Header list of 3nla.pdb file
Complete list - r 16 2 Bytes
HEADER ANTIFREEZE 24-FEB-98 3NLA
TITLE NMR STRUCTURE OF THE N-TERMINAL DOMAIN WITH A LINKER PORTION OF
TITLE 2 ANTARCTIC EEL POUT ANTIFREEZE PROTEIN RD3, 40 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANTIFREEZE PROTEIN RD3 TYPE III;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN WITH A LINKER PORTION;
COMPND 5 SYNONYM: RD3-NL;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LYCODICHTHYS DEARBORNI;
SOURCE 3 ORGANISM_COMMON: ANTARCTIC EEL POUT;
SOURCE 4 ORGANISM_TAXID: 8201;
SOURCE 5 VARIANT: RD3;
SOURCE 6 ORGAN: BLOOD;
SOURCE 7 TISSUE: BLOOD PLASMA;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: JM105;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PKK223-3UC
KEYWDS ANTIFREEZE PROTEIN, THERMAL HYSTERESIS PROTEIN, ICE BINDING PROTEIN,
KEYWDS 2 ANTIFREEZE
EXPDTA SOLUTION NMR
NUMMDL 40
AUTHOR K.MIURA,S.OHGIYA,T.HOSHINO,N.NEMOTO,K.HIKICHI,S.TSUDA
REVDAT 3 16-MAR-22 3NLA 1 REMARK
REVDAT 2 24-FEB-09 3NLA 1 VERSN
REVDAT 1 23-FEB-99 3NLA 0
JRNL AUTH Z.JIA,C.I.DELUCA,H.CHAO,P.L.DAVIES
JRNL TITL STRUCTURAL BASIS FOR THE BINDING OF A GLOBULAR ANTIFREEZE
JRNL TITL 2 PROTEIN TO ICE.
JRNL REF NATURE V. 384 285 1996
JRNL REFN ISSN 0028-0836
JRNL PMID 8918883
JRNL DOI 10.1038/384285A0
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH Z.JIA,C.I.DELUCA,H.CHAO,P.L.DAVIES
REMARK 1 TITL STRUCTURAL BASIS FOR THE BINDING OF A GLOBULAR ANTIFREEZE
REMARK 1 TITL 2 PROTEIN TO ICE
REMARK 1 REF NATURE V. 384 285 1996
REMARK 1 REFN ISSN 0028-0836
REMARK 1 REFERENCE 2
REMARK 1 AUTH F.D.SONNICHSEN,C.I.DELUCA,P.L.DAVIES,B.D.SYKES
REMARK 1 TITL REFINED SOLUTION STRUCTURE OF TYPE III ANTIFREEZE PROTEIN:
REMARK 1 TITL 2 HYDROPHOBIC GROUPS MAY BE INVOLVED IN THE ENERGETICS OF THE
REMARK 1 TITL 3 PROTEIN-ICE INTERACTION
REMARK 1 REF STRUCTURE V. 4 1325 1996
REMARK 1 REFN ISSN 0969-2126
REMARK 1 REFERENCE 3
REMARK 1 AUTH X.WANG,A.L.DEVRIES,C.H.CHENG
REMARK 1 TITL ANTIFREEZE PEPTIDE HETEROGENEITY IN AN ANTARCTIC EEL POUT
REMARK 1 TITL 2 INCLUDES AN UNUSUALLY LARGE MAJOR VARIANT COMPRISED OF TWO 7
REMARK 1 TITL 3 KDA TYPE III AFPS LINKED IN TANDEM
REMARK 1 REF BIOCHIM.BIOPHYS.ACTA V.1247 163 1995
REMARK 1 REFN ISSN 0006-3002
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE.
REMARK 4
REMARK 4 3NLA COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000179064.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 277
REMARK 210 PH : 6.7
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQFCOSY; TOCSY; NOESY; 15N-HSQC;
REMARK 210 15N_TOCSYHSQC; 15N-NOESYHSQC;
REMARK 210 15N-HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY; JNM-A
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; JEOL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.851
REMARK 210 METHOD USED : SA
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 40
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING DOUBLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY ON 15N-LABELED RD3-NL
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 1-40
REMARK 465 RES C SSSEQI
REMARK 465 MET A 0
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 H SER A 4 O GLU A 25 1.49
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 ALA A 7 104.52 -42.62
REMARK 500 1 ASN A 8 -70.85 -75.69
REMARK 500 1 PRO A 12 -158.37 -71.78
REMARK 500 1 ASN A 14 20.31 49.41
REMARK 500 1 THR A 18 -157.85 -130.51
REMARK 500 1 PRO A 29 -165.18 -75.87
REMARK 500 1 PRO A 33 -161.50 -73.03
REMARK 500 1 VAL A 41 104.11 -42.88
REMARK 500 1 PRO A 50 -169.54 -72.72
REMARK 500 1 LYS A 61 -71.63 -69.51
REMARK 500 1 GLU A 64 -81.49 -75.51
REMARK 500 1 SER A 69 -60.49 -175.83
REMARK 500 2 PRO A 12 -96.45 -72.19
REMARK 500 2 GLU A 36 33.46 -92.39
REMARK 500 2 PRO A 50 -163.14 -72.72
REMARK 500 2 LYS A 61 -92.74 -64.99
REMARK 500 2 TYR A 63 157.99 -44.92
REMARK 500 2 GLU A 64 -80.35 -80.79
REMARK 500 2 ASP A 65 33.12 -98.36
REMARK 500 2 SER A 69 -57.68 172.99
REMARK 500 3 PRO A 12 -159.23 -72.89
REMARK 500 3 ASN A 14 19.92 59.25
REMARK 500 3 VAL A 26 39.41 -92.15
REMARK 500 3 LEU A 51 169.11 -44.25
REMARK 500 3 MET A 59 49.02 -94.52
REMARK 500 3 GLU A 64 -160.87 -64.61
REMARK 500 3 ASP A 65 84.56 -61.91
REMARK 500 3 THR A 68 -104.22 -100.46
REMARK 500 3 SER A 69 -66.05 -96.22
REMARK 500 4 ASN A 8 -80.07 -73.58
REMARK 500 4 VAL A 26 79.81 -68.87
REMARK 500 4 ALA A 34 26.41 45.93
REMARK 500 4 PRO A 50 -165.02 -73.15
REMARK 500 4 LYS A 61 -84.36 -60.08
REMARK 500 4 TYR A 63 167.81 -46.13
REMARK 500 4 GLU A 64 -86.14 -99.41
REMARK 500 4 THR A 68 -91.27 -73.36
REMARK 500 5 ASN A 8 -73.13 -82.46
REMARK 500 5 PRO A 12 -95.08 -73.69
REMARK 500 5 ASN A 14 89.33 42.26
REMARK 500 5 PRO A 33 -168.48 -73.12
REMARK 500 5 GLU A 36 47.89 -104.89
REMARK 500 5 ASN A 46 42.16 -109.95
REMARK 500 5 LEU A 51 151.11 67.82
REMARK 500 5 MET A 59 57.56 -99.52
REMARK 500 5 LYS A 61 -83.95 -64.53
REMARK 500 5 TYR A 63 171.70 -45.43
REMARK 500 5 GLU A 64 -155.48 -98.43
REMARK 500 5 ASP A 65 79.19 -59.90
REMARK 500 5 THR A 68 -97.83 -86.30
REMARK 500
REMARK 500 THIS ENTRY HAS 377 RAMACHANDRAN OUTLIERS.
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 ARG A 47 0.25 SIDE CHAIN
REMARK 500 2 ARG A 47 0.28 SIDE CHAIN
REMARK 500 3 ARG A 47 0.24 SIDE CHAIN
REMARK 500 4 ARG A 47 0.16 SIDE CHAIN
REMARK 500 5 ARG A 47 0.14 SIDE CHAIN
REMARK 500 6 ARG A 47 0.31 SIDE CHAIN
REMARK 500 7 ARG A 47 0.17 SIDE CHAIN
REMARK 500 8 ARG A 47 0.31 SIDE CHAIN
REMARK 500 10 ARG A 47 0.32 SIDE CHAIN
REMARK 500 12 ARG A 47 0.22 SIDE CHAIN
REMARK 500 14 ARG A 47 0.32 SIDE CHAIN
REMARK 500 15 ARG A 47 0.23 SIDE CHAIN
REMARK 500 16 ARG A 47 0.26 SIDE CHAIN
REMARK 500 18 ARG A 47 0.28 SIDE CHAIN
REMARK 500 19 ARG A 47 0.32 SIDE CHAIN
REMARK 500 20 ARG A 47 0.24 SIDE CHAIN
REMARK 500 21 ARG A 47 0.28 SIDE CHAIN
REMARK 500 22 ARG A 47 0.09 SIDE CHAIN
REMARK 500 23 ARG A 47 0.27 SIDE CHAIN
REMARK 500 24 ARG A 47 0.30 SIDE CHAIN
REMARK 500 25 ARG A 47 0.29 SIDE CHAIN
REMARK 500 26 ARG A 47 0.18 SIDE CHAIN
REMARK 500 27 ARG A 47 0.24 SIDE CHAIN
REMARK 500 28 ARG A 47 0.31 SIDE CHAIN
REMARK 500 29 ARG A 47 0.25 SIDE CHAIN
REMARK 500 30 ARG A 47 0.31 SIDE CHAIN
REMARK 500 31 ARG A 47 0.13 SIDE CHAIN
REMARK 500 32 ARG A 47 0.27 SIDE CHAIN
REMARK 500 33 ARG A 47 0.32 SIDE CHAIN
REMARK 500 34 ARG A 47 0.22 SIDE CHAIN
REMARK 500 35 ARG A 47 0.32 SIDE CHAIN
REMARK 500 36 ARG A 47 0.26 SIDE CHAIN
REMARK 500 37 ARG A 47 0.11 SIDE CHAIN
REMARK 500 38 ARG A 47 0.23 SIDE CHAIN
REMARK 500 39 ARG A 47 0.31 SIDE CHAIN
REMARK 500 40 ARG A 47 0.28 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: 1
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ICE BINDING SITE.
DBREF 3NLA A 1 73 UNP P35753 ANP3_RHIDE 1 73
SEQRES 1 A 74 MET ASN LYS ALA SER VAL VAL ALA ASN GLN LEU ILE PRO
SEQRES 2 A 74 ILE ASN THR ALA LEU THR LEU ILE MET MET LYS ALA GLU
SEQRES 3 A 74 VAL VAL THR PRO MET GLY ILE PRO ALA GLU GLU ILE PRO
SEQRES 4 A 74 ASN LEU VAL GLY MET GLN VAL ASN ARG ALA VAL PRO LEU
SEQRES 5 A 74 GLY THR THR LEU MET PRO ASP MET VAL LYS ASN TYR GLU
SEQRES 6 A 74 ASP GLY THR THR SER PRO GLY LEU LYS
HELIX 1 1 ILE A 37 LEU A 40 1 4
SHEET 1 A 3 ALA A 24 GLU A 25 0
SHEET 2 A 3 SER A 4 ALA A 7 -1 N SER A 4 O GLU A 25
SHEET 3 A 3 THR A 53 THR A 54 -1 N THR A 53 O ALA A 7
CISPEP 1 THR A 28 PRO A 29 1 -0.15
CISPEP 2 THR A 28 PRO A 29 2 -0.05
CISPEP 3 THR A 28 PRO A 29 3 -0.15
CISPEP 4 THR A 28 PRO A 29 4 -0.13
CISPEP 5 THR A 28 PRO A 29 5 -0.22
CISPEP 6 THR A 28 PRO A 29 6 -0.29
CISPEP 7 THR A 28 PRO A 29 7 -0.30
CISPEP 8 THR A 28 PRO A 29 8 -0.05
CISPEP 9 THR A 28 PRO A 29 9 -0.12
CISPEP 10 THR A 28 PRO A 29 10 -0.23
CISPEP 11 THR A 28 PRO A 29 11 -0.26
CISPEP 12 THR A 28 PRO A 29 12 -0.37
CISPEP 13 THR A 28 PRO A 29 13 -0.16
CISPEP 14 THR A 28 PRO A 29 14 -0.21
CISPEP 15 THR A 28 PRO A 29 15 -0.13
CISPEP 16 THR A 28 PRO A 29 16 -0.06
CISPEP 17 THR A 28 PRO A 29 17 -0.13
CISPEP 18 THR A 28 PRO A 29 18 -0.12
CISPEP 19 THR A 28 PRO A 29 19 -0.08
CISPEP 20 THR A 28 PRO A 29 20 -0.22
CISPEP 21 THR A 28 PRO A 29 21 -0.27
CISPEP 22 THR A 28 PRO A 29 22 -0.21
CISPEP 23 THR A 28 PRO A 29 23 -0.23
CISPEP 24 THR A 28 PRO A 29 24 -0.14
CISPEP 25 THR A 28 PRO A 29 25 -0.14
CISPEP 26 THR A 28 PRO A 29 26 -0.21
CISPEP 27 THR A 28 PRO A 29 27 -0.17
CISPEP 28 THR A 28 PRO A 29 28 -0.23
CISPEP 29 THR A 28 PRO A 29 29 -0.19
CISPEP 30 THR A 28 PRO A 29 30 -0.17
CISPEP 31 THR A 28 PRO A 29 31 -0.17
CISPEP 32 THR A 28 PRO A 29 32 -0.25
CISPEP 33 THR A 28 PRO A 29 33 -0.13
CISPEP 34 THR A 28 PRO A 29 34 -0.23
CISPEP 35 THR A 28 PRO A 29 35 -0.19
CISPEP 36 THR A 28 PRO A 29 36 -0.15
CISPEP 37 THR A 28 PRO A 29 37 -0.14
CISPEP 38 THR A 28 PRO A 29 38 -0.13
CISPEP 39 THR A 28 PRO A 29 39 -0.44
CISPEP 40 THR A 28 PRO A 29 40 -0.19
SITE 1 1 5 GLN A 9 ASN A 14 THR A 15 THR A 18
SITE 2 1 5 GLN A 44
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 16 2 Bytes