Header list of 1m7l.pdb file
Complete list - b 23 2 Bytes
HEADER SUGAR BINDING PROTEIN 22-JUL-02 1M7L TITLE SOLUTION STRUCTURE OF THE COILED-COIL TRIMERIZATION DOMAIN FROM LUNG TITLE 2 SURFACTANT PROTEIN D COMPND MOL_ID: 1; COMPND 2 MOLECULE: PULMONARY SURFACTANT-ASSOCIATED PROTEIN D; COMPND 3 CHAIN: A, B, C; COMPND 4 FRAGMENT: TRIMERIC COILED-COIL DOMAIN; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PGEX-2T KEYWDS COILED COIL, LUNG SURFACTANT PROTEIN, TRIMER, AMBIGUOUS DISTANCE KEYWDS 2 RESTRAINTS, NMR-SPECTROSCOPY, SUGAR BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 21 AUTHOR H.KOVACS,S.I.O'DONOGHUE,H.-J.HOPPE,D.COMFORT,K.B.M.REID,I.D.CAMPBELL, AUTHOR 2 M.NILGES REVDAT 3 23-FEB-22 1M7L 1 REMARK SEQADV REVDAT 2 24-FEB-09 1M7L 1 VERSN REVDAT 1 27-NOV-02 1M7L 0 JRNL AUTH H.KOVACS,S.I.O'DONOGHUE,H.-J.HOPPE,D.COMFORT,K.B.M.REID, JRNL AUTH 2 I.D.CAMPBELL,M.NILGES JRNL TITL SOLUTION STRUCTURE OF THE COILED-COIL TRIMERIZATION DOMAIN JRNL TITL 2 FROM LUNG SURFACTANT PROTEIN D JRNL REF J.BIOMOL.NMR V. 24 89 2002 JRNL REFN ISSN 0925-2738 JRNL PMID 12495025 JRNL DOI 10.1023/A:1020980006628 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XPLOR 3.851 REMARK 3 AUTHORS : A. T. BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 NMR STRUCTURE CALCULATION USING THE SYMMETRY ADR METHOD REMARK 3 (ADR=AMBIGUOUS DISTANCE RESTRAINTS) DEVELOPED FOR REMARK 3 SYMMETRIC OLIGOMERS BY NILGES, M. (1993) PROTEINS REMARK 3 17, 297-309; O'DONOGHUE, S. I., REMARK 3 KING, G. F. AND NILGES, M (1996) J. BIOMOL. NMR 8, 193-206. REMARK 4 REMARK 4 1M7L COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-JUL-02. REMARK 100 THE DEPOSITION ID IS D_1000016695. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 4.4 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; 15N-NOESY; 15N REMARK 210 -TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ REMARK 210 SPECTROMETER MODEL : OXFORD; HOME-ASSEBLED REMARK 210 SPECTROMETER MANUFACTURER : NULL REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : ARIA REMARK 210 METHOD USED : XPLOR USING THE AUTOMATED REMARK 210 STRUCTURE CALCULATION ARIA REMARK 210 ROUTINE REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C 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 HA2 GLY C 97 HE21 GLN C 100 1.31 REMARK 500 HA2 GLY A 17 HE21 GLN A 20 1.31 REMARK 500 HA2 GLY B 57 HE21 GLN B 60 1.33 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 LYS A 31 32.41 -97.98 REMARK 500 1 LEU A 34 -27.23 -172.84 REMARK 500 1 PRO A 36 -179.21 -65.62 REMARK 500 1 LYS B 71 31.39 -98.23 REMARK 500 1 LEU B 74 -27.18 -170.55 REMARK 500 1 PRO B 76 -179.19 -65.58 REMARK 500 1 LEU C 114 -28.56 -170.77 REMARK 500 2 LEU A 34 -31.43 -175.56 REMARK 500 2 PRO A 36 -158.97 -86.87 REMARK 500 2 ASN A 37 -152.27 -114.98 REMARK 500 2 LEU B 74 -31.38 -175.63 REMARK 500 2 PRO B 76 -159.53 -87.62 REMARK 500 2 ASN B 77 -151.85 -114.12 REMARK 500 2 LEU C 114 -32.10 -176.17 REMARK 500 2 PRO C 116 -159.20 -86.93 REMARK 500 2 ASN C 117 -149.40 -114.25 REMARK 500 3 LEU A 34 -29.14 -171.58 REMARK 500 3 LEU B 74 -30.29 -172.57 REMARK 500 3 LEU C 114 -33.31 -169.95 REMARK 500 4 GLU A 33 -126.29 -81.22 REMARK 500 4 LEU A 34 -75.42 62.45 REMARK 500 4 ASN A 37 -89.23 -102.96 REMARK 500 4 GLU B 73 -127.01 -81.28 REMARK 500 4 LEU B 74 -74.84 62.07 REMARK 500 4 ASN B 77 -89.39 -102.57 REMARK 500 4 GLU C 113 -124.41 -76.46 REMARK 500 4 LEU C 114 -84.85 59.88 REMARK 500 4 ASN C 117 -89.07 -102.74 REMARK 500 5 LEU A 34 -36.22 -177.71 REMARK 500 5 PRO A 36 -172.39 -65.51 REMARK 500 5 ASN A 37 -161.79 -100.32 REMARK 500 5 LEU B 74 -33.13 -176.28 REMARK 500 5 PRO B 76 -172.11 -65.63 REMARK 500 5 ASN B 77 -161.35 -100.47 REMARK 500 5 LEU C 114 -33.81 -177.74 REMARK 500 5 PRO C 116 -168.46 -65.52 REMARK 500 5 ASN C 117 -162.13 -104.62 REMARK 500 6 LEU A 34 -36.66 -167.92 REMARK 500 6 LEU B 74 -36.06 -167.72 REMARK 500 6 LEU C 114 -37.54 -167.39 REMARK 500 8 LEU A 34 -39.90 -164.04 REMARK 500 8 LEU B 74 -41.27 -162.20 REMARK 500 8 LEU C 114 -32.83 -167.32 REMARK 500 9 PHE A 35 -72.35 -41.32 REMARK 500 9 PHE B 75 -72.52 -41.16 REMARK 500 9 PHE C 115 -72.13 -40.41 REMARK 500 10 LEU A 34 -74.45 -54.82 REMARK 500 10 PHE A 35 53.03 -104.31 REMARK 500 10 LEU B 74 -74.22 -55.71 REMARK 500 10 PHE B 75 52.21 -104.28 REMARK 500 REMARK 500 THIS ENTRY HAS 100 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1M7L A 1 38 UNP P35247 SFTPD_HUMAN 220 257 DBREF 1M7L B 41 78 UNP P35247 SFTPD_HUMAN 220 257 DBREF 1M7L C 81 118 UNP P35247 SFTPD_HUMAN 220 257 SEQADV 1M7L GLY A 39 UNP P35247 CLONING ARTIFACT SEQADV 1M7L ILE A 40 UNP P35247 CLONING ARTIFACT SEQADV 1M7L GLY B 79 UNP P35247 CLONING ARTIFACT SEQADV 1M7L ILE B 80 UNP P35247 CLONING ARTIFACT SEQADV 1M7L GLY C 119 UNP P35247 CLONING ARTIFACT SEQADV 1M7L ILE C 120 UNP P35247 CLONING ARTIFACT SEQRES 1 A 40 GLY LEU PRO ASP VAL ALA SER LEU ARG GLN GLN VAL GLU SEQRES 2 A 40 ALA LEU GLN GLY GLN VAL GLN HIS LEU GLN ALA ALA PHE SEQRES 3 A 40 SER GLN TYR LYS LYS VAL GLU LEU PHE PRO ASN GLY GLY SEQRES 4 A 40 ILE SEQRES 1 B 40 GLY LEU PRO ASP VAL ALA SER LEU ARG GLN GLN VAL GLU SEQRES 2 B 40 ALA LEU GLN GLY GLN VAL GLN HIS LEU GLN ALA ALA PHE SEQRES 3 B 40 SER GLN TYR LYS LYS VAL GLU LEU PHE PRO ASN GLY GLY SEQRES 4 B 40 ILE SEQRES 1 C 40 GLY LEU PRO ASP VAL ALA SER LEU ARG GLN GLN VAL GLU SEQRES 2 C 40 ALA LEU GLN GLY GLN VAL GLN HIS LEU GLN ALA ALA PHE SEQRES 3 C 40 SER GLN TYR LYS LYS VAL GLU LEU PHE PRO ASN GLY GLY SEQRES 4 C 40 ILE HELIX 1 1 GLY A 1 LYS A 31 1 31 HELIX 2 2 GLY B 41 LYS B 71 1 31 HELIX 3 3 GLY C 81 LYS C 111 1 31 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