HEADER TRANSFERASE 02-SEP-97 1AUV
TITLE STRUCTURE OF THE C DOMAIN OF SYNAPSIN IA FROM BOVINE BRAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SYNAPSIN IA;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 110 - 420;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 CELL_LINE: B834;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: B834 (DE3)
KEYWDS SYNAPSE, PHOSPHORYLATION, SYNAPSIN IA C-DOMAIN, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.ESSER,C.WANG,J.DEISENHOFER
REVDAT 4 15-FEB-12 1AUV 1 HEADER
REVDAT 3 13-JUL-11 1AUV 1 VERSN
REVDAT 2 24-FEB-09 1AUV 1 VERSN
REVDAT 1 18-MAR-98 1AUV 0
JRNL AUTH L.ESSER,C.R.WANG,M.HOSAKA,C.S.SMAGULA,T.C.SUDHOF,
JRNL AUTH 2 J.DEISENHOFER
JRNL TITL SYNAPSIN I IS STRUCTURALLY SIMILAR TO ATP-UTILIZING ENZYMES.
JRNL REF EMBO J. V. 17 977 1998
JRNL REFN ISSN 0261-4189
JRNL PMID 9463376
JRNL DOI 10.1093/EMBOJ/17.4.977
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.R.WANG,L.ESSER,C.S.SMAGULA,T.C.SUDHOF,J.DEISENHOFER
REMARK 1 TITL IDENTIFICATION, EXPRESSION, AND CRYSTALLIZATION OF THE
REMARK 1 TITL 2 PROTEASE-RESISTANT CONSERVED DOMAIN OF SYNAPSIN I
REMARK 1 REF PROTEIN SCI. V. 6 2264 1997
REMARK 1 REFN ISSN 0961-8368
REMARK 1 REFERENCE 2
REMARK 1 AUTH T.C.SUDHOF,A.J.CZERNIK,H.T.KAO,K.TAKEI,P.A.JOHNSTON,
REMARK 1 AUTH 2 A.HORIUCHI,S.D.KANAZIR,M.A.WAGNER,M.S.PERIN,P.DE CAMILLI,
REMARK 1 AUTH 3 P.GREENGARD
REMARK 1 TITL SYNAPSINS: MOSAICS OF SHARED AND INDIVIDUAL DOMAINS IN A
REMARK 1 TITL 2 FAMILY OF SYNAPTIC VESICLE PHOSPHOPROTEINS
REMARK 1 REF SCIENCE V. 245 1474 1989
REMARK 1 REFN ISSN 0036-8075
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1000000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0010
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 81.4
REMARK 3 NUMBER OF REFLECTIONS : 52329
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 5178
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.28
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 54.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5202
REMARK 3 BIN R VALUE (WORKING SET) : 0.2870
REMARK 3 BIN FREE R VALUE : 0.3080
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 600
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.013
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4636
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 161
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.27
REMARK 3 ESD FROM SIGMAA (A) : 0.32
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.33
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.30
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 1.60
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.38
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 3.400 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 5.420 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.490 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 5.130 ; 2.500
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PARHCSDX_ACE_LE.PRO
REMARK 3 PARAMETER FILE 2 : HT_OT.INP
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX_ACE_LE.PRO
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 1AUV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : OCT-95
REMARK 200 TEMPERATURE (KELVIN) : 130
REMARK 200 PH : 7.25
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : FUJI
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55873
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 74.3
REMARK 200 DATA REDUNDANCY : 1.900
REMARK 200 R MERGE (I) : 0.04800
REMARK 200 R SYM (I) : 0.04800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.22
REMARK 200 COMPLETENESS FOR SHELL (%) : 48.0
REMARK 200 DATA REDUNDANCY IN SHELL : 1.58
REMARK 200 R MERGE FOR SHELL (I) : 0.11300
REMARK 200 R SYM FOR SHELL (I) : 0.11300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: MLPHARE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: DATA WERE COLLECTED USING THE INVERSE BEAM METHOD
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM 5 % PEG
REMARK 280 4000, 50 MM HEPES, PH 7.25 AT 26 DEG. CELSIUS., TEMPERATURE 299K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 120.62667
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 60.31333
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 60.31333
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 120.62667
REMARK 290
REMARK 290 REMARK: NULL
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 350 BIOMT1 2 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 110
REMARK 465 ALA A 111
REMARK 465 SER A 330
REMARK 465 VAL A 331
REMARK 465 SER A 332
REMARK 465 GLY A 333
REMARK 465 ASN A 334
REMARK 465 TRP A 335
REMARK 465 LYS A 336
REMARK 465 THR A 337
REMARK 465 ASN A 338
REMARK 465 THR A 339
REMARK 465 GLY A 340
REMARK 465 SER A 341
REMARK 465 ALA A 342
REMARK 465 MSE A 343
REMARK 465 LEU A 418
REMARK 465 PRO A 419
REMARK 465 ARG A 420
REMARK 465 THR B 329
REMARK 465 SER B 330
REMARK 465 VAL B 331
REMARK 465 SER B 332
REMARK 465 GLY B 333
REMARK 465 ASN B 334
REMARK 465 TRP B 335
REMARK 465 LYS B 336
REMARK 465 THR B 337
REMARK 465 ASN B 338
REMARK 465 THR B 339
REMARK 465 GLY B 340
REMARK 465 SER B 341
REMARK 465 ALA B 342
REMARK 465 MSE B 343
REMARK 465 LEU B 418
REMARK 465 PRO B 419
REMARK 465 ARG B 420
REMARK 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 VAL A 167
REMARK 475 LEU A 168
REMARK 475 ARG A 169
REMARK 475 ASN A 170
REMARK 475 GLY A 171
REMARK 475 VAL A 172
REMARK 475 LYS A 173
REMARK 475 VAL A 174
REMARK 475 VAL A 175
REMARK 475 MSE A 192
REMARK 475 ALA A 193
REMARK 475 ARG A 194
REMARK 475 ASN A 195
REMARK 475 GLY A 196
REMARK 475 VAL B 167
REMARK 475 LEU B 168
REMARK 475 ARG B 169
REMARK 475 ASN B 170
REMARK 475 GLY B 171
REMARK 475 VAL B 172
REMARK 475 LYS B 173
REMARK 475 VAL B 174
REMARK 475 MSE B 192
REMARK 475 ALA B 193
REMARK 475 ARG B 194
REMARK 475 ASN B 195
REMARK 475 GLY B 196
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 GLU A 138 -59.96 -121.06
REMARK 500 GLU A 166 -88.38 90.85
REMARK 500 VAL A 167 -72.39 74.50
REMARK 500 ARG A 169 -167.24 -176.20
REMARK 500 LYS A 173 122.70 68.75
REMARK 500 MSE A 192 12.25 -66.97
REMARK 500 ARG A 194 70.15 39.14
REMARK 500 ASN A 195 -64.82 175.24
REMARK 500 HIS A 255 -36.74 -35.77
REMARK 500 LYS A 256 -58.92 -27.33
REMARK 500 THR A 262 -16.67 -46.81
REMARK 500 ASP B 150 29.09 -79.34
REMARK 500 GLU B 166 33.21 -148.56
REMARK 500 VAL B 167 102.22 -58.54
REMARK 500 ASN B 170 -55.23 75.42
REMARK 500 ASN B 195 30.55 72.70
REMARK 500 PRO B 253 -9.97 -56.75
REMARK 500 ASN B 254 -175.34 178.28
REMARK 500 ALA B 273 -169.93 -118.04
REMARK 500 HIS B 274 178.13 176.56
REMARK 500 LYS B 299 27.40 48.67
REMARK 500 HIS B 398 31.86 -73.58
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 TYR A 198 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 GLU A 166 24.7 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B2154 DISTANCE = 5.23 ANGSTROMS
DBREF 1AUV A 110 420 UNP P17599 SYN1_BOVIN 110 420
DBREF 1AUV B 110 420 UNP P17599 SYN1_BOVIN 110 420
SEQADV 1AUV MSE A 165 UNP P17599 MET 165 MODIFIED RESIDUE
SEQADV 1AUV MSE A 192 UNP P17599 MET 192 MODIFIED RESIDUE
SEQADV 1AUV MSE A 232 UNP P17599 MET 232 MODIFIED RESIDUE
SEQADV 1AUV MSE A 258 UNP P17599 MET 258 MODIFIED RESIDUE
SEQADV 1AUV MSE A 270 UNP P17599 MET 270 MODIFIED RESIDUE
SEQADV 1AUV MSE A 277 UNP P17599 MET 277 MODIFIED RESIDUE
SEQADV 1AUV MSE A 327 UNP P17599 MET 327 MODIFIED RESIDUE
SEQADV 1AUV MSE A 343 UNP P17599 MET 343 CONFLICT
SEQADV 1AUV MSE A 349 UNP P17599 MET 349 MODIFIED RESIDUE
SEQADV 1AUV MSE A 392 UNP P17599 MET 392 MODIFIED RESIDUE
SEQADV 1AUV MSE A 414 UNP P17599 MET 414 MODIFIED RESIDUE
SEQADV 1AUV MSE B 165 UNP P17599 MET 165 MODIFIED RESIDUE
SEQADV 1AUV MSE B 192 UNP P17599 MET 192 MODIFIED RESIDUE
SEQADV 1AUV MSE B 232 UNP P17599 MET 232 MODIFIED RESIDUE
SEQADV 1AUV MSE B 258 UNP P17599 MET 258 MODIFIED RESIDUE
SEQADV 1AUV MSE B 270 UNP P17599 MET 270 MODIFIED RESIDUE
SEQADV 1AUV MSE B 277 UNP P17599 MET 277 MODIFIED RESIDUE
SEQADV 1AUV MSE B 327 UNP P17599 MET 327 MODIFIED RESIDUE
SEQADV 1AUV MSE B 343 UNP P17599 MET 343 CONFLICT
SEQADV 1AUV MSE B 349 UNP P17599 MET 349 MODIFIED RESIDUE
SEQADV 1AUV MSE B 392 UNP P17599 MET 392 MODIFIED RESIDUE
SEQADV 1AUV MSE B 414 UNP P17599 MET 414 MODIFIED RESIDUE
SEQRES 1 A 311 GLY ALA ALA ALA ARG VAL LEU LEU VAL ILE ASP GLU PRO
SEQRES 2 A 311 HIS THR ASP TRP ALA LYS TYR PHE LYS GLY LYS LYS ILE
SEQRES 3 A 311 HIS GLY GLU ILE ASP ILE LYS VAL GLU GLN ALA GLU PHE
SEQRES 4 A 311 SER ASP LEU ASN LEU VAL ALA HIS ALA ASN GLY GLY PHE
SEQRES 5 A 311 SER VAL ASP MSE GLU VAL LEU ARG ASN GLY VAL LYS VAL
SEQRES 6 A 311 VAL ARG SER LEU LYS PRO ASP PHE VAL LEU ILE ARG GLN
SEQRES 7 A 311 HIS ALA PHE SER MSE ALA ARG ASN GLY ASP TYR ARG SER
SEQRES 8 A 311 LEU VAL ILE GLY LEU GLN TYR ALA GLY ILE PRO SER ILE
SEQRES 9 A 311 ASN SER LEU HIS SER VAL TYR ASN PHE CYS ASP LYS PRO
SEQRES 10 A 311 TRP VAL PHE ALA GLN MSE VAL ARG LEU HIS LYS LYS LEU
SEQRES 11 A 311 GLY THR GLU GLU PHE PRO LEU ILE ASN GLN THR PHE TYR
SEQRES 12 A 311 PRO ASN HIS LYS GLU MSE LEU SER SER THR THR TYR PRO
SEQRES 13 A 311 VAL VAL VAL LYS MSE GLY HIS ALA HIS SER GLY MSE GLY
SEQRES 14 A 311 LYS VAL LYS VAL ASP ASN GLN HIS ASP PHE GLN ASP ILE
SEQRES 15 A 311 ALA SER VAL VAL ALA LEU THR LYS THR TYR ALA THR THR
SEQRES 16 A 311 GLU PRO PHE ILE ASP ALA LYS TYR ASP VAL ARG ILE GLN
SEQRES 17 A 311 LYS ILE GLY GLN ASN TYR LYS ALA TYR MSE ARG THR SER
SEQRES 18 A 311 VAL SER GLY ASN TRP LYS THR ASN THR GLY SER ALA MSE
SEQRES 19 A 311 LEU GLU GLN ILE ALA MSE SER ASP ARG TYR LYS LEU TRP
SEQRES 20 A 311 VAL ASP THR CYS SER GLU ILE PHE GLY GLY LEU ASP ILE
SEQRES 21 A 311 CYS ALA VAL GLU ALA LEU HIS GLY LYS ASP GLY ARG ASP
SEQRES 22 A 311 HIS ILE ILE GLU VAL VAL GLY SER SER MSE PRO LEU ILE
SEQRES 23 A 311 GLY ASP HIS GLN ASP GLU ASP LYS GLN LEU ILE VAL GLU
SEQRES 24 A 311 LEU VAL VAL ASN LYS MSE ALA GLN ALA LEU PRO ARG
SEQRES 1 B 311 GLY ALA ALA ALA ARG VAL LEU LEU VAL ILE ASP GLU PRO
SEQRES 2 B 311 HIS THR ASP TRP ALA LYS TYR PHE LYS GLY LYS LYS ILE
SEQRES 3 B 311 HIS GLY GLU ILE ASP ILE LYS VAL GLU GLN ALA GLU PHE
SEQRES 4 B 311 SER ASP LEU ASN LEU VAL ALA HIS ALA ASN GLY GLY PHE
SEQRES 5 B 311 SER VAL ASP MSE GLU VAL LEU ARG ASN GLY VAL LYS VAL
SEQRES 6 B 311 VAL ARG SER LEU LYS PRO ASP PHE VAL LEU ILE ARG GLN
SEQRES 7 B 311 HIS ALA PHE SER MSE ALA ARG ASN GLY ASP TYR ARG SER
SEQRES 8 B 311 LEU VAL ILE GLY LEU GLN TYR ALA GLY ILE PRO SER ILE
SEQRES 9 B 311 ASN SER LEU HIS SER VAL TYR ASN PHE CYS ASP LYS PRO
SEQRES 10 B 311 TRP VAL PHE ALA GLN MSE VAL ARG LEU HIS LYS LYS LEU
SEQRES 11 B 311 GLY THR GLU GLU PHE PRO LEU ILE ASN GLN THR PHE TYR
SEQRES 12 B 311 PRO ASN HIS LYS GLU MSE LEU SER SER THR THR TYR PRO
SEQRES 13 B 311 VAL VAL VAL LYS MSE GLY HIS ALA HIS SER GLY MSE GLY
SEQRES 14 B 311 LYS VAL LYS VAL ASP ASN GLN HIS ASP PHE GLN ASP ILE
SEQRES 15 B 311 ALA SER VAL VAL ALA LEU THR LYS THR TYR ALA THR THR
SEQRES 16 B 311 GLU PRO PHE ILE ASP ALA LYS TYR ASP VAL ARG ILE GLN
SEQRES 17 B 311 LYS ILE GLY GLN ASN TYR LYS ALA TYR MSE ARG THR SER
SEQRES 18 B 311 VAL SER GLY ASN TRP LYS THR ASN THR GLY SER ALA MSE
SEQRES 19 B 311 LEU GLU GLN ILE ALA MSE SER ASP ARG TYR LYS LEU TRP
SEQRES 20 B 311 VAL ASP THR CYS SER GLU ILE PHE GLY GLY LEU ASP ILE
SEQRES 21 B 311 CYS ALA VAL GLU ALA LEU HIS GLY LYS ASP GLY ARG ASP
SEQRES 22 B 311 HIS ILE ILE GLU VAL VAL GLY SER SER MSE PRO LEU ILE
SEQRES 23 B 311 GLY ASP HIS GLN ASP GLU ASP LYS GLN LEU ILE VAL GLU
SEQRES 24 B 311 LEU VAL VAL ASN LYS MSE ALA GLN ALA LEU PRO ARG
MODRES 1AUV MSE A 165 MET SELENOMETHIONINE
MODRES 1AUV MSE A 192 MET SELENOMETHIONINE
MODRES 1AUV MSE A 232 MET SELENOMETHIONINE
MODRES 1AUV MSE A 258 MET SELENOMETHIONINE
MODRES 1AUV MSE A 270 MET SELENOMETHIONINE
MODRES 1AUV MSE A 277 MET SELENOMETHIONINE
MODRES 1AUV MSE A 327 MET SELENOMETHIONINE
MODRES 1AUV MSE A 349 MET SELENOMETHIONINE
MODRES 1AUV MSE A 392 MET SELENOMETHIONINE
MODRES 1AUV MSE A 414 MET SELENOMETHIONINE
MODRES 1AUV MSE B 165 MET SELENOMETHIONINE
MODRES 1AUV MSE B 192 MET SELENOMETHIONINE
MODRES 1AUV MSE B 232 MET SELENOMETHIONINE
MODRES 1AUV MSE B 258 MET SELENOMETHIONINE
MODRES 1AUV MSE B 270 MET SELENOMETHIONINE
MODRES 1AUV MSE B 277 MET SELENOMETHIONINE
MODRES 1AUV MSE B 327 MET SELENOMETHIONINE
MODRES 1AUV MSE B 349 MET SELENOMETHIONINE
MODRES 1AUV MSE B 392 MET SELENOMETHIONINE
MODRES 1AUV MSE B 414 MET SELENOMETHIONINE
HET MSE A 165 8
HET MSE A 192 8
HET MSE A 232 8
HET MSE A 258 8
HET MSE A 270 8
HET MSE A 277 8
HET MSE A 327 8
HET MSE A 349 8
HET MSE A 392 8
HET MSE A 414 8
HET MSE B 165 8
HET MSE B 192 8
HET MSE B 232 8
HET MSE B 258 8
HET MSE B 270 8
HET MSE B 277 8
HET MSE B 327 8
HET MSE B 349 8
HET MSE B 392 8
HET MSE B 414 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 20(C5 H11 N O2 SE)
FORMUL 3 HOH *161(H2 O)
HELIX 1 1 TRP A 126 PHE A 130 1 5
HELIX 2 2 ILE A 135 GLY A 137 5 3
HELIX 3 3 PHE A 148 ASP A 150 5 3
HELIX 4 4 ARG A 199 TYR A 207 1 9
HELIX 5 5 LEU A 216 PHE A 222 1 7
HELIX 6 6 LYS A 225 LEU A 239 1 15
HELIX 7 7 GLN A 285 THR A 298 1 14
HELIX 8 8 ASP A 351 GLY A 365 1 15
HELIX 9 9 GLN A 399 ALA A 415 1 17
HELIX 10 10 TRP B 126 PHE B 130 1 5
HELIX 11 11 ILE B 135 GLY B 137 5 3
HELIX 12 12 ARG B 199 TYR B 207 1 9
HELIX 13 13 LEU B 216 ASN B 221 1 6
HELIX 14 14 LYS B 225 LEU B 239 1 15
HELIX 15 15 GLN B 285 THR B 298 1 14
HELIX 16 16 ASP B 351 GLY B 365 1 15
HELIX 17 17 GLN B 399 ALA B 415 1 17
SHEET 1 A 3 ILE A 141 ALA A 146 0
SHEET 2 A 3 ARG A 114 ILE A 119 1 N ARG A 114 O LYS A 142
SHEET 3 A 3 PHE A 182 ILE A 185 1 N PHE A 182 O LEU A 117
SHEET 1 B 2 ASN A 152 ALA A 155 0
SHEET 2 B 2 PHE A 161 ASP A 164 -1 N ASP A 164 O ASN A 152
SHEET 1 C 4 THR A 250 TYR A 252 0
SHEET 2 C 4 ALA A 302 PRO A 306 -1 N THR A 304 O THR A 250
SHEET 3 C 4 VAL A 266 LYS A 269 -1 N LYS A 269 O THR A 303
SHEET 4 C 4 VAL A 280 VAL A 282 -1 N VAL A 282 O VAL A 266
SHEET 1 D 4 ASN A 322 TYR A 326 0
SHEET 2 D 4 ALA A 310 ILE A 319 -1 N ILE A 319 O ASN A 322
SHEET 3 D 4 ILE A 369 GLY A 377 -1 N HIS A 376 O LYS A 311
SHEET 4 D 4 ASP A 382 VAL A 388 -1 N VAL A 388 O ALA A 371
SHEET 1 E 4 ILE B 141 ALA B 146 0
SHEET 2 E 4 ARG B 114 ILE B 119 1 N ARG B 114 O LYS B 142
SHEET 3 E 4 PHE B 182 ILE B 185 1 N PHE B 182 O LEU B 117
SHEET 4 E 4 PRO B 211 ILE B 213 1 N PRO B 211 O VAL B 183
SHEET 1 F 2 ASN B 152 ALA B 155 0
SHEET 2 F 2 PHE B 161 ASP B 164 -1 N ASP B 164 O ASN B 152
SHEET 1 G 4 THR B 250 TYR B 252 0
SHEET 2 G 4 ALA B 302 PRO B 306 -1 N THR B 304 O THR B 250
SHEET 3 G 4 VAL B 266 LYS B 269 -1 N LYS B 269 O THR B 303
SHEET 4 G 4 VAL B 280 VAL B 282 -1 N VAL B 282 O VAL B 266
SHEET 1 H 4 ASN B 322 TYR B 326 0
SHEET 2 H 4 ALA B 310 ILE B 319 -1 N ILE B 319 O ASN B 322
SHEET 3 H 4 ILE B 369 GLY B 377 -1 N HIS B 376 O LYS B 311
SHEET 4 H 4 ASP B 382 VAL B 388 -1 N VAL B 388 O ALA B 371
LINK N MSE A 165 C ASP A 164 1555 1555 1.33
LINK C MSE A 165 N GLU A 166 1555 1555 1.34
LINK N MSE A 192 C SER A 191 1555 1555 1.33
LINK C MSE A 192 N ALA A 193 1555 1555 1.33
LINK N MSE A 232 C GLN A 231 1555 1555 1.32
LINK C MSE A 232 N VAL A 233 1555 1555 1.33
LINK N MSE A 258 C GLU A 257 1555 1555 1.33
LINK C MSE A 258 N LEU A 259 1555 1555 1.34
LINK N MSE A 270 C LYS A 269 1555 1555 1.32
LINK C MSE A 270 N GLY A 271 1555 1555 1.34
LINK N MSE A 277 C GLY A 276 1555 1555 1.33
LINK C MSE A 277 N GLY A 278 1555 1555 1.33
LINK N MSE A 327 C TYR A 326 1555 1555 1.32
LINK C MSE A 327 N ARG A 328 1555 1555 1.33
LINK N MSE A 349 C ALA A 348 1555 1555 1.33
LINK C MSE A 349 N SER A 350 1555 1555 1.31
LINK N MSE A 392 C SER A 391 1555 1555 1.33
LINK C MSE A 392 N PRO A 393 1555 1555 1.35
LINK N MSE A 414 C LYS A 413 1555 1555 1.33
LINK C MSE A 414 N ALA A 415 1555 1555 1.33
LINK N MSE B 165 C ASP B 164 1555 1555 1.33
LINK C MSE B 165 N GLU B 166 1555 1555 1.33
LINK N MSE B 192 C SER B 191 1555 1555 1.33
LINK C MSE B 192 N ALA B 193 1555 1555 1.33
LINK N MSE B 232 C GLN B 231 1555 1555 1.33
LINK C MSE B 232 N VAL B 233 1555 1555 1.33
LINK N MSE B 258 C GLU B 257 1555 1555 1.33
LINK C MSE B 258 N LEU B 259 1555 1555 1.34
LINK N MSE B 270 C LYS B 269 1555 1555 1.33
LINK C MSE B 270 N GLY B 271 1555 1555 1.34
LINK N MSE B 277 C GLY B 276 1555 1555 1.33
LINK C MSE B 277 N GLY B 278 1555 1555 1.33
LINK N MSE B 327 C TYR B 326 1555 1555 1.33
LINK C MSE B 327 N ARG B 328 1555 1555 1.34
LINK N MSE B 349 C ALA B 348 1555 1555 1.32
LINK C MSE B 349 N SER B 350 1555 1555 1.32
LINK N MSE B 392 C SER B 391 1555 1555 1.34
LINK C MSE B 392 N PRO B 393 1555 1555 1.34
LINK N MSE B 414 C LYS B 413 1555 1555 1.32
LINK C MSE B 414 N ALA B 415 1555 1555 1.33
CISPEP 1 ILE A 213 ASN A 214 0 -0.32
CISPEP 2 TYR A 264 PRO A 265 0 -0.54
CISPEP 3 ILE B 213 ASN B 214 0 -0.15
CISPEP 4 TYR B 264 PRO B 265 0 -0.22
CRYST1 76.400 76.400 180.940 90.00 90.00 120.00 P 32 2 1 12
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 0.013089 0.007557 0.000000 0.00000
SCALE2 0.000000 0.015114 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005527 0.00000
MTRIX1 1 -0.414908 -0.346441 0.841326 61.62489 1
MTRIX2 1 -0.332841 -0.802790 -0.494717 107.25087 1
MTRIX3 1 0.846799 -0.485290 0.217774 0.29079 1
(ATOM LINES ARE NOT SHOWN.)
END