Header list of 2ftu.pdb file
Complete list - r 9 2 Bytes
HEADER LIPID BINDING PROTEIN 24-JAN-06 2FTU TITLE SOLUTION STRUCTURE OF DOMAIN 3 OF RAP COMPND MOL_ID: 1; COMPND 2 MOLECULE: ALPHA-2-MACROGLOBULIN RECEPTOR-ASSOCIATED PROTEIN, DOMAIN COMPND 3 3; COMPND 4 CHAIN: A; COMPND 5 FRAGMENT: RESIDUES 240-357; 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: LRPAP1; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID KEYWDS DOMAIN 3; RAP; RECEPTOR-ASSOCIATED PROTEIN, LIPID BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR D.LEE,J.D.WALSH,Y.-X.WANG REVDAT 3 09-MAR-22 2FTU 1 REMARK REVDAT 2 24-FEB-09 2FTU 1 VERSN REVDAT 1 09-MAY-06 2FTU 0 JRNL AUTH D.LEE,J.D.WALSH,I.MIKHAILENKO,P.YU,M.MIGLIORINI,Y.WU, JRNL AUTH 2 S.KRUEGER,J.E.CURTIS,B.HARRIS,S.LOCKETT,S.C.BLACKLOW, JRNL AUTH 3 D.K.STRICKLAND,Y.X.WANG JRNL TITL RAP USES A HISTIDINE SWITCH TO REGULATE ITS INTERACTION WITH JRNL TITL 2 LRP IN THE ER AND GOLGI. JRNL REF MOL.CELL V. 22 423 2006 JRNL REFN ISSN 1097-2765 JRNL PMID 16678114 JRNL DOI 10.1016/J.MOLCEL.2006.04.011 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CYANA 2.1.4 REMARK 3 AUTHORS : P.GUNTERT ET AL. REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2FTU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-MAR-06. REMARK 100 THE DEPOSITION ID IS D_1000036304. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : NULL REMARK 210 PH : NULL REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : NULL REMARK 210 SPECTROMETER MODEL : NULL REMARK 210 SPECTROMETER MANUFACTURER : NULL REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : CYANA 2.1.4 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS 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: 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 3 TYR A 55 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES REMARK 500 4 ARG A 82 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES REMARK 500 9 ARG A 67 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES REMARK 500 11 ARG A 91 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 17 ARG A 109 NE - CZ - NH2 ANGL. DEV. = -3.4 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 TYR A 7 -144.37 -137.09 REMARK 500 1 THR A 9 -19.42 -165.05 REMARK 500 1 GLU A 10 -166.24 -73.47 REMARK 500 1 GLU A 12 16.59 -64.77 REMARK 500 1 PHE A 13 62.03 -112.94 REMARK 500 1 GLU A 14 -72.79 -102.89 REMARK 500 1 GLU A 15 65.23 -152.98 REMARK 500 1 PRO A 16 -73.46 -79.60 REMARK 500 1 VAL A 18 -71.18 -81.28 REMARK 500 1 SER A 27 -3.40 -155.18 REMARK 500 1 ALA A 28 -80.78 -53.17 REMARK 500 1 ASN A 29 47.54 -160.82 REMARK 500 1 LEU A 30 -132.84 -93.29 REMARK 500 1 ALA A 113 85.53 47.70 REMARK 500 1 ARG A 114 -73.99 -60.02 REMARK 500 1 HIS A 115 -40.15 163.51 REMARK 500 1 ASN A 116 57.35 -107.18 REMARK 500 1 GLU A 117 178.66 56.37 REMARK 500 2 VAL A 2 -78.65 -139.20 REMARK 500 2 HIS A 4 -75.28 -122.67 REMARK 500 2 GLU A 10 61.28 -163.24 REMARK 500 2 GLU A 14 29.27 -164.56 REMARK 500 2 ARG A 17 -76.57 -153.64 REMARK 500 2 SER A 27 14.41 -142.65 REMARK 500 2 ASN A 29 20.39 -169.61 REMARK 500 2 LEU A 30 -168.42 -73.08 REMARK 500 2 ALA A 113 68.67 29.20 REMARK 500 2 ASN A 116 10.91 -173.24 REMARK 500 3 VAL A 2 -84.51 -159.85 REMARK 500 3 TYR A 7 107.13 -160.69 REMARK 500 3 ALA A 11 165.08 91.80 REMARK 500 3 GLU A 14 -95.84 -86.36 REMARK 500 3 PRO A 16 -73.10 -73.62 REMARK 500 3 ARG A 17 -39.81 -149.53 REMARK 500 3 SER A 27 29.48 -157.29 REMARK 500 3 ALA A 28 -71.97 -63.91 REMARK 500 3 ASN A 29 49.12 173.98 REMARK 500 3 LEU A 30 -129.36 -92.81 REMARK 500 3 ARG A 109 -74.92 -75.47 REMARK 500 3 ALA A 113 74.36 42.96 REMARK 500 4 HIS A 4 72.39 -151.17 REMARK 500 4 GLN A 5 -93.06 45.71 REMARK 500 4 GLU A 10 33.76 73.65 REMARK 500 4 GLU A 12 1.00 59.70 REMARK 500 4 GLU A 15 59.21 -150.54 REMARK 500 4 ARG A 17 -8.87 -55.85 REMARK 500 4 GLN A 26 -34.19 -38.99 REMARK 500 4 LEU A 30 -164.01 -104.92 REMARK 500 4 SER A 71 9.19 -69.74 REMARK 500 4 ASP A 74 -105.57 -92.81 REMARK 500 REMARK 500 THIS ENTRY HAS 264 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 GLU A 117 LEU A 118 2 144.82 REMARK 500 GLU A 117 LEU A 118 3 -147.90 REMARK 500 GLU A 117 LEU A 118 6 -141.63 REMARK 500 GLN A 5 GLY A 6 8 147.31 REMARK 500 GLU A 12 PHE A 13 10 149.78 REMARK 500 ARG A 112 ALA A 113 10 -144.88 REMARK 500 GLU A 117 LEU A 118 12 -147.47 REMARK 500 GLY A 6 TYR A 7 15 -130.84 REMARK 500 ARG A 112 ALA A 113 15 139.95 REMARK 500 ARG A 114 HIS A 115 18 147.33 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 TYR A 55 0.07 SIDE CHAIN REMARK 500 1 ARG A 80 0.09 SIDE CHAIN REMARK 500 2 ARG A 39 0.09 SIDE CHAIN REMARK 500 2 ARG A 77 0.11 SIDE CHAIN REMARK 500 3 ARG A 67 0.13 SIDE CHAIN REMARK 500 3 ARG A 82 0.10 SIDE CHAIN REMARK 500 3 ARG A 91 0.08 SIDE CHAIN REMARK 500 4 ARG A 77 0.08 SIDE CHAIN REMARK 500 5 ARG A 77 0.08 SIDE CHAIN REMARK 500 5 TYR A 97 0.10 SIDE CHAIN REMARK 500 5 ARG A 109 0.18 SIDE CHAIN REMARK 500 6 ARG A 1 0.09 SIDE CHAIN REMARK 500 6 ARG A 91 0.12 SIDE CHAIN REMARK 500 6 ARG A 109 0.10 SIDE CHAIN REMARK 500 7 TYR A 97 0.14 SIDE CHAIN REMARK 500 7 ARG A 109 0.12 SIDE CHAIN REMARK 500 9 ARG A 1 0.08 SIDE CHAIN REMARK 500 9 ARG A 77 0.08 SIDE CHAIN REMARK 500 9 ARG A 91 0.08 SIDE CHAIN REMARK 500 10 TYR A 97 0.07 SIDE CHAIN REMARK 500 11 ARG A 1 0.12 SIDE CHAIN REMARK 500 11 ARG A 80 0.08 SIDE CHAIN REMARK 500 11 ARG A 114 0.10 SIDE CHAIN REMARK 500 12 ARG A 39 0.12 SIDE CHAIN REMARK 500 12 ARG A 77 0.10 SIDE CHAIN REMARK 500 12 TYR A 97 0.08 SIDE CHAIN REMARK 500 12 ARG A 112 0.08 SIDE CHAIN REMARK 500 13 PHE A 45 0.11 SIDE CHAIN REMARK 500 13 TYR A 97 0.07 SIDE CHAIN REMARK 500 14 ARG A 67 0.09 SIDE CHAIN REMARK 500 14 ARG A 109 0.12 SIDE CHAIN REMARK 500 16 ARG A 112 0.08 SIDE CHAIN REMARK 500 17 ARG A 17 0.10 SIDE CHAIN REMARK 500 17 ARG A 39 0.09 SIDE CHAIN REMARK 500 17 ARG A 91 0.11 SIDE CHAIN REMARK 500 17 ARG A 109 0.08 SIDE CHAIN REMARK 500 18 ARG A 1 0.08 SIDE CHAIN REMARK 500 18 TYR A 55 0.07 SIDE CHAIN REMARK 500 19 TYR A 7 0.12 SIDE CHAIN REMARK 500 19 ARG A 17 0.11 SIDE CHAIN REMARK 500 19 ARG A 80 0.08 SIDE CHAIN REMARK 500 19 TYR A 97 0.08 SIDE CHAIN REMARK 500 20 TYR A 7 0.08 SIDE CHAIN REMARK 500 20 ARG A 77 0.15 SIDE CHAIN REMARK 500 20 ARG A 112 0.14 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2FFT RELATED DB: PDB REMARK 900 RELATED ID: 2FFV RELATED DB: PDB DBREF 2FTU A 1 118 UNP P30533 AMRP_HUMAN 240 357 SEQRES 1 A 118 ARG VAL SER HIS GLN GLY TYR SER THR GLU ALA GLU PHE SEQRES 2 A 118 GLU GLU PRO ARG VAL ILE ASP LEU TRP ASP LEU ALA GLN SEQRES 3 A 118 SER ALA ASN LEU THR ASP LYS GLU LEU GLU ALA PHE ARG SEQRES 4 A 118 GLU GLU LEU LYS HIS PHE GLU ALA LYS ILE GLU LYS HIS SEQRES 5 A 118 ASN HIS TYR GLN LYS GLN LEU GLU ILE ALA HIS GLU LYS SEQRES 6 A 118 LEU ARG HIS ALA GLU SER VAL GLY ASP GLY GLU ARG VAL SEQRES 7 A 118 SER ARG SER ARG GLU LYS HIS ALA LEU LEU GLU GLY ARG SEQRES 8 A 118 THR LYS GLU LEU GLY TYR THR VAL LYS LYS HIS LEU GLN SEQRES 9 A 118 ASP LEU SER GLY ARG ILE SER ARG ALA ARG HIS ASN GLU SEQRES 10 A 118 LEU HELIX 1 1 ARG A 17 ALA A 25 1 9 HELIX 2 2 THR A 31 SER A 71 1 41 HELIX 3 3 GLY A 75 ALA A 113 1 39 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