 -38.17
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 MET A 1 GLU A 2 5 117.42
REMARK 500 MET A 1 GLU A 2 10 132.02
REMARK 500 MET A 1 GLU A 2 18 131.48
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 1 TYR A 10 0.08 SIDE CHAIN
REMARK 500 2 TYR A 10 0.07 SIDE CHAIN
REMARK 500 2 ARG A 74 0.17 SIDE CHAIN
REMARK 500 3 ARG A 74 0.08 SIDE CHAIN
REMARK 500 4 ARG A 74 0.11 SIDE CHAIN
REMARK 500 6 ARG A 74 0.11 SIDE CHAIN
REMARK 500 7 ARG A 74 0.10 SIDE CHAIN
REMARK 500 8 HIS A 38 0.10 SIDE CHAIN
REMARK 500 8 ARG A 74 0.12 SIDE CHAIN
REMARK 500 9 TYR A 10 0.07 SIDE CHAIN
REMARK 500 10 ASP A 33 0.07 SIDE CHAIN
REMARK 500 10 ARG A 74 0.09 SIDE CHAIN
REMARK 500 11 ARG A 74 0.13 SIDE CHAIN
REMARK 500 12 ASP A 33 0.08 SIDE CHAIN
REMARK 500 12 ARG A 74 0.13 SIDE CHAIN
REMARK 500 14 ASP A 33 0.07 SIDE CHAIN
REMARK 500 14 TYR A 53 0.07 SIDE CHAIN
REMARK 500 14 ARG A 74 0.10 SIDE CHAIN
REMARK 500 15 ARG A 74 0.09 SIDE CHAIN
REMARK 500 18 ARG A 74 0.20 SIDE CHAIN
REMARK 500 19 ARG A 74 0.13 SIDE CHAIN
REMARK 500 20 ARG A 74 0.13 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 16 CYS A 25 24.1 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1GXG RELATED DB: PDB
REMARK 900 NON-COGNATE PROTEIN-PROTEIN INTERACTIONS: THE
REMARK 900 NMR STRUCTURE OF THE COLICIN E8 INHIBITOR
REMARK 900 PROTEIN IM8 AND ITS INTERACTION WITH THE
REMARK 900 DNASE DOMAIN OF COLICIN E9
REMARK 900 RELATED ID: 1IMY RELATED DB: PDB
REMARK 900 COLICIN E8 IMMUNITY PROTEIN IM8, NMR, 20
REMARK 900 STRUCTURES
REMARK 900 RELATED ID: 1IMZ RELATED DB: PDB
REMARK 900 COLICIN E8 IMMUNITY PROTEIN IM8, NMR,
REMARK 900 MINIMIZED AVERAGE STRUCTURE
DBREF 1GXH A 1 85 UNP P09881 IMM8_ECOLI 1 85
SEQRES 1 A 85 MET GLU LEU LYS ASN SER ILE SER ASP TYR THR GLU THR
SEQRES 2 A 85 GLU PHE LYS LYS ILE ILE GLU ASP ILE ILE ASN CYS GLU
SEQRES 3 A 85 GLY ASP GLU LYS LYS GLN ASP ASP ASN LEU GLU HIS PHE
SEQRES 4 A 85 ILE SER VAL THR GLU HIS PRO SER GLY SER ASP LEU ILE
SEQRES 5 A 85 TYR TYR PRO GLU GLY ASN ASN ASP GLY SER PRO GLU ALA
SEQRES 6 A 85 VAL ILE LYS GLU ILE LYS GLU TRP ARG ALA ALA ASN GLY
SEQRES 7 A 85 LYS SER GLY PHE LYS GLN GLY
HELIX 1 1 THR A 11 CYS A 25 1 15
HELIX 2 2 GLU A 29 VAL A 42 1 14
HELIX 3 3 SER A 49 TYR A 54 1 6
HELIX 4 4 PRO A 63 ASN A 77 1 15
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 25 2 Bytes