Header list of 2hgm.pdb file
Complete list - r 9 2 Bytes
HEADER RNA BINDING PROTEIN 27-JUN-06 2HGM
TITLE NMR STRUCTURE OF THE SECOND QRRM DOMAIN OF HUMAN HNRNP F
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN F;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: QUASI RNA RECOGNITION MOTIF 2 (QRRM2);
COMPND 5 SYNONYM: HNRPF PROTEIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: HNRPF;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODON PLUS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28B(+)
KEYWDS RNA RECOGNITION MOTIF, G-TRACT, G-QUADRUPLEX, ALTERNATIVE SPLICING,
KEYWDS 2 RNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR C.DOMINGUEZ,F.H.-T.ALLAIN
REVDAT 4 09-MAR-22 2HGM 1 REMARK SEQADV
REVDAT 3 24-FEB-09 2HGM 1 VERSN
REVDAT 2 08-AUG-06 2HGM 1 JRNL
REVDAT 1 11-JUL-06 2HGM 0
JRNL AUTH C.DOMINGUEZ,F.H.ALLAIN
JRNL TITL NMR STRUCTURE OF THE THREE QUASI RNA RECOGNITION MOTIFS
JRNL TITL 2 (QRRMS) OF HUMAN HNRNP F AND INTERACTION STUDIES WITH BCL-X
JRNL TITL 3 G-TRACT RNA: A NOVEL MODE OF RNA RECOGNITION.
JRNL REF NUCLEIC ACIDS RES. V. 34 3634 2006
JRNL REFN ISSN 0305-1048
JRNL PMID 16885237
JRNL DOI 10.1093/NAR/GKL488
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : ATNOSCANDID 1.1, AMBER 7.0
REMARK 3 AUTHORS : HERMANN (ATNOSCANDID), CASE (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2HGM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JUN-06.
REMARK 100 THE DEPOSITION ID IS D_1000038325.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 313
REMARK 210 PH : 6.2
REMARK 210 IONIC STRENGTH : 25MM NAH2PO4, 50 MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.3 MM HNRNP F QRRM1 U-15N, 25MM
REMARK 210 NAH2PO4 (PH 6.2), 50MM NACL, 10
REMARK 210 MM BETA-MERCAPTOETHANOL; 0.3 MM
REMARK 210 HNRNP F QRRM1 U-15N,13C, 25MM
REMARK 210 NAH2PO4 (PH 6.2), 50MM NACL, 10
REMARK 210 MM BETA-MERCAPTOETHANOL; 0.3 MM
REMARK 210 HNRNP F QRRM1 U-15N, 25MM
REMARK 210 NAH2PO4 (PH 6.2), 50MM NACL, 10
REMARK 210 MM BETA-MERCAPTOETHANOL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 4D_13C-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 900 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CYANA 2.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 14
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 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 MODELS 1-15
REMARK 465 RES C SSSEQI
REMARK 465 MET A 69
REMARK 465 GLY A 70
REMARK 465 SER A 71
REMARK 465 SER A 72
REMARK 465 HIS A 73
REMARK 465 HIS A 74
REMARK 465 HIS A 75
REMARK 465 HIS A 76
REMARK 465 HIS A 77
REMARK 465 HIS A 78
REMARK 465 SER A 79
REMARK 465 SER A 80
REMARK 465 GLY A 81
REMARK 465 LEU A 82
REMARK 465 VAL A 83
REMARK 465 PRO A 84
REMARK 465 ARG A 85
REMARK 465 GLY A 86
REMARK 465 SER A 87
REMARK 465 HIS A 88
REMARK 465 MET A 89
REMARK 465 ALA A 90
REMARK 465 SER A 91
REMARK 465 MET A 92
REMARK 465 THR A 93
REMARK 465 GLY A 94
REMARK 465 GLY A 95
REMARK 465 GLN A 96
REMARK 465 GLN A 97
REMARK 465 MET A 98
REMARK 465 GLY A 99
REMARK 465 ARG A 100
REMARK 465 GLY A 101
REMARK 465 SER A 102
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 HG SER A 107 OD1 ASP A 110 1.60
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 ARG A 114 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 1 ARG A 116 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 1 ARG A 192 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 2 ARG A 179 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 2 ARG A 192 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 3 ARG A 179 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 3 TYR A 194 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 5 VAL A 128 CA - CB - CG1 ANGL. DEV. = 9.9 DEGREES
REMARK 500 6 ARG A 114 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 6 ARG A 116 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 6 VAL A 128 CA - CB - CG1 ANGL. DEV. = 9.8 DEGREES
REMARK 500 6 ARG A 179 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 6 ARG A 192 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 7 VAL A 128 CA - CB - CG1 ANGL. DEV. = 9.2 DEGREES
REMARK 500 7 ARG A 175 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 7 VAL A 191 CA - CB - CG1 ANGL. DEV. = 12.8 DEGREES
REMARK 500 8 ARG A 114 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 8 ARG A 116 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 8 VAL A 128 CA - CB - CG1 ANGL. DEV. = 9.3 DEGREES
REMARK 500 9 VAL A 128 CA - CB - CG1 ANGL. DEV. = 9.4 DEGREES
REMARK 500 10 VAL A 157 CA - CB - CG1 ANGL. DEV. = 9.1 DEGREES
REMARK 500 10 ARG A 192 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 11 VAL A 128 CA - CB - CG1 ANGL. DEV. = 10.0 DEGREES
REMARK 500 11 VAL A 128 CA - CB - CG2 ANGL. DEV. = 9.1 DEGREES
REMARK 500 11 ARG A 175 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 12 VAL A 128 CA - CB - CG1 ANGL. DEV. = 10.4 DEGREES
REMARK 500 13 VAL A 128 CA - CB - CG1 ANGL. DEV. = 10.1 DEGREES
REMARK 500 14 VAL A 128 CA - CB - CG1 ANGL. DEV. = 10.0 DEGREES
REMARK 500 14 VAL A 128 CA - CB - CG2 ANGL. DEV. = 9.2 DEGREES
REMARK 500 15 VAL A 128 CA - CB - CG1 ANGL. DEV. = 9.1 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 SER A 104 -20.32 42.59
REMARK 500 1 ALA A 105 -30.09 -160.20
REMARK 500 1 SER A 107 -47.47 -147.25
REMARK 500 1 ALA A 108 -41.93 -175.21
REMARK 500 1 ASP A 110 36.13 -70.83
REMARK 500 1 ARG A 116 77.22 -152.66
REMARK 500 1 PRO A 147 -1.98 -57.37
REMARK 500 1 ILE A 151 -118.95 -143.70
REMARK 500 1 THR A 152 73.32 -172.76
REMARK 500 1 HIS A 172 -47.58 60.58
REMARK 500 1 LYS A 173 -66.76 -145.10
REMARK 500 1 GLU A 174 -142.30 36.82
REMARK 500 1 TYR A 180 14.13 -146.84
REMARK 500 1 ILE A 181 107.08 42.96
REMARK 500 1 GLN A 188 -10.62 -31.62
REMARK 500 2 SER A 104 -29.21 58.45
REMARK 500 2 ALA A 105 50.35 -154.08
REMARK 500 2 SER A 107 70.53 -155.24
REMARK 500 2 ALA A 108 -44.45 -147.46
REMARK 500 2 ASN A 109 -46.90 -171.73
REMARK 500 2 ASP A 110 45.22 -71.08
REMARK 500 2 ARG A 116 79.55 -155.58
REMARK 500 2 PRO A 144 -72.68 -87.07
REMARK 500 2 PRO A 147 -3.28 -57.46
REMARK 500 2 ILE A 151 -117.82 -143.47
REMARK 500 2 THR A 152 76.04 -175.70
REMARK 500 2 LYS A 171 35.70 -72.43
REMARK 500 2 GLU A 174 -170.44 -66.96
REMARK 500 2 GLN A 188 4.12 -29.33
REMARK 500 2 ARG A 192 36.62 -87.11
REMARK 500 2 SER A 193 30.50 -66.60
REMARK 500 3 SER A 104 -165.15 -67.07
REMARK 500 3 ALA A 105 -33.10 64.31
REMARK 500 3 SER A 107 -53.52 -146.39
REMARK 500 3 ALA A 108 -72.82 -162.34
REMARK 500 3 ASP A 110 37.87 -82.27
REMARK 500 3 ARG A 116 89.86 -150.67
REMARK 500 3 PRO A 144 -92.22 -79.80
REMARK 500 3 PRO A 147 0.88 -55.08
REMARK 500 3 ILE A 151 -98.40 -138.43
REMARK 500 3 THR A 152 78.21 164.33
REMARK 500 3 HIS A 172 -46.42 45.69
REMARK 500 3 GLN A 188 2.76 -32.86
REMARK 500 4 SER A 104 102.64 -48.87
REMARK 500 4 ALA A 105 19.44 -150.63
REMARK 500 4 SER A 107 106.20 -165.68
REMARK 500 4 ALA A 108 -9.85 -143.46
REMARK 500 4 PRO A 144 -86.87 -87.86
REMARK 500 4 PRO A 147 -6.40 -56.07
REMARK 500 4 ILE A 151 -100.85 -140.74
REMARK 500
REMARK 500 THIS ENTRY HAS 204 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 ASP A 106 SER A 107 1 140.56
REMARK 500 GLY A 153 GLU A 154 1 148.74
REMARK 500 ARG A 179 TYR A 180 1 -124.33
REMARK 500 TYR A 180 ILE A 181 1 134.98
REMARK 500 GLU A 189 GLU A 190 1 149.74
REMARK 500 GLY A 153 GLU A 154 2 148.50
REMARK 500 ARG A 179 TYR A 180 2 -119.30
REMARK 500 TYR A 180 ILE A 181 2 -139.00
REMARK 500 ARG A 192 SER A 193 2 -148.04
REMARK 500 GLY A 153 GLU A 154 3 145.32
REMARK 500 ARG A 179 TYR A 180 3 -149.76
REMARK 500 TYR A 180 ILE A 181 3 -148.18
REMARK 500 LEU A 115 ARG A 116 4 141.01
REMARK 500 ARG A 179 TYR A 180 4 -126.12
REMARK 500 TYR A 180 ILE A 181 4 -141.69
REMARK 500 ARG A 179 TYR A 180 5 -113.68
REMARK 500 TYR A 180 ILE A 181 5 -141.24
REMARK 500 GLY A 153 GLU A 154 6 142.02
REMARK 500 ARG A 179 TYR A 180 6 -132.71
REMARK 500 TYR A 180 ILE A 181 6 -139.75
REMARK 500 ARG A 179 TYR A 180 7 -126.10
REMARK 500 TYR A 180 ILE A 181 7 -148.41
REMARK 500 VAL A 191 ARG A 192 7 -138.46
REMARK 500 GLY A 153 GLU A 154 8 149.26
REMARK 500 ARG A 179 TYR A 180 8 -128.32
REMARK 500 TYR A 180 ILE A 181 8 -146.73
REMARK 500 LEU A 115 ARG A 116 9 140.84
REMARK 500 GLY A 117 LEU A 118 9 -141.14
REMARK 500 ARG A 179 TYR A 180 9 -140.28
REMARK 500 TYR A 180 ILE A 181 9 -142.60
REMARK 500 GLU A 190 VAL A 191 9 -149.75
REMARK 500 GLY A 133 LEU A 134 10 -149.17
REMARK 500 ARG A 179 TYR A 180 10 -119.88
REMARK 500 TYR A 180 ILE A 181 10 -138.38
REMARK 500 ARG A 179 TYR A 180 11 -118.95
REMARK 500 TYR A 180 ILE A 181 11 -144.00
REMARK 500 ARG A 179 TYR A 180 12 -144.19
REMARK 500 TYR A 180 ILE A 181 12 -149.26
REMARK 500 LEU A 115 ARG A 116 13 146.95
REMARK 500 ARG A 179 TYR A 180 13 -143.33
REMARK 500 TYR A 180 ILE A 181 13 -147.75
REMARK 500 ALA A 105 ASP A 106 14 -147.45
REMARK 500 ARG A 179 TYR A 180 14 -126.25
REMARK 500 TYR A 180 ILE A 181 14 -139.25
REMARK 500 LEU A 115 ARG A 116 15 148.56
REMARK 500 GLY A 153 GLU A 154 15 142.71
REMARK 500 ARG A 179 TYR A 180 15 -135.63
REMARK 500 TYR A 180 ILE A 181 15 -139.76
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 2 ARG A 175 0.08 SIDE CHAIN
REMARK 500 2 ARG A 192 0.08 SIDE CHAIN
REMARK 500 5 ARG A 192 0.08 SIDE CHAIN
REMARK 500 7 ARG A 192 0.20 SIDE CHAIN
REMARK 500 8 ARG A 175 0.10 SIDE CHAIN
REMARK 500 12 ARG A 179 0.08 SIDE CHAIN
REMARK 500 15 ARG A 175 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2HGN RELATED DB: PDB
REMARK 900 RELATED ID: 2HGL RELATED DB: PDB
DBREF 2HGM A 103 194 UNP Q5T0N2 Q5T0N2_HUMAN 103 194
SEQADV 2HGM MET A 69 UNP Q5T0N2 CLONING ARTIFACT
SEQADV 2HGM GLY A 70 UNP Q5T0N2 CLONING ARTIFACT
SEQADV 2HGM SER A 71 UNP Q5T0N2 CLONING ARTIFACT
SEQADV 2HGM SER A 72 UNP Q5T0N2 CLONING ARTIFACT
SEQADV 2HGM HIS A 73 UNP Q5T0N2 EXPRESSION TAG
SEQADV 2HGM HIS A 74 UNP Q5T0N2 EXPRESSION TAG
SEQADV 2HGM HIS A 75 UNP Q5T0N2 EXPRESSION TAG
SEQADV 2HGM HIS A 76 UNP Q5T0N2 EXPRESSION TAG
SEQADV 2HGM HIS A 77 UNP Q5T0N2 EXPRESSION TAG
SEQADV 2HGM HIS A 78 UNP Q5T0N2 EXPRESSION TAG
SEQADV 2HGM SER A 79 UNP Q5T0N2 CLONING ARTIFACT
SEQADV 2HGM SER A 80 UNP Q5T0N2 CLONING ARTIFACT
SEQADV 2HGM GLY A 81 UNP Q5T0N2 CLONING ARTIFACT
SEQADV 2HGM LEU A 82 UNP Q5T0N2 CLONING ARTIFACT
SEQADV 2HGM VAL A 83 UNP Q5T0N2 CLONING ARTIFACT
SEQADV 2HGM PRO A 84 UNP Q5T0N2 CLONING ARTIFACT
SEQADV 2HGM ARG A 85 UNP Q5T0N2 CLONING ARTIFACT
SEQADV 2HGM GLY A 86 UNP Q5T0N2 CLONING ARTIFACT
SEQADV 2HGM SER A 87 UNP Q5T0N2 CLONING ARTIFACT
SEQADV 2HGM HIS A 88 UNP Q5T0N2 CLONING ARTIFACT
SEQADV 2HGM MET A 89 UNP Q5T0N2 CLONING ARTIFACT
SEQADV 2HGM ALA A 90 UNP Q5T0N2 CLONING ARTIFACT
SEQADV 2HGM SER A 91 UNP Q5T0N2 CLONING ARTIFACT
SEQADV 2HGM MET A 92 UNP Q5T0N2 CLONING ARTIFACT
SEQADV 2HGM THR A 93 UNP Q5T0N2 CLONING ARTIFACT
SEQADV 2HGM GLY A 94 UNP Q5T0N2 CLONING ARTIFACT
SEQADV 2HGM GLY A 95 UNP Q5T0N2 CLONING ARTIFACT
SEQADV 2HGM GLN A 96 UNP Q5T0N2 CLONING ARTIFACT
SEQADV 2HGM GLN A 97 UNP Q5T0N2 CLONING ARTIFACT
SEQADV 2HGM MET A 98 UNP Q5T0N2 CLONING ARTIFACT
SEQADV 2HGM GLY A 99 UNP Q5T0N2 CLONING ARTIFACT
SEQADV 2HGM ARG A 100 UNP Q5T0N2 CLONING ARTIFACT
SEQADV 2HGM GLY A 101 UNP Q5T0N2 CLONING ARTIFACT
SEQADV 2HGM SER A 102 UNP Q5T0N2 CLONING ARTIFACT
SEQRES 1 A 126 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 126 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY
SEQRES 3 A 126 GLY GLN GLN MET GLY ARG GLY SER ASN SER ALA ASP SER
SEQRES 4 A 126 ALA ASN ASP GLY PHE VAL ARG LEU ARG GLY LEU PRO PHE
SEQRES 5 A 126 GLY CYS THR LYS GLU GLU ILE VAL GLN PHE PHE SER GLY
SEQRES 6 A 126 LEU GLU ILE VAL PRO ASN GLY ILE THR LEU PRO VAL ASP
SEQRES 7 A 126 PRO GLU GLY LYS ILE THR GLY GLU ALA PHE VAL GLN PHE
SEQRES 8 A 126 ALA SER GLN GLU LEU ALA GLU LYS ALA LEU GLY LYS HIS
SEQRES 9 A 126 LYS GLU ARG ILE GLY HIS ARG TYR ILE GLU VAL PHE LYS
SEQRES 10 A 126 SER SER GLN GLU GLU VAL ARG SER TYR
HELIX 1 1 THR A 123 PHE A 131 1 9
HELIX 2 2 GLU A 163 GLY A 170 1 8
HELIX 3 3 SER A 187 ARG A 192 1 6
SHEET 1 A 4 ILE A 136 THR A 142 0
SHEET 2 A 4 GLU A 154 PHE A 159 -1 O PHE A 156 N THR A 142
SHEET 3 A 4 PHE A 112 ARG A 116 -1 N LEU A 115 O ALA A 155
SHEET 4 A 4 PHE A 184 SER A 186 -1 O PHE A 184 N ARG A 114
CISPEP 1 ASN A 103 SER A 104 3 -3.57
CISPEP 2 SER A 104 ALA A 105 4 -5.81
CISPEP 3 SER A 107 ALA A 108 4 -6.67
CISPEP 4 SER A 104 ALA A 105 6 -3.98
CISPEP 5 ALA A 108 ASN A 109 6 -8.74
CISPEP 6 SER A 107 ALA A 108 13 1.84
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 9 2 Bytes