Header list of 2a9h.pdb file
Complete list - 20 20 Bytes
HEADER METAL TRANSPORT, MEMBRANE PROTEIN 11-JUL-05 2A9H
TITLE NMR STRUCTURAL STUDIES OF A POTASSIUM CHANNEL / CHARYBDOTOXIN COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VOLTAGE-GATED POTASSIUM CHANNEL;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: CHARYBDOTOXIN;
COMPND 8 CHAIN: E;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES LIVIDANS;
SOURCE 3 ORGANISM_TAXID: 1916;
SOURCE 4 GENE: KCSA, SKC1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: C41 (DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PIVEX-D2.4D;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES
KEYWDS POTASSIUM CHANNEL, KCSA, MEMBRANE PROTEIN, METAL TRANSPORT
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR L.YU,C.SUN,D.SONG,J.SHEN,N.XU,A.GUNASEKERA,P.J.HAJDUK,E.T.OLEJNICZAK
REVDAT 4 20-OCT-21 2A9H 1 SEQADV
REVDAT 3 25-DEC-19 2A9H 1 REMARK SEQADV SEQRES LINK
REVDAT 2 24-FEB-09 2A9H 1 VERSN
REVDAT 1 10-JAN-06 2A9H 0
JRNL AUTH L.YU,C.SUN,D.SONG,J.SHEN,N.XU,A.GUNASEKERA,P.J.HAJDUK,
JRNL AUTH 2 E.T.OLEJNICZAK
JRNL TITL NUCLEAR MAGNETIC RESONANCE STRUCTURAL STUDIES OF A POTASSIUM
JRNL TITL 2 CHANNEL-CHARYBDOTOXIN COMPLEX.
JRNL REF BIOCHEMISTRY V. 44 15834 2005
JRNL REFN ISSN 0006-2960
JRNL PMID 16313186
JRNL DOI 10.1021/BI051656D
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 2002, CNS 2002
REMARK 3 AUTHORS : BRUNGER (CNS), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2A9H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JUL-05.
REMARK 100 THE DEPOSITION ID IS D_1000033653.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 315
REMARK 210 PH : 7.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM KCSA, 2H AND SELECTIVELY
REMARK 210 13C-METHYL LABELED IN 20 MM
REMARK 210 SODIUM PHOSPHATE (PH 7.5), 5 MM
REMARK 210 KCL, 1 MM DTT, AND 80 MM
REMARK 210 FOSCHOLINE-12, 90% H2O/10% D2O
REMARK 210 OR 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D 13C-EDITED NOESY; 3D-FILTERED
REMARK 210 NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 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 : MOLECULAR SIMULATED ANNEALING /
REMARK 210 DYNAMICS / DOCKING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
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: PENTAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E
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 MET A -22
REMARK 465 SER A -21
REMARK 465 GLY A -20
REMARK 465 SER A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 SER A -12
REMARK 465 SER A -11
REMARK 465 GLY A -10
REMARK 465 ILE A -9
REMARK 465 GLU A -8
REMARK 465 GLY A -7
REMARK 465 ARG A -6
REMARK 465 GLY A -5
REMARK 465 ARG A -4
REMARK 465 LEU A -3
REMARK 465 ILE A -2
REMARK 465 LYS A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 PRO A 2
REMARK 465 PRO A 3
REMARK 465 MET A 4
REMARK 465 LEU A 5
REMARK 465 SER A 6
REMARK 465 GLY A 7
REMARK 465 LEU A 8
REMARK 465 LEU A 9
REMARK 465 ALA A 10
REMARK 465 ARG A 11
REMARK 465 LEU A 12
REMARK 465 VAL A 13
REMARK 465 LYS A 14
REMARK 465 LEU A 15
REMARK 465 LEU A 16
REMARK 465 LEU A 17
REMARK 465 GLY A 18
REMARK 465 ARG A 19
REMARK 465 HIS A 20
REMARK 465 GLY A 21
REMARK 465 SER A 22
REMARK 465 GLU A 120
REMARK 465 ARG A 121
REMARK 465 ARG A 122
REMARK 465 GLY A 123
REMARK 465 HIS A 124
REMARK 465 PHE A 125
REMARK 465 VAL A 126
REMARK 465 ARG A 127
REMARK 465 HIS A 128
REMARK 465 SER A 129
REMARK 465 GLU A 130
REMARK 465 LYS A 131
REMARK 465 ALA A 132
REMARK 465 MET B -22
REMARK 465 SER B -21
REMARK 465 GLY B -20
REMARK 465 SER B -19
REMARK 465 HIS B -18
REMARK 465 HIS B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 SER B -12
REMARK 465 SER B -11
REMARK 465 GLY B -10
REMARK 465 ILE B -9
REMARK 465 GLU B -8
REMARK 465 GLY B -7
REMARK 465 ARG B -6
REMARK 465 GLY B -5
REMARK 465 ARG B -4
REMARK 465 LEU B -3
REMARK 465 ILE B -2
REMARK 465 LYS B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 PRO B 2
REMARK 465 PRO B 3
REMARK 465 MET B 4
REMARK 465 LEU B 5
REMARK 465 SER B 6
REMARK 465 GLY B 7
REMARK 465 LEU B 8
REMARK 465 LEU B 9
REMARK 465 ALA B 10
REMARK 465 ARG B 11
REMARK 465 LEU B 12
REMARK 465 VAL B 13
REMARK 465 LYS B 14
REMARK 465 LEU B 15
REMARK 465 LEU B 16
REMARK 465 LEU B 17
REMARK 465 GLY B 18
REMARK 465 ARG B 19
REMARK 465 HIS B 20
REMARK 465 GLY B 21
REMARK 465 SER B 22
REMARK 465 GLU B 120
REMARK 465 ARG B 121
REMARK 465 ARG B 122
REMARK 465 GLY B 123
REMARK 465 HIS B 124
REMARK 465 PHE B 125
REMARK 465 VAL B 126
REMARK 465 ARG B 127
REMARK 465 HIS B 128
REMARK 465 SER B 129
REMARK 465 GLU B 130
REMARK 465 LYS B 131
REMARK 465 ALA B 132
REMARK 465 MET C -22
REMARK 465 SER C -21
REMARK 465 GLY C -20
REMARK 465 SER C -19
REMARK 465 HIS C -18
REMARK 465 HIS C -17
REMARK 465 HIS C -16
REMARK 465 HIS C -15
REMARK 465 HIS C -14
REMARK 465 HIS C -13
REMARK 465 SER C -12
REMARK 465 SER C -11
REMARK 465 GLY C -10
REMARK 465 ILE C -9
REMARK 465 GLU C -8
REMARK 465 GLY C -7
REMARK 465 ARG C -6
REMARK 465 GLY C -5
REMARK 465 ARG C -4
REMARK 465 LEU C -3
REMARK 465 ILE C -2
REMARK 465 LYS C -1
REMARK 465 HIS C 0
REMARK 465 MET C 1
REMARK 465 PRO C 2
REMARK 465 PRO C 3
REMARK 465 MET C 4
REMARK 465 LEU C 5
REMARK 465 SER C 6
REMARK 465 GLY C 7
REMARK 465 LEU C 8
REMARK 465 LEU C 9
REMARK 465 ALA C 10
REMARK 465 ARG C 11
REMARK 465 LEU C 12
REMARK 465 VAL C 13
REMARK 465 LYS C 14
REMARK 465 LEU C 15
REMARK 465 LEU C 16
REMARK 465 LEU C 17
REMARK 465 GLY C 18
REMARK 465 ARG C 19
REMARK 465 HIS C 20
REMARK 465 GLY C 21
REMARK 465 SER C 22
REMARK 465 GLU C 120
REMARK 465 ARG C 121
REMARK 465 ARG C 122
REMARK 465 GLY C 123
REMARK 465 HIS C 124
REMARK 465 PHE C 125
REMARK 465 VAL C 126
REMARK 465 ARG C 127
REMARK 465 HIS C 128
REMARK 465 SER C 129
REMARK 465 GLU C 130
REMARK 465 LYS C 131
REMARK 465 ALA C 132
REMARK 465 MET D -22
REMARK 465 SER D -21
REMARK 465 GLY D -20
REMARK 465 SER D -19
REMARK 465 HIS D -18
REMARK 465 HIS D -17
REMARK 465 HIS D -16
REMARK 465 HIS D -15
REMARK 465 HIS D -14
REMARK 465 HIS D -13
REMARK 465 SER D -12
REMARK 465 SER D -11
REMARK 465 GLY D -10
REMARK 465 ILE D -9
REMARK 465 GLU D -8
REMARK 465 GLY D -7
REMARK 465 ARG D -6
REMARK 465 GLY D -5
REMARK 465 ARG D -4
REMARK 465 LEU D -3
REMARK 465 ILE D -2
REMARK 465 LYS D -1
REMARK 465 HIS D 0
REMARK 465 MET D 1
REMARK 465 PRO D 2
REMARK 465 PRO D 3
REMARK 465 MET D 4
REMARK 465 LEU D 5
REMARK 465 SER D 6
REMARK 465 GLY D 7
REMARK 465 LEU D 8
REMARK 465 LEU D 9
REMARK 465 ALA D 10
REMARK 465 ARG D 11
REMARK 465 LEU D 12
REMARK 465 VAL D 13
REMARK 465 LYS D 14
REMARK 465 LEU D 15
REMARK 465 LEU D 16
REMARK 465 LEU D 17
REMARK 465 GLY D 18
REMARK 465 ARG D 19
REMARK 465 HIS D 20
REMARK 465 GLY D 21
REMARK 465 SER D 22
REMARK 465 GLU D 120
REMARK 465 ARG D 121
REMARK 465 ARG D 122
REMARK 465 GLY D 123
REMARK 465 HIS D 124
REMARK 465 PHE D 125
REMARK 465 VAL D 126
REMARK 465 ARG D 127
REMARK 465 HIS D 128
REMARK 465 SER D 129
REMARK 465 GLU D 130
REMARK 465 LYS D 131
REMARK 465 ALA D 132
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 LEU A 24 -44.98 -177.23
REMARK 500 PRO A 55 87.31 -69.74
REMARK 500 ALA A 57 -70.53 -73.96
REMARK 500 ALA A 58 31.49 -163.89
REMARK 500 LEU A 59 50.88 -92.98
REMARK 500 VAL A 76 -74.22 -90.54
REMARK 500 VAL A 84 -48.28 -139.31
REMARK 500 ARG A 117 37.27 -165.99
REMARK 500 LEU B 24 -44.97 -177.52
REMARK 500 PRO B 55 103.46 -48.84
REMARK 500 ALA B 58 50.86 -95.74
REMARK 500 VAL B 76 -74.73 -90.06
REMARK 500 ARG B 117 31.05 -163.25
REMARK 500 LEU C 24 -45.09 -161.23
REMARK 500 ALA C 54 150.69 172.12
REMARK 500 VAL C 76 -74.40 -90.01
REMARK 500 ARG C 117 90.71 -166.94
REMARK 500 LEU D 24 -45.10 -169.28
REMARK 500 ALA D 54 152.51 172.58
REMARK 500 PRO D 55 90.19 -51.87
REMARK 500 LEU D 59 -63.36 -130.63
REMARK 500 VAL D 76 -72.99 -89.68
REMARK 500 VAL D 84 -62.56 -127.12
REMARK 500 ARG D 117 62.06 -165.87
REMARK 500 SER E 806 159.85 -48.66
REMARK 500 THR E 808 -48.59 -140.11
REMARK 500 HIS E 821 -76.90 -118.09
REMARK 500 ASN E 822 48.74 171.45
REMARK 500 ARG E 825 104.56 57.97
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2A9H A 1 132 UNP P0A334 KCSA_STRLI 1 132
DBREF 2A9H B 1 132 UNP P0A334 KCSA_STRLI 1 132
DBREF 2A9H C 1 132 UNP P0A334 KCSA_STRLI 1 132
DBREF 2A9H D 1 132 UNP P0A334 KCSA_STRLI 1 132
DBREF 2A9H E 801 837 PDB 2A9H 2A9H 801 837
SEQADV 2A9H MET A -22 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H SER A -21 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H GLY A -20 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H SER A -19 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H HIS A -18 UNP P0A334 EXPRESSION TAG
SEQADV 2A9H HIS A -17 UNP P0A334 EXPRESSION TAG
SEQADV 2A9H HIS A -16 UNP P0A334 EXPRESSION TAG
SEQADV 2A9H HIS A -15 UNP P0A334 EXPRESSION TAG
SEQADV 2A9H HIS A -14 UNP P0A334 EXPRESSION TAG
SEQADV 2A9H HIS A -13 UNP P0A334 EXPRESSION TAG
SEQADV 2A9H SER A -12 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H SER A -11 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H GLY A -10 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H ILE A -9 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H GLU A -8 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H GLY A -7 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H ARG A -6 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H GLY A -5 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H ARG A -4 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H LEU A -3 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H ILE A -2 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H LYS A -1 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H HIS A 0 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H ALA A 58 UNP P0A334 GLN 58 ENGINEERED MUTATION
SEQADV 2A9H SER A 61 UNP P0A334 THR 61 ENGINEERED MUTATION
SEQADV 2A9H ASP A 64 UNP P0A334 ARG 64 ENGINEERED MUTATION
SEQADV 2A9H CYS A 90 UNP P0A334 LEU 90 ENGINEERED MUTATION
SEQADV 2A9H TYR A 103 UNP P0A334 PHE 103 ENGINEERED MUTATION
SEQADV 2A9H PHE A 107 UNP P0A334 THR 107 ENGINEERED MUTATION
SEQADV 2A9H VAL A 110 UNP P0A334 LEU 110 ENGINEERED MUTATION
SEQADV 2A9H MET B -22 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H SER B -21 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H GLY B -20 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H SER B -19 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H HIS B -18 UNP P0A334 EXPRESSION TAG
SEQADV 2A9H HIS B -17 UNP P0A334 EXPRESSION TAG
SEQADV 2A9H HIS B -16 UNP P0A334 EXPRESSION TAG
SEQADV 2A9H HIS B -15 UNP P0A334 EXPRESSION TAG
SEQADV 2A9H HIS B -14 UNP P0A334 EXPRESSION TAG
SEQADV 2A9H HIS B -13 UNP P0A334 EXPRESSION TAG
SEQADV 2A9H SER B -12 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H SER B -11 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H GLY B -10 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H ILE B -9 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H GLU B -8 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H GLY B -7 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H ARG B -6 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H GLY B -5 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H ARG B -4 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H LEU B -3 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H ILE B -2 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H LYS B -1 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H HIS B 0 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H ALA B 58 UNP P0A334 GLN 58 ENGINEERED MUTATION
SEQADV 2A9H SER B 61 UNP P0A334 THR 61 ENGINEERED MUTATION
SEQADV 2A9H ASP B 64 UNP P0A334 ARG 64 ENGINEERED MUTATION
SEQADV 2A9H CYS B 90 UNP P0A334 LEU 90 ENGINEERED MUTATION
SEQADV 2A9H TYR B 103 UNP P0A334 PHE 103 ENGINEERED MUTATION
SEQADV 2A9H PHE B 107 UNP P0A334 THR 107 ENGINEERED MUTATION
SEQADV 2A9H VAL B 110 UNP P0A334 LEU 110 ENGINEERED MUTATION
SEQADV 2A9H MET C -22 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H SER C -21 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H GLY C -20 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H SER C -19 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H HIS C -18 UNP P0A334 EXPRESSION TAG
SEQADV 2A9H HIS C -17 UNP P0A334 EXPRESSION TAG
SEQADV 2A9H HIS C -16 UNP P0A334 EXPRESSION TAG
SEQADV 2A9H HIS C -15 UNP P0A334 EXPRESSION TAG
SEQADV 2A9H HIS C -14 UNP P0A334 EXPRESSION TAG
SEQADV 2A9H HIS C -13 UNP P0A334 EXPRESSION TAG
SEQADV 2A9H SER C -12 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H SER C -11 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H GLY C -10 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H ILE C -9 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H GLU C -8 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H GLY C -7 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H ARG C -6 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H GLY C -5 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H ARG C -4 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H LEU C -3 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H ILE C -2 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H LYS C -1 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H HIS C 0 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H ALA C 58 UNP P0A334 GLN 58 ENGINEERED MUTATION
SEQADV 2A9H SER C 61 UNP P0A334 THR 61 ENGINEERED MUTATION
SEQADV 2A9H ASP C 64 UNP P0A334 ARG 64 ENGINEERED MUTATION
SEQADV 2A9H CYS C 90 UNP P0A334 LEU 90 ENGINEERED MUTATION
SEQADV 2A9H TYR C 103 UNP P0A334 PHE 103 ENGINEERED MUTATION
SEQADV 2A9H PHE C 107 UNP P0A334 THR 107 ENGINEERED MUTATION
SEQADV 2A9H VAL C 110 UNP P0A334 LEU 110 ENGINEERED MUTATION
SEQADV 2A9H MET D -22 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H SER D -21 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H GLY D -20 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H SER D -19 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H HIS D -18 UNP P0A334 EXPRESSION TAG
SEQADV 2A9H HIS D -17 UNP P0A334 EXPRESSION TAG
SEQADV 2A9H HIS D -16 UNP P0A334 EXPRESSION TAG
SEQADV 2A9H HIS D -15 UNP P0A334 EXPRESSION TAG
SEQADV 2A9H HIS D -14 UNP P0A334 EXPRESSION TAG
SEQADV 2A9H HIS D -13 UNP P0A334 EXPRESSION TAG
SEQADV 2A9H SER D -12 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H SER D -11 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H GLY D -10 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H ILE D -9 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H GLU D -8 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H GLY D -7 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H ARG D -6 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H GLY D -5 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H ARG D -4 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H LEU D -3 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H ILE D -2 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H LYS D -1 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H HIS D 0 UNP P0A334 CLONING ARTIFACT
SEQADV 2A9H ALA D 58 UNP P0A334 GLN 58 ENGINEERED MUTATION
SEQADV 2A9H SER D 61 UNP P0A334 THR 61 ENGINEERED MUTATION
SEQADV 2A9H ASP D 64 UNP P0A334 ARG 64 ENGINEERED MUTATION
SEQADV 2A9H CYS D 90 UNP P0A334 LEU 90 ENGINEERED MUTATION
SEQADV 2A9H TYR D 103 UNP P0A334 PHE 103 ENGINEERED MUTATION
SEQADV 2A9H PHE D 107 UNP P0A334 THR 107 ENGINEERED MUTATION
SEQADV 2A9H VAL D 110 UNP P0A334 LEU 110 ENGINEERED MUTATION
SEQRES 1 A 155 MET SER GLY SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 155 ILE GLU GLY ARG GLY ARG LEU ILE LYS HIS MET PRO PRO
SEQRES 3 A 155 MET LEU SER GLY LEU LEU ALA ARG LEU VAL LYS LEU LEU
SEQRES 4 A 155 LEU GLY ARG HIS GLY SER ALA LEU HIS TRP ARG ALA ALA
SEQRES 5 A 155 GLY ALA ALA THR VAL LEU LEU VAL ILE VAL LEU LEU ALA
SEQRES 6 A 155 GLY SER TYR LEU ALA VAL LEU ALA GLU ARG GLY ALA PRO
SEQRES 7 A 155 GLY ALA ALA LEU ILE SER TYR PRO ASP ALA LEU TRP TRP
SEQRES 8 A 155 SER VAL GLU THR ALA THR THR VAL GLY TYR GLY ASP LEU
SEQRES 9 A 155 TYR PRO VAL THR LEU TRP GLY ARG CYS VAL ALA VAL VAL
SEQRES 10 A 155 VAL MET VAL ALA GLY ILE THR SER TYR GLY LEU VAL PHE
SEQRES 11 A 155 ALA ALA VAL ALA THR TRP PHE VAL GLY ARG GLU GLN GLU
SEQRES 12 A 155 ARG ARG GLY HIS PHE VAL ARG HIS SER GLU LYS ALA
SEQRES 1 B 155 MET SER GLY SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 155 ILE GLU GLY ARG GLY ARG LEU ILE LYS HIS MET PRO PRO
SEQRES 3 B 155 MET LEU SER GLY LEU LEU ALA ARG LEU VAL LYS LEU LEU
SEQRES 4 B 155 LEU GLY ARG HIS GLY SER ALA LEU HIS TRP ARG ALA ALA
SEQRES 5 B 155 GLY ALA ALA THR VAL LEU LEU VAL ILE VAL LEU LEU ALA
SEQRES 6 B 155 GLY SER TYR LEU ALA VAL LEU ALA GLU ARG GLY ALA PRO
SEQRES 7 B 155 GLY ALA ALA LEU ILE SER TYR PRO ASP ALA LEU TRP TRP
SEQRES 8 B 155 SER VAL GLU THR ALA THR THR VAL GLY TYR GLY ASP LEU
SEQRES 9 B 155 TYR PRO VAL THR LEU TRP GLY ARG CYS VAL ALA VAL VAL
SEQRES 10 B 155 VAL MET VAL ALA GLY ILE THR SER TYR GLY LEU VAL PHE
SEQRES 11 B 155 ALA ALA VAL ALA THR TRP PHE VAL GLY ARG GLU GLN GLU
SEQRES 12 B 155 ARG ARG GLY HIS PHE VAL ARG HIS SER GLU LYS ALA
SEQRES 1 C 155 MET SER GLY SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 155 ILE GLU GLY ARG GLY ARG LEU ILE LYS HIS MET PRO PRO
SEQRES 3 C 155 MET LEU SER GLY LEU LEU ALA ARG LEU VAL LYS LEU LEU
SEQRES 4 C 155 LEU GLY ARG HIS GLY SER ALA LEU HIS TRP ARG ALA ALA
SEQRES 5 C 155 GLY ALA ALA THR VAL LEU LEU VAL ILE VAL LEU LEU ALA
SEQRES 6 C 155 GLY SER TYR LEU ALA VAL LEU ALA GLU ARG GLY ALA PRO
SEQRES 7 C 155 GLY ALA ALA LEU ILE SER TYR PRO ASP ALA LEU TRP TRP
SEQRES 8 C 155 SER VAL GLU THR ALA THR THR VAL GLY TYR GLY ASP LEU
SEQRES 9 C 155 TYR PRO VAL THR LEU TRP GLY ARG CYS VAL ALA VAL VAL
SEQRES 10 C 155 VAL MET VAL ALA GLY ILE THR SER TYR GLY LEU VAL PHE
SEQRES 11 C 155 ALA ALA VAL ALA THR TRP PHE VAL GLY ARG GLU GLN GLU
SEQRES 12 C 155 ARG ARG GLY HIS PHE VAL ARG HIS SER GLU LYS ALA
SEQRES 1 D 155 MET SER GLY SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 155 ILE GLU GLY ARG GLY ARG LEU ILE LYS HIS MET PRO PRO
SEQRES 3 D 155 MET LEU SER GLY LEU LEU ALA ARG LEU VAL LYS LEU LEU
SEQRES 4 D 155 LEU GLY ARG HIS GLY SER ALA LEU HIS TRP ARG ALA ALA
SEQRES 5 D 155 GLY ALA ALA THR VAL LEU LEU VAL ILE VAL LEU LEU ALA
SEQRES 6 D 155 GLY SER TYR LEU ALA VAL LEU ALA GLU ARG GLY ALA PRO
SEQRES 7 D 155 GLY ALA ALA LEU ILE SER TYR PRO ASP ALA LEU TRP TRP
SEQRES 8 D 155 SER VAL GLU THR ALA THR THR VAL GLY TYR GLY ASP LEU
SEQRES 9 D 155 TYR PRO VAL THR LEU TRP GLY ARG CYS VAL ALA VAL VAL
SEQRES 10 D 155 VAL MET VAL ALA GLY ILE THR SER TYR GLY LEU VAL PHE
SEQRES 11 D 155 ALA ALA VAL ALA THR TRP PHE VAL GLY ARG GLU GLN GLU
SEQRES 12 D 155 ARG ARG GLY HIS PHE VAL ARG HIS SER GLU LYS ALA
SEQRES 1 E 37 PCA PHE THR ASN VAL SER CYS THR THR SER LYS GLU CYS
SEQRES 2 E 37 TRP SER VAL CYS GLN ARG LEU HIS ASN THR SER ARG GLY
SEQRES 3 E 37 LYS CYS MET ASN LYS LYS CYS ARG CYS TYR SER
MODRES 2A9H PCA E 801 GLN PYROGLUTAMIC ACID
HET PCA E 801 14
HETNAM PCA PYROGLUTAMIC ACID
FORMUL 5 PCA C5 H7 N O3
HELIX 1 1 LEU A 24 ARG A 52 1 29
HELIX 2 2 SER A 61 THR A 74 1 14
HELIX 3 3 THR A 85 GLY A 116 1 32
HELIX 4 4 LEU B 24 ARG B 52 1 29
HELIX 5 5 SER B 61 THR B 74 1 14
HELIX 6 6 THR B 85 GLY B 116 1 32
HELIX 7 7 LEU C 24 ARG C 52 1 29
HELIX 8 8 SER C 61 THR C 74 1 14
HELIX 9 9 THR C 85 GLY C 116 1 32
HELIX 10 10 LEU D 24 ARG D 52 1 29
HELIX 11 11 SER D 61 THR D 74 1 14
HELIX 12 12 THR D 85 GLY D 116 1 32
HELIX 13 13 THR E 809 HIS E 821 1 13
SSBOND 1 CYS E 807 CYS E 828 1555 1555 2.03
SSBOND 2 CYS E 813 CYS E 833 1555 1555 2.03
SSBOND 3 CYS E 817 CYS E 835 1555 1555 2.03
LINK C PCA E 801 N PHE E 802 1555 1555 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 - 20 20 Bytes