Header list of 1zae.pdb file
Complete list - r 2 2 Bytes
HEADER DNA BINDING PROTEIN 06-APR-05 1ZAE
TITLE SOLUTION STRUCTURE OF THE FUNCTIONAL DOMAIN OF PHI29 REPLICATION
TITLE 2 ORGANIZER P16.7C
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EARLY PROTEIN GP16.7;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN;
COMPND 5 SYNONYM: P16.7C;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS PHAGE PHI29;
SOURCE 3 ORGANISM_TAXID: 10756;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET28B
KEYWDS PHI-29 REPLICATION, NONSPECIFIC DNA BINDING PROTEIN, HELICAL DIMER,
KEYWDS 2 DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR J.L.ASENSIO,A.ALBERT,D.MUNOZ-ESPIN,C.GONZALEZ,J.HERMOSO,L.VILLAR,
AUTHOR 2 J.JIMENEZ-BARBERO,M.SALAS,W.J.J.MEIJER
REVDAT 4 02-MAR-22 1ZAE 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1ZAE 1 VERSN
REVDAT 2 21-JUN-05 1ZAE 1 JRNL
REVDAT 1 19-APR-05 1ZAE 0
SPRSDE 19-APR-05 1ZAE 1Z61
JRNL AUTH J.L.ASENSIO,A.ALBERT,D.MUNOZ-ESPIN,C.GONZALEZ,J.HERMOSO,
JRNL AUTH 2 L.VILLAR,J.JIMENEZ-BARBERO,M.SALAS,W.J.J.MEIJER
JRNL TITL STRUCTURE OF THE FUNCTIONAL DOMAIN OF PHI29 REPLICATION
JRNL TITL 2 ORGANIZER: INSIGHTS INTO OLIGOMERIZATION AND DNA BINDING
JRNL REF J.BIOL.CHEM. V. 280 20730 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 15772069
JRNL DOI 10.1074/JBC.M501687200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.4, AMBER 5.0
REMARK 3 AUTHORS : GUNTER, P. (DYANA), KOLLMAN, P. (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ZAE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-APR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032497.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308; 308; 303; 298
REMARK 210 PH : 5; 7; 5; 5
REMARK 210 IONIC STRENGTH : 200MM NACL; 200MM NACL; 200MM
REMARK 210 NACL; 200MM NACL
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT;
REMARK 210 AMBIENT
REMARK 210 SAMPLE CONTENTS : 400UM P16.7C, 200MM NACL, 10MM
REMARK 210 SODIUM PHOSPHATE BUFFER, 4MM DTT
REMARK 210 AT PH 5.0; 800UM P16.7C, 200MM
REMARK 210 NACL, 10MM SODIUM PHOSPHATE
REMARK 210 BUFFER, 4MM DTT AT PH 5.0; 400UM
REMARK 210 P16.7C, 200MM NACL, 10MM SODIUM
REMARK 210 PHOSPHATE BUFFER, 4MM DTT AT PH
REMARK 210 7.0; 800UM P16.7C, 200MM NACL,
REMARK 210 10MM SODIUM PHOSPHATE BUFFER,
REMARK 210 4MM DTT AT PH 7.0
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; DMX
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 MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 25
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES
REMARK 210 SUBMITTED
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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: 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 ARG A 113 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 1 ARG B 113 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 1 ARG B 126 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 2 ARG A 126 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 2 ARG B 113 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 2 ARG B 126 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 3 ARG A 113 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 3 ARG A 126 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 3 ARG B 98 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 3 ARG B 113 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 3 ARG B 126 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 4 ARG A 126 NE - CZ - NH2 ANGL. DEV. = 3.1 DEGREES
REMARK 500 5 ARG A 113 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 5 ARG B 113 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 5 ARG B 126 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 7 ARG A 113 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 7 ARG A 126 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 7 ARG B 85 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 8 ARG A 113 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 8 LEU A 124 CB - CG - CD1 ANGL. DEV. = 10.7 DEGREES
REMARK 500 8 ARG B 113 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 9 ARG B 98 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 9 ARG B 98 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 10 ARG A 113 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 10 ARG B 113 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 11 ARG A 113 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 11 ARG B 126 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 12 ARG A 113 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 13 ARG B 98 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 14 ARG A 98 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 15 ARG A 113 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 15 ARG B 113 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 16 ARG B 98 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 16 ARG B 113 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 16 ARG B 126 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 18 ARG B 113 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 19 ARG A 98 NE - CZ - NH1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 20 ARG A 85 CD - NE - CZ ANGL. DEV. = 8.6 DEGREES
REMARK 500 20 ARG B 126 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 21 ARG A 98 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 23 ARG A 113 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 24 ARG B 113 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 25 ARG A 113 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 25 ARG B 85 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 25 ARG B 126 NE - CZ - NH1 ANGL. DEV. = 3.5 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 1 LYS A 123 109.71 -42.66
REMARK 500 1 TYR A 125 28.93 -69.74
REMARK 500 1 ARG A 126 -60.26 65.00
REMARK 500 1 SER A 128 49.59 -79.44
REMARK 500 1 LYS B 64 44.48 -69.88
REMARK 500 1 THR B 65 69.70 -158.19
REMARK 500 1 ASN B 67 73.36 -161.93
REMARK 500 1 LEU B 68 68.22 70.87
REMARK 500 1 ASP B 93 -74.92 -84.58
REMARK 500 1 ARG B 98 107.54 57.33
REMARK 500 1 SER B 101 -178.83 -171.22
REMARK 500 1 TYR B 125 29.85 -70.67
REMARK 500 1 ARG B 126 -64.67 67.73
REMARK 500 2 ASN A 67 103.54 -53.30
REMARK 500 2 LEU A 68 68.46 61.91
REMARK 500 2 ASP A 89 12.24 -67.26
REMARK 500 2 LYS A 123 100.10 -42.44
REMARK 500 2 TYR A 125 36.54 -72.20
REMARK 500 2 ARG A 126 -71.31 54.85
REMARK 500 2 SER A 128 89.26 -54.49
REMARK 500 2 ASN B 83 44.53 80.53
REMARK 500 2 ARG B 98 76.19 50.92
REMARK 500 2 ARG B 126 -60.77 70.42
REMARK 500 2 SER B 128 76.59 -68.87
REMARK 500 3 THR A 65 -47.72 -153.43
REMARK 500 3 ASN A 67 139.64 -32.37
REMARK 500 3 ARG A 98 113.64 64.30
REMARK 500 3 LYS A 122 130.98 -31.56
REMARK 500 3 TYR A 125 25.60 -74.49
REMARK 500 3 ARG A 126 -60.74 64.95
REMARK 500 3 MET B 62 80.70 -69.58
REMARK 500 3 THR B 65 -135.88 44.31
REMARK 500 3 LEU B 68 82.75 64.35
REMARK 500 3 ASN B 83 34.87 124.14
REMARK 500 3 SER B 88 -41.47 -26.94
REMARK 500 3 ARG B 98 72.63 69.13
REMARK 500 3 LYS B 122 132.63 -38.23
REMARK 500 3 TYR B 125 24.94 -69.94
REMARK 500 3 ARG B 126 -63.70 63.33
REMARK 500 4 LYS A 64 34.64 -78.93
REMARK 500 4 VAL A 66 -9.62 57.33
REMARK 500 4 LEU A 68 87.88 -67.62
REMARK 500 4 ARG A 126 -76.35 67.69
REMARK 500 4 SER A 128 115.16 -29.42
REMARK 500 4 LEU A 129 74.94 -69.67
REMARK 500 4 MET B 62 -155.74 -95.54
REMARK 500 4 ASP B 63 117.51 -38.66
REMARK 500 4 LYS B 64 132.60 -36.38
REMARK 500 4 THR B 65 86.57 -63.62
REMARK 500 4 ASN B 67 102.93 -58.13
REMARK 500
REMARK 500 THIS ENTRY HAS 349 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 LYS A 123 LEU A 124 1 142.65
REMARK 500 LYS A 123 LEU A 124 2 141.19
REMARK 500 ASP A 63 LYS A 64 5 -146.97
REMARK 500 ASN A 67 LEU A 68 7 -135.02
REMARK 500 LYS B 123 LEU B 124 8 149.73
REMARK 500 ASN A 67 LEU A 68 12 -114.13
REMARK 500 LYS B 123 LEU B 124 12 149.17
REMARK 500 LYS B 123 LEU B 124 15 148.67
REMARK 500 LYS A 123 LEU A 124 16 148.45
REMARK 500 LYS B 123 LEU B 124 17 148.75
REMARK 500 LYS A 123 LEU A 124 18 149.38
REMARK 500 ASN A 67 LEU A 68 19 146.00
REMARK 500 ASP B 63 LYS B 64 21 129.44
REMARK 500 LYS B 123 LEU B 124 21 144.20
REMARK 500 LYS A 123 LEU A 124 22 149.98
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 79 0.13 SIDE CHAIN
REMARK 500 1 TYR B 79 0.19 SIDE CHAIN
REMARK 500 1 ARG B 85 0.08 SIDE CHAIN
REMARK 500 1 TYR B 115 0.09 SIDE CHAIN
REMARK 500 1 TYR B 125 0.14 SIDE CHAIN
REMARK 500 2 TYR A 79 0.15 SIDE CHAIN
REMARK 500 2 TYR B 79 0.17 SIDE CHAIN
REMARK 500 2 TYR B 125 0.12 SIDE CHAIN
REMARK 500 3 TYR A 79 0.20 SIDE CHAIN
REMARK 500 3 TYR A 115 0.07 SIDE CHAIN
REMARK 500 3 TYR A 125 0.11 SIDE CHAIN
REMARK 500 3 TYR B 79 0.21 SIDE CHAIN
REMARK 500 3 TYR B 115 0.07 SIDE CHAIN
REMARK 500 3 TYR B 125 0.11 SIDE CHAIN
REMARK 500 4 HIS A 61 0.09 SIDE CHAIN
REMARK 500 4 TYR A 79 0.14 SIDE CHAIN
REMARK 500 4 TYR A 115 0.12 SIDE CHAIN
REMARK 500 4 TYR A 125 0.07 SIDE CHAIN
REMARK 500 4 TYR B 79 0.16 SIDE CHAIN
REMARK 500 4 TYR B 108 0.10 SIDE CHAIN
REMARK 500 4 TYR B 125 0.07 SIDE CHAIN
REMARK 500 5 TYR A 79 0.17 SIDE CHAIN
REMARK 500 5 ARG A 85 0.12 SIDE CHAIN
REMARK 500 5 TYR A 125 0.15 SIDE CHAIN
REMARK 500 5 TYR B 79 0.18 SIDE CHAIN
REMARK 500 6 TYR A 79 0.21 SIDE CHAIN
REMARK 500 6 TYR A 115 0.09 SIDE CHAIN
REMARK 500 6 TYR A 125 0.10 SIDE CHAIN
REMARK 500 6 TYR B 79 0.13 SIDE CHAIN
REMARK 500 6 TYR B 115 0.09 SIDE CHAIN
REMARK 500 7 TYR A 79 0.17 SIDE CHAIN
REMARK 500 7 TYR A 125 0.14 SIDE CHAIN
REMARK 500 7 HIS B 61 0.10 SIDE CHAIN
REMARK 500 7 TYR B 79 0.22 SIDE CHAIN
REMARK 500 7 TYR B 125 0.27 SIDE CHAIN
REMARK 500 8 TYR A 79 0.17 SIDE CHAIN
REMARK 500 8 TYR B 79 0.14 SIDE CHAIN
REMARK 500 9 TYR A 79 0.20 SIDE CHAIN
REMARK 500 9 ARG A 85 0.11 SIDE CHAIN
REMARK 500 9 TYR A 108 0.09 SIDE CHAIN
REMARK 500 9 ARG A 113 0.09 SIDE CHAIN
REMARK 500 9 TYR A 115 0.08 SIDE CHAIN
REMARK 500 9 TYR B 79 0.19 SIDE CHAIN
REMARK 500 9 TYR B 108 0.12 SIDE CHAIN
REMARK 500 10 TYR A 79 0.20 SIDE CHAIN
REMARK 500 10 ARG A 85 0.08 SIDE CHAIN
REMARK 500 10 TYR A 115 0.09 SIDE CHAIN
REMARK 500 10 TYR A 125 0.22 SIDE CHAIN
REMARK 500 10 TYR B 79 0.18 SIDE CHAIN
REMARK 500 10 TYR B 115 0.06 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 147 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2BNK RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF P16.7C
DBREF 1ZAE A 63 130 UNP P16517 VG167_BPPH2 63 130
DBREF 1ZAE B 63 130 UNP P16517 VG167_BPPH2 63 130
SEQADV 1ZAE HIS A 61 UNP P16517 CLONING ARTIFACT
SEQADV 1ZAE MET A 62 UNP P16517 CLONING ARTIFACT
SEQADV 1ZAE HIS B 61 UNP P16517 CLONING ARTIFACT
SEQADV 1ZAE MET B 62 UNP P16517 CLONING ARTIFACT
SEQRES 1 A 70 HIS MET ASP LYS THR VAL ASN LEU SER ALA CYS GLU VAL
SEQRES 2 A 70 ALA VAL LEU ASP LEU TYR GLU GLN SER ASN ILE ARG ILE
SEQRES 3 A 70 PRO SER ASP ILE ILE GLU ASP LEU VAL ASN GLN ARG LEU
SEQRES 4 A 70 GLN SER GLU GLN GLU VAL LEU ASN TYR ILE GLU THR GLN
SEQRES 5 A 70 ARG THR TYR TRP LYS LEU GLU ASN GLN LYS LYS LEU TYR
SEQRES 6 A 70 ARG GLY SER LEU LYS
SEQRES 1 B 70 HIS MET ASP LYS THR VAL ASN LEU SER ALA CYS GLU VAL
SEQRES 2 B 70 ALA VAL LEU ASP LEU TYR GLU GLN SER ASN ILE ARG ILE
SEQRES 3 B 70 PRO SER ASP ILE ILE GLU ASP LEU VAL ASN GLN ARG LEU
SEQRES 4 B 70 GLN SER GLU GLN GLU VAL LEU ASN TYR ILE GLU THR GLN
SEQRES 5 B 70 ARG THR TYR TRP LYS LEU GLU ASN GLN LYS LYS LEU TYR
SEQRES 6 B 70 ARG GLY SER LEU LYS
HELIX 1 1 SER A 69 SER A 82 1 14
HELIX 2 2 PRO A 87 ARG A 98 1 12
HELIX 3 3 SER A 101 LYS A 122 1 22
HELIX 4 4 SER B 69 SER B 82 1 14
HELIX 5 5 PRO B 87 ARG B 98 1 12
HELIX 6 6 SER B 101 LYS B 122 1 22
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 2 2 Bytes