Header list of 1br0.pdb file
Complete list - v 3 2 Bytes
HEADER MEMBRANE PROTEIN 25-AUG-98 1BR0 TITLE THREE DIMENSIONAL STRUCTURE OF THE N-TERMINAL DOMAIN OF SYNTAXIN 1A COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN (SYNTAXIN 1-A); COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: N-TERMINAL; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 3 ORGANISM_COMMON: NORWAY RAT; SOURCE 4 ORGANISM_TAXID: 10116; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS SYNTAXIN, MEMBRANE FUSION, SYNAPTIC VESICLE EXOCYTOSIS, MEMBRANE KEYWDS 2 PROTEIN EXPDTA SOLUTION NMR NUMMDL 15 AUTHOR I.FERNANDEZ,J.UBACH,I.DUBULOVA,X.ZHANG,T.C.SUDHOF,J.RIZO REVDAT 5 03-NOV-21 1BR0 1 REMARK SEQADV REVDAT 4 24-FEB-09 1BR0 1 VERSN REVDAT 3 01-APR-03 1BR0 1 JRNL REVDAT 2 29-DEC-99 1BR0 4 HEADER COMPND REMARK JRNL REVDAT 2 2 4 ATOM SOURCE SEQRES REVDAT 1 02-SEP-98 1BR0 0 JRNL AUTH I.FERNANDEZ,J.UBACH,I.DULUBOVA,X.ZHANG,T.C.SUDHOF,J.RIZO JRNL TITL THREE-DIMENSIONAL STRUCTURE OF AN EVOLUTIONARILY CONSERVED JRNL TITL 2 N-TERMINAL DOMAIN OF SYNTAXIN 1A. JRNL REF CELL(CAMBRIDGE,MASS.) V. 94 841 1998 JRNL REFN ISSN 0092-8674 JRNL PMID 9753330 JRNL DOI 10.1016/S0092-8674(00)81742-0 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DISCOVER REMARK 3 AUTHORS : BIOSYM REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1BR0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE DEPOSITION ID IS D_1000008215. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 305 REMARK 210 PH : 6.3 REMARK 210 IONIC STRENGTH : 60 MM PHOSPHATE REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : UNITY500 REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : FELIX, NMRVIEW, NMRPIPE, INSIGHT REMARK 210 II, DISCOVER, NMTCHITECT REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15 REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION 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: 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 LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) 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 RES CSSEQI ATM2 DEVIATION REMARK 500 1 GLU A 32 CD GLU A 32 OE1 0.118 REMARK 500 1 GLU A 35 CD GLU A 35 OE2 0.118 REMARK 500 1 GLU A 38 CD GLU A 38 OE1 0.118 REMARK 500 1 GLU A 39 CD GLU A 39 OE1 0.118 REMARK 500 1 GLU A 49 CD GLU A 49 OE1 0.117 REMARK 500 1 GLU A 52 CD GLU A 52 OE2 0.118 REMARK 500 1 GLU A 53 CD GLU A 53 OE1 0.118 REMARK 500 1 HIS A 58 CG HIS A 58 CD2 0.067 REMARK 500 1 GLU A 69 CD GLU A 69 OE1 0.117 REMARK 500 1 GLU A 73 CD GLU A 73 OE1 0.118 REMARK 500 1 GLU A 74 CD GLU A 74 OE2 0.118 REMARK 500 1 GLU A 76 CD GLU A 76 OE1 0.118 REMARK 500 1 GLU A 77 CD GLU A 77 OE1 0.117 REMARK 500 1 GLU A 97 CD GLU A 97 OE1 0.118 REMARK 500 1 GLU A 101 CD GLU A 101 OE2 0.118 REMARK 500 1 GLU A 103 CD GLU A 103 OE2 0.118 REMARK 500 1 GLU A 104 CD GLU A 104 OE2 0.118 REMARK 500 1 HIS A 120 CG HIS A 120 CD2 0.060 REMARK 500 1 GLU A 129 CD GLU A 129 OE2 0.119 REMARK 500 1 GLU A 133 CD GLU A 133 OE1 0.119 REMARK 500 1 GLU A 143 CD GLU A 143 OE2 0.118 REMARK 500 2 GLU A 32 CD GLU A 32 OE2 0.118 REMARK 500 2 GLU A 35 CD GLU A 35 OE1 0.118 REMARK 500 2 GLU A 38 CD GLU A 38 OE1 0.118 REMARK 500 2 GLU A 39 CD GLU A 39 OE2 0.118 REMARK 500 2 GLU A 49 CD GLU A 49 OE1 0.119 REMARK 500 2 GLU A 52 CD GLU A 52 OE1 0.118 REMARK 500 2 GLU A 53 CD GLU A 53 OE1 0.118 REMARK 500 2 HIS A 58 CG HIS A 58 CD2 0.062 REMARK 500 2 GLU A 69 CD GLU A 69 OE1 0.119 REMARK 500 2 GLU A 73 CD GLU A 73 OE1 0.118 REMARK 500 2 GLU A 74 CD GLU A 74 OE2 0.118 REMARK 500 2 GLU A 76 CD GLU A 76 OE1 0.118 REMARK 500 2 GLU A 77 CD GLU A 77 OE1 0.118 REMARK 500 2 GLU A 97 CD GLU A 97 OE2 0.118 REMARK 500 2 GLU A 101 CD GLU A 101 OE1 0.119 REMARK 500 2 GLU A 103 CD GLU A 103 OE1 0.118 REMARK 500 2 GLU A 104 CD GLU A 104 OE1 0.119 REMARK 500 2 HIS A 120 CG HIS A 120 CD2 0.054 REMARK 500 2 GLU A 129 CD GLU A 129 OE1 0.118 REMARK 500 2 GLU A 133 CD GLU A 133 OE1 0.118 REMARK 500 2 GLU A 143 CD GLU A 143 OE2 0.119 REMARK 500 3 GLU A 32 CD GLU A 32 OE2 0.117 REMARK 500 3 GLU A 35 CD GLU A 35 OE2 0.118 REMARK 500 3 GLU A 38 CD GLU A 38 OE1 0.118 REMARK 500 3 GLU A 39 CD GLU A 39 OE1 0.118 REMARK 500 3 GLU A 49 CD GLU A 49 OE2 0.118 REMARK 500 3 GLU A 52 CD GLU A 52 OE2 0.118 REMARK 500 3 GLU A 53 CD GLU A 53 OE2 0.118 REMARK 500 3 HIS A 58 CG HIS A 58 CD2 0.064 REMARK 500 REMARK 500 THIS ENTRY HAS 310 BOND DEVIATIONS. 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 1 ASP A 27 CB - CG - OD1 ANGL. DEV. = -6.4 DEGREES REMARK 500 1 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES REMARK 500 1 ARG A 28 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES REMARK 500 1 ASP A 31 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES REMARK 500 1 ARG A 41 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES REMARK 500 1 ARG A 41 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES REMARK 500 1 ASP A 45 CB - CG - OD1 ANGL. DEV. = -6.4 DEGREES REMARK 500 1 ARG A 56 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES REMARK 500 1 ARG A 56 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES REMARK 500 1 HIS A 58 ND1 - CE1 - NE2 ANGL. DEV. = 8.8 DEGREES REMARK 500 1 LEU A 62 CA - CB - CG ANGL. DEV. = 14.4 DEGREES REMARK 500 1 ALA A 63 N - CA - CB ANGL. DEV. = -8.7 DEGREES REMARK 500 1 ASP A 68 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES REMARK 500 1 LYS A 70 CB - CA - C ANGL. DEV. = 16.5 DEGREES REMARK 500 1 LYS A 70 CA - C - N ANGL. DEV. = -16.0 DEGREES REMARK 500 1 THR A 71 CA - CB - CG2 ANGL. DEV. = 11.3 DEGREES REMARK 500 1 ASP A 81 CB - CG - OD1 ANGL. DEV. = -6.4 DEGREES REMARK 500 1 ARG A 90 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES REMARK 500 1 ARG A 90 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES REMARK 500 1 GLU A 104 N - CA - CB ANGL. DEV. = -11.2 DEGREES REMARK 500 1 ARG A 108 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES REMARK 500 1 ARG A 108 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES REMARK 500 1 ASP A 112 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES REMARK 500 1 ARG A 114 NE - CZ - NH1 ANGL. DEV. = 5.6 DEGREES REMARK 500 1 ARG A 114 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES REMARK 500 1 ARG A 116 NE - CZ - NH1 ANGL. DEV. = 5.6 DEGREES REMARK 500 1 ARG A 116 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES REMARK 500 1 HIS A 120 ND1 - CE1 - NE2 ANGL. DEV. = 8.9 DEGREES REMARK 500 1 ARG A 125 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES REMARK 500 1 ARG A 125 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES REMARK 500 1 ASP A 140 CB - CG - OD1 ANGL. DEV. = -6.2 DEGREES REMARK 500 1 ARG A 142 NE - CZ - NH1 ANGL. DEV. = 5.7 DEGREES REMARK 500 1 ARG A 142 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES REMARK 500 1 ARG A 144 NE - CZ - NH1 ANGL. DEV. = 5.6 DEGREES REMARK 500 1 ARG A 144 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES REMARK 500 2 ASP A 27 CB - CG - OD1 ANGL. DEV. = -6.4 DEGREES REMARK 500 2 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 5.7 DEGREES REMARK 500 2 ARG A 28 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES REMARK 500 2 ASP A 31 CB - CG - OD1 ANGL. DEV. = -6.5 DEGREES REMARK 500 2 ASP A 31 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES REMARK 500 2 ARG A 41 NE - CZ - NH1 ANGL. DEV. = 5.7 DEGREES REMARK 500 2 ARG A 41 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES REMARK 500 2 ASP A 45 CB - CG - OD1 ANGL. DEV. = -6.4 DEGREES REMARK 500 2 ARG A 56 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES REMARK 500 2 ARG A 56 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES REMARK 500 2 HIS A 58 ND1 - CE1 - NE2 ANGL. DEV. = 8.8 DEGREES REMARK 500 2 ASP A 68 CB - CG - OD1 ANGL. DEV. = -6.4 DEGREES REMARK 500 2 ASP A 81 CB - CG - OD2 ANGL. DEV. = -6.5 DEGREES REMARK 500 2 ARG A 90 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES REMARK 500 2 ARG A 90 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 491 ANGLE DEVIATIONS. 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 LEU A 62 -31.32 -39.42 REMARK 500 1 SER A 64 77.23 -24.60 REMARK 500 1 ASN A 66 -21.52 -155.30 REMARK 500 1 PRO A 67 -92.73 -61.60 REMARK 500 1 GLU A 69 -96.13 -69.53 REMARK 500 1 ASN A 107 83.23 71.52 REMARK 500 2 PRO A 67 -79.81 -78.04 REMARK 500 2 ASN A 107 78.53 78.03 REMARK 500 2 ARG A 142 3.22 -152.94 REMARK 500 2 GLU A 143 -72.80 -91.25 REMARK 500 3 PRO A 67 -157.33 -87.52 REMARK 500 3 ASN A 107 72.41 -170.72 REMARK 500 3 SER A 110 161.22 50.41 REMARK 500 3 ALA A 111 -51.17 60.79 REMARK 500 3 ARG A 144 42.01 -85.62 REMARK 500 4 LYS A 57 -71.17 -73.37 REMARK 500 4 GLU A 69 71.36 40.47 REMARK 500 4 LYS A 70 90.82 -28.32 REMARK 500 4 THR A 71 6.16 -46.92 REMARK 500 4 VAL A 89 -60.96 -90.15 REMARK 500 4 ASN A 107 78.04 -175.35 REMARK 500 5 PRO A 65 -9.12 -56.30 REMARK 500 5 ASN A 107 80.75 69.84 REMARK 500 5 SER A 109 71.45 25.37 REMARK 500 5 ARG A 142 46.55 -156.71 REMARK 500 5 ARG A 144 -28.14 138.57 REMARK 500 6 LEU A 62 -32.88 -38.67 REMARK 500 6 ALA A 63 36.41 -140.94 REMARK 500 6 SER A 64 75.56 -23.43 REMARK 500 6 ASN A 66 -49.75 -135.33 REMARK 500 6 PRO A 67 -165.36 -61.12 REMARK 500 6 ASP A 68 154.07 178.48 REMARK 500 6 LYS A 70 82.79 -28.31 REMARK 500 6 THR A 71 40.52 -20.48 REMARK 500 6 ASN A 107 90.26 99.06 REMARK 500 7 ALA A 63 39.99 -143.58 REMARK 500 7 SER A 64 74.86 -23.62 REMARK 500 7 ASN A 66 -52.24 -137.29 REMARK 500 7 PRO A 67 -168.21 -68.56 REMARK 500 7 ASN A 107 73.70 62.28 REMARK 500 7 SER A 109 92.11 -166.11 REMARK 500 7 ALA A 111 -40.54 46.98 REMARK 500 7 ARG A 144 -73.96 -84.83 REMARK 500 7 SER A 145 5.04 52.47 REMARK 500 8 PRO A 65 -8.63 -58.53 REMARK 500 8 ASN A 107 83.53 73.58 REMARK 500 8 GLU A 129 -6.90 -57.82 REMARK 500 8 VAL A 130 -54.41 -128.14 REMARK 500 8 ARG A 142 39.88 -158.88 REMARK 500 8 ARG A 144 -20.19 179.34 REMARK 500 REMARK 500 THIS ENTRY HAS 93 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 4 TYR A 141 0.07 SIDE CHAIN REMARK 500 5 TYR A 134 0.07 SIDE CHAIN REMARK 500 9 HIS A 58 0.10 SIDE CHAIN REMARK 500 12 TYR A 141 0.09 SIDE CHAIN REMARK 500 14 TYR A 141 0.08 SIDE CHAIN REMARK 500 15 TYR A 141 0.07 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 12 GLU A 103 13.00 REMARK 500 13 GLU A 101 -10.68 REMARK 500 REMARK 500 REMARK: NULL DBREF 1BR0 A 27 146 UNP P32851 STX1A_RAT 27 146 SEQADV 1BR0 SER A 145 UNP P32851 CYS 145 ENGINEERED MUTATION SEQRES 1 A 120 ASP ARG PHE MET ASP GLU PHE PHE GLU GLN VAL GLU GLU SEQRES 2 A 120 ILE ARG GLY PHE ILE ASP LYS ILE ALA GLU ASN VAL GLU SEQRES 3 A 120 GLU VAL LYS ARG LYS HIS SER ALA ILE LEU ALA SER PRO SEQRES 4 A 120 ASN PRO ASP GLU LYS THR LYS GLU GLU LEU GLU GLU LEU SEQRES 5 A 120 MET SER ASP ILE LYS LYS THR ALA ASN LYS VAL ARG SER SEQRES 6 A 120 LYS LEU LYS SER ILE GLU GLN SER ILE GLU GLN GLU GLU SEQRES 7 A 120 GLY LEU ASN ARG SER SER ALA ASP LEU ARG ILE ARG LYS SEQRES 8 A 120 THR GLN HIS SER THR LEU SER ARG LYS PHE VAL GLU VAL SEQRES 9 A 120 MET SER GLU TYR ASN ALA THR GLN SER ASP TYR ARG GLU SEQRES 10 A 120 ARG SER LYS HELIX 1 1 ARG A 28 ILE A 61 1 34 HELIX 2 2 LEU A 75 GLU A 104 1 30 HELIX 3 3 ASP A 112 ARG A 142 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 - v 3 2 Bytes