Header list of 1byn.pdb file
Complete list - b 16 2 Bytes
HEADER ENDOCYTOSIS/EXOCYTOSIS 18-OCT-98 1BYN
TITLE SOLUTION STRUCTURE OF THE CALCIUM-BOUND FIRST C2-DOMAIN OF
TITLE 2 SYNAPTOTAGMIN I
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (SYNAPTOTAGMIN I);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C2A-DOMAIN;
COMPND 5 ENGINEERED: 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 BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21-DE3
KEYWDS SYNAPTOTAGMIN, C2-DOMAIN, EXOCYTOSIS, NEUROTRANSMITTER RELEASE,
KEYWDS 2 ENDOCYTOSIS-EXOCYTOSIS COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR X.SHAO,I.FERNANDEZ,T.C.SUDHOF,J.RIZO
REVDAT 4 16-FEB-22 1BYN 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1BYN 1 VERSN
REVDAT 2 22-DEC-99 1BYN 4 HEADER COMPND REMARK JRNL
REVDAT 2 2 4 ATOM SOURCE SEQRES
REVDAT 1 21-OCT-98 1BYN 0
JRNL AUTH X.SHAO,I.FERNANDEZ,T.C.SUDHOF,J.RIZO
JRNL TITL SOLUTION STRUCTURES OF THE CA2+-FREE AND CA2+-BOUND C2A
JRNL TITL 2 DOMAIN OF SYNAPTOTAGMIN I: DOES CA2+ INDUCE A CONFORMATIONAL
JRNL TITL 3 CHANGE?
JRNL REF BIOCHEMISTRY V. 37 16106 1998
JRNL REFN ISSN 0006-2960
JRNL PMID 9819203
JRNL DOI 10.1021/BI981789H
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 1BYN 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_1000008150.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 307
REMARK 210 PH : 5.0
REMARK 210 IONIC STRENGTH : 100 MM NACL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D; 3D AND 4D HOMONUCLEAR;
REMARK 210 HETERONUCLEAR; TRIPLE RESONANCE
REMARK 210 EXPERIMENTS
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY 500
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DISCOVER, NMRCHITECT
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : FEWEST RESTRAINTS VIOLATIONS
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: 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 HIS A 198 CG HIS A 198 CD2 0.057
REMARK 500 1 HIS A 237 CG HIS A 237 CD2 0.071
REMARK 500 1 HIS A 254 CG HIS A 254 CD2 0.060
REMARK 500 2 HIS A 198 CG HIS A 198 CD2 0.062
REMARK 500 2 HIS A 237 CG HIS A 237 CD2 0.068
REMARK 500 2 HIS A 254 CG HIS A 254 CD2 0.059
REMARK 500 3 HIS A 237 CG HIS A 237 CD2 0.071
REMARK 500 3 HIS A 254 CG HIS A 254 CD2 0.059
REMARK 500 4 HIS A 198 CG HIS A 198 CD2 0.058
REMARK 500 4 HIS A 237 CG HIS A 237 CD2 0.070
REMARK 500 4 HIS A 254 CG HIS A 254 CD2 0.060
REMARK 500 5 HIS A 198 CG HIS A 198 CD2 0.063
REMARK 500 5 HIS A 237 CG HIS A 237 CD2 0.068
REMARK 500 5 HIS A 254 CG HIS A 254 CD2 0.059
REMARK 500 6 HIS A 198 CG HIS A 198 CD2 0.056
REMARK 500 6 HIS A 237 CG HIS A 237 CD2 0.067
REMARK 500 6 HIS A 254 CG HIS A 254 CD2 0.060
REMARK 500 7 HIS A 198 CG HIS A 198 CD2 0.060
REMARK 500 7 HIS A 237 CG HIS A 237 CD2 0.071
REMARK 500 7 HIS A 254 CG HIS A 254 CD2 0.061
REMARK 500 8 HIS A 198 CG HIS A 198 CD2 0.057
REMARK 500 8 HIS A 237 CG HIS A 237 CD2 0.069
REMARK 500 8 HIS A 254 CG HIS A 254 CD2 0.060
REMARK 500 9 HIS A 198 CG HIS A 198 CD2 0.058
REMARK 500 9 HIS A 237 CG HIS A 237 CD2 0.066
REMARK 500 9 HIS A 254 CG HIS A 254 CD2 0.059
REMARK 500 10 HIS A 198 CG HIS A 198 CD2 0.057
REMARK 500 10 HIS A 237 CG HIS A 237 CD2 0.069
REMARK 500 10 HIS A 254 CG HIS A 254 CD2 0.061
REMARK 500 11 HIS A 198 CG HIS A 198 CD2 0.059
REMARK 500 11 HIS A 237 CG HIS A 237 CD2 0.068
REMARK 500 11 HIS A 254 CG HIS A 254 CD2 0.059
REMARK 500 12 HIS A 198 CG HIS A 198 CD2 0.060
REMARK 500 12 HIS A 237 CG HIS A 237 CD2 0.069
REMARK 500 12 HIS A 254 CG HIS A 254 CD2 0.060
REMARK 500 13 HIS A 198 CG HIS A 198 CD2 0.059
REMARK 500 13 HIS A 237 CG HIS A 237 CD2 0.069
REMARK 500 13 HIS A 254 CG HIS A 254 CD2 0.058
REMARK 500 14 HIS A 237 CG HIS A 237 CD2 0.069
REMARK 500 14 HIS A 254 CG HIS A 254 CD2 0.060
REMARK 500 15 HIS A 198 CG HIS A 198 CD2 0.056
REMARK 500 15 HIS A 237 CG HIS A 237 CD2 0.068
REMARK 500 15 HIS A 254 CG HIS A 254 CD2 0.060
REMARK 500 16 HIS A 198 CG HIS A 198 CD2 0.055
REMARK 500 16 HIS A 237 CG HIS A 237 CD2 0.071
REMARK 500 16 HIS A 254 CG HIS A 254 CD2 0.059
REMARK 500 17 HIS A 198 CG HIS A 198 CD2 0.054
REMARK 500 17 HIS A 237 CG HIS A 237 CD2 0.068
REMARK 500 17 HIS A 254 CG HIS A 254 CD2 0.068
REMARK 500 18 HIS A 237 CG HIS A 237 CD2 0.069
REMARK 500
REMARK 500 THIS ENTRY HAS 56 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 HIS A 198 ND1 - CE1 - NE2 ANGL. DEV. = 8.7 DEGREES
REMARK 500 1 ARG A 199 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 1 ARG A 233 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 1 HIS A 237 ND1 - CE1 - NE2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 1 PHE A 252 N - CA - CB ANGL. DEV. = -11.1 DEGREES
REMARK 500 1 HIS A 254 ND1 - CE1 - NE2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 1 ARG A 260 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 2 HIS A 198 ND1 - CE1 - NE2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 2 ARG A 199 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 2 ARG A 233 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 2 HIS A 237 ND1 - CE1 - NE2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 2 VAL A 245 CA - CB - CG1 ANGL. DEV. = 9.5 DEGREES
REMARK 500 2 HIS A 254 ND1 - CE1 - NE2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 2 ARG A 260 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 3 HIS A 198 ND1 - CE1 - NE2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 3 ARG A 199 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 3 ARG A 233 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 3 HIS A 237 ND1 - CE1 - NE2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 3 HIS A 254 ND1 - CE1 - NE2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 3 ARG A 260 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 4 ASP A 178 N - CA - CB ANGL. DEV. = -12.0 DEGREES
REMARK 500 4 HIS A 198 ND1 - CE1 - NE2 ANGL. DEV. = 8.7 DEGREES
REMARK 500 4 ARG A 199 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 4 ARG A 233 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 4 HIS A 237 ND1 - CE1 - NE2 ANGL. DEV. = 8.7 DEGREES
REMARK 500 4 HIS A 254 ND1 - CE1 - NE2 ANGL. DEV. = 8.7 DEGREES
REMARK 500 4 ARG A 260 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 5 HIS A 198 ND1 - CE1 - NE2 ANGL. DEV. = 8.7 DEGREES
REMARK 500 5 ARG A 199 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 5 THR A 201 CA - CB - CG2 ANGL. DEV. = 8.5 DEGREES
REMARK 500 5 ARG A 233 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 5 HIS A 237 ND1 - CE1 - NE2 ANGL. DEV. = 8.7 DEGREES
REMARK 500 5 HIS A 254 ND1 - CE1 - NE2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 5 ARG A 260 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 6 HIS A 198 ND1 - CE1 - NE2 ANGL. DEV. = 8.7 DEGREES
REMARK 500 6 ARG A 199 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 6 ARG A 233 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 6 HIS A 237 ND1 - CE1 - NE2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 6 VAL A 245 CA - CB - CG2 ANGL. DEV. = 9.4 DEGREES
REMARK 500 6 HIS A 254 CB - CA - C ANGL. DEV. = 12.1 DEGREES
REMARK 500 6 HIS A 254 ND1 - CE1 - NE2 ANGL. DEV. = 8.7 DEGREES
REMARK 500 6 ARG A 260 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 6 ALA A 265 CB - CA - C ANGL. DEV. = 11.2 DEGREES
REMARK 500 7 HIS A 198 ND1 - CE1 - NE2 ANGL. DEV. = 8.7 DEGREES
REMARK 500 7 ARG A 199 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 7 ARG A 233 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 7 HIS A 237 ND1 - CE1 - NE2 ANGL. DEV. = 8.7 DEGREES
REMARK 500 7 HIS A 254 ND1 - CE1 - NE2 ANGL. DEV. = 8.7 DEGREES
REMARK 500 7 ARG A 260 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 8 HIS A 198 ND1 - CE1 - NE2 ANGL. DEV. = 8.9 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 135 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 ASN A 156 62.26 62.29
REMARK 500 1 ILE A 163 -70.41 -92.81
REMARK 500 1 ASP A 178 76.70 -111.91
REMARK 500 1 LYS A 189 71.65 73.51
REMARK 500 1 ARG A 233 -17.68 58.72
REMARK 500 1 PHE A 234 -57.00 -150.63
REMARK 500 1 HIS A 254 -122.04 -115.86
REMARK 500 2 ASN A 156 74.87 66.84
REMARK 500 2 ILE A 163 -73.07 -95.07
REMARK 500 2 MET A 173 68.21 69.66
REMARK 500 2 ASP A 178 77.24 -112.35
REMARK 500 2 LYS A 189 66.03 71.34
REMARK 500 2 LYS A 200 61.33 66.29
REMARK 500 3 ASN A 156 73.77 67.99
REMARK 500 3 ASP A 178 79.06 -113.83
REMARK 500 3 LYS A 189 68.26 70.07
REMARK 500 3 PHE A 252 75.53 -107.66
REMARK 500 3 VAL A 255 111.52 38.28
REMARK 500 4 ASN A 156 74.28 66.83
REMARK 500 4 ILE A 163 -66.62 -91.76
REMARK 500 4 ASP A 172 -152.73 -122.31
REMARK 500 4 LYS A 189 70.79 73.53
REMARK 500 4 ASN A 207 64.06 37.14
REMARK 500 4 ILE A 240 -76.09 -93.87
REMARK 500 4 PHE A 252 73.07 -105.13
REMARK 500 4 HIS A 254 -127.50 -120.05
REMARK 500 5 ASN A 156 72.45 68.10
REMARK 500 5 LYS A 189 69.12 73.58
REMARK 500 5 ARG A 233 -96.81 51.02
REMARK 500 5 ILE A 240 -70.50 -81.02
REMARK 500 6 ASN A 156 72.18 67.11
REMARK 500 6 ILE A 163 -69.94 -94.03
REMARK 500 6 LYS A 189 72.76 71.40
REMARK 500 6 HIS A 254 -125.12 -112.20
REMARK 500 6 ALA A 265 -132.87 -98.80
REMARK 500 6 GLU A 266 85.00 61.00
REMARK 500 7 ASN A 156 72.65 64.84
REMARK 500 7 ILE A 163 -72.23 -102.95
REMARK 500 7 ASP A 172 -149.94 -95.62
REMARK 500 7 LYS A 190 -66.46 -97.08
REMARK 500 7 HIS A 198 79.54 -101.40
REMARK 500 7 HIS A 254 -124.49 -116.98
REMARK 500 8 ASN A 156 71.54 67.94
REMARK 500 8 ASP A 178 79.03 -108.87
REMARK 500 8 LYS A 189 76.43 76.03
REMARK 500 8 ASN A 207 63.57 34.22
REMARK 500 8 ILE A 240 -75.07 -92.02
REMARK 500 8 HIS A 254 -122.30 -116.72
REMARK 500 8 GLU A 266 75.45 -106.30
REMARK 500 9 ASN A 156 68.70 68.68
REMARK 500
REMARK 500 THIS ENTRY HAS 130 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 5 TYR A 147 0.10 SIDE CHAIN
REMARK 500 12 TYR A 147 0.06 SIDE CHAIN
REMARK 500 18 TYR A 147 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 273 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU A 171 O
REMARK 620 2 ASP A 172 OD1 68.9
REMARK 620 3 ASP A 230 OD1 129.2 66.2
REMARK 620 4 ASP A 230 OD2 97.2 62.7 40.7
REMARK 620 5 ASP A 232 OD2 136.7 124.6 89.3 125.9
REMARK 620 6 ASP A 232 OD1 108.9 82.9 87.9 125.2 45.7
REMARK 620 7 ASP A 238 OD2 80.7 140.5 149.9 149.0 64.4 83.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 272 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 172 OD1
REMARK 620 2 ASP A 172 OD2 45.7
REMARK 620 3 ASP A 178 OD2 110.1 112.3
REMARK 620 4 ASP A 230 OD1 73.7 119.4 87.6
REMARK 620 5 PHE A 231 O 148.3 165.9 66.4 74.7
REMARK 620 6 ASP A 232 OD1 83.0 75.1 166.8 98.2 103.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 274 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 232 OD2
REMARK 620 2 SER A 235 OG 107.2
REMARK 620 3 LYS A 236 O 87.9 85.9
REMARK 620 4 ASP A 238 OD1 87.6 152.8 71.6
REMARK 620 5 ASP A 238 OD2 64.2 161.9 108.8 45.3
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 272
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 273
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 274
DBREF 1BYN A 140 267 UNP P21707 SYT1_RAT 140 267
SEQADV 1BYN ASP A 188 UNP P21707 GLU 188 CONFLICT
SEQRES 1 A 128 GLU LYS LEU GLY LYS LEU GLN TYR SER LEU ASP TYR ASP
SEQRES 2 A 128 PHE GLN ASN ASN GLN LEU LEU VAL GLY ILE ILE GLN ALA
SEQRES 3 A 128 ALA GLU LEU PRO ALA LEU ASP MET GLY GLY THR SER ASP
SEQRES 4 A 128 PRO TYR VAL LYS VAL PHE LEU LEU PRO ASP LYS LYS LYS
SEQRES 5 A 128 LYS PHE GLU THR LYS VAL HIS ARG LYS THR LEU ASN PRO
SEQRES 6 A 128 VAL PHE ASN GLU GLN PHE THR PHE LYS VAL PRO TYR SER
SEQRES 7 A 128 GLU LEU GLY GLY LYS THR LEU VAL MET ALA VAL TYR ASP
SEQRES 8 A 128 PHE ASP ARG PHE SER LYS HIS ASP ILE ILE GLY GLU PHE
SEQRES 9 A 128 LYS VAL PRO MET ASN THR VAL ASP PHE GLY HIS VAL THR
SEQRES 10 A 128 GLU GLU TRP ARG ASP LEU GLN SER ALA GLU LYS
HET CA A 272 1
HET CA A 273 1
HET CA A 274 1
HETNAM CA CALCIUM ION
FORMUL 2 CA 3(CA 2+)
HELIX 1 1 TYR A 216 LEU A 219 1 4
HELIX 2 2 MET A 247 THR A 249 5 3
SHEET 1 A 4 VAL A 255 ASP A 261 0
SHEET 2 A 4 LYS A 144 ASP A 152 -1 N LEU A 149 O THR A 256
SHEET 3 A 4 GLN A 157 ALA A 166 -1 N ALA A 166 O LYS A 144
SHEET 4 A 4 GLU A 208 PHE A 212 -1 N PHE A 212 O LEU A 158
SHEET 1 B 3 PRO A 179 LEU A 186 0
SHEET 2 B 3 THR A 223 ASP A 230 -1 N TYR A 229 O TYR A 180
SHEET 3 B 3 ILE A 239 PRO A 246 -1 N VAL A 245 O LEU A 224
LINK O LEU A 171 CA CA A 273 1555 1555 2.79
LINK OD1 ASP A 172 CA CA A 272 1555 1555 2.81
LINK OD2 ASP A 172 CA CA A 272 1555 1555 2.82
LINK OD1 ASP A 172 CA CA A 273 1555 1555 2.83
LINK OD2 ASP A 178 CA CA A 272 1555 1555 2.81
LINK OD1 ASP A 230 CA CA A 272 1555 1555 2.81
LINK OD1 ASP A 230 CA CA A 273 1555 1555 3.31
LINK OD2 ASP A 230 CA CA A 273 1555 1555 2.84
LINK O PHE A 231 CA CA A 272 1555 1555 2.81
LINK OD1 ASP A 232 CA CA A 272 1555 1555 2.82
LINK OD2 ASP A 232 CA CA A 273 1555 1555 2.83
LINK OD1 ASP A 232 CA CA A 273 1555 1555 2.80
LINK OD2 ASP A 232 CA CA A 274 1555 1555 2.84
LINK OG SER A 235 CA CA A 274 1555 1555 2.84
LINK O LYS A 236 CA CA A 274 1555 1555 2.81
LINK OD2 ASP A 238 CA CA A 273 1555 1555 2.82
LINK OD1 ASP A 238 CA CA A 274 1555 1555 2.84
LINK OD2 ASP A 238 CA CA A 274 1555 1555 2.83
CISPEP 1 LEU A 186 PRO A 187 1 -10.16
CISPEP 2 LEU A 186 PRO A 187 2 -0.48
CISPEP 3 LEU A 186 PRO A 187 3 -4.03
CISPEP 4 LEU A 186 PRO A 187 4 1.54
CISPEP 5 LEU A 186 PRO A 187 5 4.56
CISPEP 6 LEU A 186 PRO A 187 6 -10.44
CISPEP 7 LEU A 186 PRO A 187 7 -0.25
CISPEP 8 LEU A 186 PRO A 187 8 -1.97
CISPEP 9 LEU A 186 PRO A 187 9 1.22
CISPEP 10 LEU A 186 PRO A 187 10 5.45
CISPEP 11 LEU A 186 PRO A 187 11 0.68
CISPEP 12 LEU A 186 PRO A 187 12 -4.71
CISPEP 13 LEU A 186 PRO A 187 13 -4.61
CISPEP 14 LEU A 186 PRO A 187 14 -0.09
CISPEP 15 LEU A 186 PRO A 187 15 10.05
CISPEP 16 LEU A 186 PRO A 187 16 -0.11
CISPEP 17 LEU A 186 PRO A 187 17 -5.69
CISPEP 18 LEU A 186 PRO A 187 18 -7.31
CISPEP 19 LEU A 186 PRO A 187 19 1.43
CISPEP 20 LEU A 186 PRO A 187 20 -7.93
SITE 1 AC1 5 ASP A 172 ASP A 178 ASP A 230 PHE A 231
SITE 2 AC1 5 ASP A 232
SITE 1 AC2 5 LEU A 171 ASP A 172 ASP A 230 ASP A 232
SITE 2 AC2 5 ASP A 238
SITE 1 AC3 4 ASP A 232 SER A 235 LYS A 236 ASP A 238
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 16 2 Bytes