Header list of 1z2f.pdb file
Complete list - r 2 2 Bytes
HEADER ANTIFREEZE PROTEIN 08-MAR-05 1Z2F TITLE SOLUTION STRUCTURE OF CFAFP-501 COMPND MOL_ID: 1; COMPND 2 MOLECULE: ANTIFREEZE PROTEIN ISOFORM 501; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: CHORISTONEURA FUMIFERANA; SOURCE 3 ORGANISM_COMMON: SPRUCE BUDWORM; SOURCE 4 ORGANISM_TAXID: 7141; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS ANTIFREEZE PROTEIN, CHORISTONEURA FUMIFERANA, SPRUCE BUDWORM, KEYWDS 2 SOLUTION STRUCTURE EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR C.LI,C.JIN REVDAT 3 02-MAR-22 1Z2F 1 REMARK REVDAT 2 24-FEB-09 1Z2F 1 VERSN REVDAT 1 11-OCT-05 1Z2F 0 JRNL AUTH C.LI,X.GUO,Z.JIA,B.XIA,C.JIN JRNL TITL SOLUTION STRUCTURE OF AN ANTIFREEZE PROTEIN CFAFP-501 FROM JRNL TITL 2 CHORISTONEURA FUMIFERANA JRNL REF J.BIOMOL.NMR V. 32 251 2005 JRNL REFN ISSN 0925-2738 JRNL PMID 16132825 JRNL DOI 10.1007/S10858-005-8206-3 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 3.5, AMBER 7.0 REMARK 3 AUTHORS : BRUKER (XWINNMR), REMARK 3 PEARLMAN,CASE,CALDWELL,ROSS,CHEATHAM,FERGUSON,SEIBEL,SINGH, REMARK 3 WEINER,KOLLMAN (AMBER) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1Z2F COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-MAR-05. REMARK 100 THE DEPOSITION ID IS D_1000032212. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 290 REMARK 210 PH : 5.7 REMARK 210 IONIC STRENGTH : 100MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.2MM CFAFP-501 U-15N,13C; 50MM REMARK 210 PHOSHPATE BUFFER,50MM SODIUM REMARK 210 CHLORIDE; 90% H2O, 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 500 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 2.1, NMRVIEW 5, CYANA REMARK 210 1.0.6 REMARK 210 METHOD USED : SIMULATED ANNEALING, MOLECULAR REMARK 210 DYNAMICS 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: THIS STRUCTURE WAS DETERMINED USING STANDARD 3D REMARK 210 HETERONUCLEAR TECHNIQUES. 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: 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 5 ARG A 102 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES REMARK 500 6 TYR A 43 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES REMARK 500 7 ARG A 40 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES REMARK 500 8 CYS A 17 CA - CB - SG ANGL. DEV. = 7.8 DEGREES REMARK 500 10 TYR A 73 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES REMARK 500 12 TYR A 43 CB - CG - CD2 ANGL. DEV. = -3.9 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 THR A 3 44.07 -74.72 REMARK 500 1 ASN A 8 8.47 -156.58 REMARK 500 1 LYS A 19 47.19 34.22 REMARK 500 1 ASN A 29 35.49 39.88 REMARK 500 1 ASP A 34 74.13 50.66 REMARK 500 1 LYS A 50 33.84 39.72 REMARK 500 1 ARG A 102 48.14 39.38 REMARK 500 2 THR A 3 156.38 64.41 REMARK 500 2 ASN A 8 16.37 55.87 REMARK 500 2 LYS A 19 -22.02 59.99 REMARK 500 2 LYS A 50 48.34 37.22 REMARK 500 2 ASP A 55 74.94 51.17 REMARK 500 2 LYS A 60 19.99 52.09 REMARK 500 2 LEU A 65 28.65 48.28 REMARK 500 3 ASN A 8 34.28 -162.04 REMARK 500 3 LYS A 19 -22.41 60.37 REMARK 500 3 ASN A 29 38.01 39.53 REMARK 500 3 LYS A 50 52.72 34.87 REMARK 500 3 LEU A 65 25.53 47.12 REMARK 500 3 PRO A 107 12.18 -64.48 REMARK 500 4 ASN A 8 53.05 -163.00 REMARK 500 4 LYS A 19 50.79 34.19 REMARK 500 4 ASN A 24 78.10 57.19 REMARK 500 4 ASP A 34 92.66 37.50 REMARK 500 4 LYS A 50 36.80 39.02 REMARK 500 4 ARG A 102 50.06 37.50 REMARK 500 5 ASN A 8 81.75 -170.25 REMARK 500 5 LYS A 19 43.37 36.04 REMARK 500 5 ASN A 29 35.60 39.82 REMARK 500 5 ASP A 34 77.82 49.43 REMARK 500 5 LYS A 50 48.52 34.92 REMARK 500 5 ASP A 55 71.90 51.15 REMARK 500 5 ALA A 120 -144.64 48.89 REMARK 500 6 ASN A 8 28.20 -162.31 REMARK 500 6 LYS A 19 6.56 55.15 REMARK 500 6 LYS A 50 50.11 33.41 REMARK 500 6 LEU A 65 28.92 47.12 REMARK 500 7 ASN A 8 17.15 55.17 REMARK 500 7 LYS A 19 -20.77 58.74 REMARK 500 7 LYS A 50 52.27 34.74 REMARK 500 7 LEU A 65 24.73 49.51 REMARK 500 7 ILE A 113 35.08 -146.32 REMARK 500 8 THR A 3 80.31 -153.47 REMARK 500 8 ASN A 8 30.70 -164.86 REMARK 500 8 LYS A 50 48.98 32.42 REMARK 500 8 LEU A 65 26.58 49.61 REMARK 500 9 ASN A 8 14.40 56.19 REMARK 500 9 LYS A 19 -4.10 56.29 REMARK 500 9 ASN A 29 38.35 38.84 REMARK 500 9 ASP A 34 74.31 46.01 REMARK 500 REMARK 500 THIS ENTRY HAS 121 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 11 TYR A 43 0.07 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 6111 RELATED DB: BMRB REMARK 900 1H, 13C, 15N ASSINGMENTS OF CFAFP501 DBREF 1Z2F A 1 121 UNP Q9GSA6 Q9GSA6_CHOFU 18 138 SEQRES 1 A 121 ASP GLY THR CYS VAL ASN THR ASN SER GLN ILE THR ALA SEQRES 2 A 121 ASN SER GLN CYS VAL LYS SER THR ALA THR ASN CYS TYR SEQRES 3 A 121 ILE ASP ASN SER GLN LEU VAL ASP THR SER ILE CYS THR SEQRES 4 A 121 ARG SER GLN TYR SER ASP ALA ASN VAL LYS LYS SER VAL SEQRES 5 A 121 THR THR ASP CYS ASN ILE ASP LYS SER GLN VAL TYR LEU SEQRES 6 A 121 THR THR CYS THR GLY SER GLN TYR ASN GLY ILE TYR ILE SEQRES 7 A 121 ARG SER SER THR THR THR GLY THR SER ILE SER GLY PRO SEQRES 8 A 121 GLY CYS SER ILE SER THR CYS THR ILE THR ARG GLY VAL SEQRES 9 A 121 ALA THR PRO ALA ALA ALA CYS LYS ILE SER GLY CYS SER SEQRES 10 A 121 LEU SER ALA MET SHEET 1 A 8 CYS A 4 ASN A 6 0 SHEET 2 A 8 SER A 20 THR A 23 1 O SER A 20 N VAL A 5 SHEET 3 A 8 ILE A 37 THR A 39 1 O CYS A 38 N THR A 23 SHEET 4 A 8 VAL A 52 THR A 54 1 O THR A 53 N ILE A 37 SHEET 5 A 8 THR A 67 THR A 69 1 O CYS A 68 N THR A 54 SHEET 6 A 8 THR A 82 THR A 84 1 O THR A 83 N THR A 67 SHEET 7 A 8 THR A 99 THR A 101 1 O ILE A 100 N THR A 84 SHEET 8 A 8 VAL A 104 ALA A 105 -1 O VAL A 104 N THR A 101 SHEET 1 B 7 GLN A 10 ILE A 11 0 SHEET 2 B 7 TYR A 26 ASP A 28 1 O ILE A 27 N GLN A 10 SHEET 3 B 7 GLN A 42 SER A 44 1 O TYR A 43 N TYR A 26 SHEET 4 B 7 ASN A 57 ASP A 59 1 O ILE A 58 N SER A 44 SHEET 5 B 7 GLN A 72 ARG A 79 1 O TYR A 73 N ASP A 59 SHEET 6 B 7 THR A 86 SER A 96 1 O ILE A 88 N GLN A 72 SHEET 7 B 7 LYS A 112 SER A 114 -1 O LYS A 112 N SER A 96 SHEET 1 C 7 GLN A 16 VAL A 18 0 SHEET 2 C 7 GLN A 31 VAL A 33 1 O LEU A 32 N GLN A 16 SHEET 3 C 7 ASN A 47 LYS A 49 1 O VAL A 48 N VAL A 33 SHEET 4 C 7 GLN A 62 TYR A 64 1 O VAL A 63 N LYS A 49 SHEET 5 C 7 GLN A 72 ARG A 79 1 O ILE A 76 N GLN A 62 SHEET 6 C 7 THR A 86 SER A 96 1 O ILE A 88 N GLN A 72 SHEET 7 C 7 SER A 117 ALA A 120 -1 O SER A 117 N SER A 89 SSBOND 1 CYS A 4 CYS A 17 1555 1555 2.03 SSBOND 2 CYS A 25 CYS A 38 1555 1555 2.04 SSBOND 3 CYS A 56 CYS A 68 1555 1555 2.04 SSBOND 4 CYS A 93 CYS A 116 1555 1555 2.03 SSBOND 5 CYS A 98 CYS A 111 1555 1555 2.04 CISPEP 1 GLY A 90 PRO A 91 1 -10.31 CISPEP 2 GLY A 90 PRO A 91 2 -10.14 CISPEP 3 GLY A 90 PRO A 91 3 2.19 CISPEP 4 GLY A 90 PRO A 91 4 -10.20 CISPEP 5 GLY A 90 PRO A 91 5 10.44 CISPEP 6 GLY A 90 PRO A 91 6 -10.43 CISPEP 7 GLY A 90 PRO A 91 7 -4.93 CISPEP 8 GLY A 90 PRO A 91 8 -10.17 CISPEP 9 GLY A 90 PRO A 91 9 -10.38 CISPEP 10 GLY A 90 PRO A 91 10 -10.80 CISPEP 11 GLY A 90 PRO A 91 11 -9.49 CISPEP 12 GLY A 90 PRO A 91 12 10.44 CISPEP 13 GLY A 90 PRO A 91 13 -10.25 CISPEP 14 GLY A 90 PRO A 91 14 -10.21 CISPEP 15 GLY A 90 PRO A 91 15 -7.39 CISPEP 16 GLY A 90 PRO A 91 16 -10.35 CISPEP 17 GLY A 90 PRO A 91 17 -10.02 CISPEP 18 GLY A 90 PRO A 91 18 -10.52 CISPEP 19 GLY A 90 PRO A 91 19 10.54 CISPEP 20 GLY A 90 PRO A 91 20 10.48 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