Header list of 1l1i.pdb file
Complete list - b 23 2 Bytes
HEADER ANTIFREEZE PROTEIN 16-FEB-02 1L1I
TITLE SOLUTION STRUCTURE OF THE TENEBRIO MOLITOR ANTIFREEZE PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THERMAL HYSTERESIS PROTEIN ISOFORM YL-1 (2-14);
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TENEBRIO MOLITOR;
SOURCE 3 ORGANISM_COMMON: YELLOW MEALWORM;
SOURCE 4 ORGANISM_TAXID: 7067;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS BETA-HELIX, ANTIFREEZE PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.E.DALEY,L.SPYRACOPOULOS,Z.JIA,P.L.DAVIES,B.D.SYKES
REVDAT 3 23-FEB-22 1L1I 1 REMARK
REVDAT 2 24-FEB-09 1L1I 1 VERSN
REVDAT 1 22-MAY-02 1L1I 0
JRNL AUTH M.E.DALEY,L.SPYRACOPOULOS,Z.JIA,P.L.DAVIES,B.D.SYKES
JRNL TITL STRUCTURE AND DYNAMICS OF A BETA-HELICAL ANTIFREEZE PROTEIN.
JRNL REF BIOCHEMISTRY V. 41 5515 2002
JRNL REFN ISSN 0006-2960
JRNL PMID 11969412
JRNL DOI 10.1021/BI0121252
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1B, CNS 1.0
REMARK 3 AUTHORS : VARIAN ASSOCIATES, INC. (VNMR), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1L1I COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-FEB-02.
REMARK 100 THE DEPOSITION ID IS D_1000015556.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 5.5
REMARK 210 IONIC STRENGTH : 0MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.4 MM TMAFP U-15N; 90% H2O, 10%
REMARK 210 D2O; 1MM TMAFP; 90% H2O, 10% D2O;
REMARK 210 1MM TMAFP; 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-EDITED_TOCSY; HNHA; HNHB;
REMARK 210 3D_15N-SEPARATED_NOESY; 2D_TOCSY;
REMARK 210 2D_NOESY; 13C-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE SGI6, NMRVIEW 4.1.2, CNS
REMARK 210 1.0
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
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: 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 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
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 CYS A 2 -40.12 -178.65
REMARK 500 1 ALA A 6 23.47 -156.13
REMARK 500 1 CYS A 8 -97.35 -117.96
REMARK 500 1 SER A 10 -57.80 -132.02
REMARK 500 1 CYS A 18 -77.04 -136.01
REMARK 500 1 PRO A 22 -83.82 -85.18
REMARK 500 1 ASN A 29 -175.08 81.47
REMARK 500 1 SER A 30 -161.23 82.76
REMARK 500 1 HIS A 32 49.25 170.05
REMARK 500 1 LYS A 35 32.49 -97.06
REMARK 500 1 THR A 40 -128.35 -88.30
REMARK 500 1 SER A 42 -145.89 -142.30
REMARK 500 1 THR A 43 -141.26 -141.82
REMARK 500 1 ASP A 44 89.70 20.63
REMARK 500 1 ASN A 53 39.30 160.73
REMARK 500 1 ASP A 56 31.97 -148.48
REMARK 500 1 GLU A 59 40.59 -96.10
REMARK 500 1 TYR A 70 92.39 -48.33
REMARK 500 1 LYS A 71 80.34 73.77
REMARK 500 1 THR A 76 -70.60 -121.76
REMARK 500 1 PRO A 82 92.96 -30.18
REMARK 500 2 ALA A 6 -75.43 65.87
REMARK 500 2 THR A 12 -44.12 -144.06
REMARK 500 2 ASN A 23 34.46 -157.99
REMARK 500 2 ASN A 29 -163.88 81.14
REMARK 500 2 SER A 30 -169.17 82.52
REMARK 500 2 HIS A 32 50.21 -177.54
REMARK 500 2 THR A 40 -150.20 -111.81
REMARK 500 2 SER A 42 -151.78 -145.69
REMARK 500 2 THR A 43 -141.13 -141.90
REMARK 500 2 ASP A 44 80.00 9.77
REMARK 500 2 CYS A 51 139.95 -177.19
REMARK 500 2 ASN A 53 28.01 45.64
REMARK 500 2 ASP A 56 23.20 -148.07
REMARK 500 2 GLU A 59 39.43 -97.27
REMARK 500 2 TYR A 70 49.68 -89.95
REMARK 500 2 LYS A 71 42.65 177.13
REMARK 500 2 ASN A 77 54.79 -152.45
REMARK 500 3 CYS A 2 31.84 -157.35
REMARK 500 3 THR A 3 24.95 -144.29
REMARK 500 3 SER A 10 34.41 -148.99
REMARK 500 3 CYS A 18 -77.76 -147.84
REMARK 500 3 PRO A 22 -80.53 -84.32
REMARK 500 3 ASN A 29 163.79 73.80
REMARK 500 3 SER A 30 143.95 82.34
REMARK 500 3 HIS A 32 40.65 88.90
REMARK 500 3 LYS A 35 32.25 -96.02
REMARK 500 3 THR A 40 48.18 -90.43
REMARK 500 3 SER A 42 -158.24 -149.93
REMARK 500 3 THR A 43 -141.14 -140.93
REMARK 500
REMARK 500 THIS ENTRY HAS 381 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EZG RELATED DB: PDB
REMARK 900 1EZG IS THE CRYSTAL STRUCTURE OF THE TMAFP
DBREF 1L1I A 1 84 UNP O16119 O16119_TENMO 29 112
SEQRES 1 A 84 GLN CYS THR GLY GLY ALA ASP CYS THR SER CYS THR GLY
SEQRES 2 A 84 ALA CYS THR GLY CYS GLY ASN CYS PRO ASN ALA VAL THR
SEQRES 3 A 84 CYS THR ASN SER GLN HIS CYS VAL LYS ALA ASN THR CYS
SEQRES 4 A 84 THR GLY SER THR ASP CYS ASN THR ALA GLN THR CYS THR
SEQRES 5 A 84 ASN SER LYS ASP CYS PHE GLU ALA ASN THR CYS THR ASP
SEQRES 6 A 84 SER THR ASN CYS TYR LYS ALA THR ALA CYS THR ASN SER
SEQRES 7 A 84 SER GLY CYS PRO GLY HIS
SHEET 1 A 5 ALA A 14 THR A 16 0
SHEET 2 A 5 VAL A 25 THR A 28 1 O VAL A 25 N ALA A 14
SHEET 3 A 5 ASN A 37 THR A 40 1 O ASN A 37 N THR A 26
SHEET 4 A 5 GLN A 49 THR A 52 1 O GLN A 49 N THR A 38
SHEET 5 A 5 ASN A 61 THR A 64 1 O ASN A 61 N THR A 50
SSBOND 1 CYS A 2 CYS A 11 1555 1555 2.03
SSBOND 2 CYS A 8 CYS A 18 1555 1555 2.03
SSBOND 3 CYS A 15 CYS A 21 1555 1555 2.03
SSBOND 4 CYS A 27 CYS A 33 1555 1555 2.03
SSBOND 5 CYS A 39 CYS A 45 1555 1555 2.03
SSBOND 6 CYS A 51 CYS A 57 1555 1555 2.03
SSBOND 7 CYS A 63 CYS A 69 1555 1555 2.03
SSBOND 8 CYS A 75 CYS A 81 1555 1555 2.03
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 - b 23 2 Bytes