HEADER HYDROLASE 14-JAN-01 1IO5
TITLE HYDROGEN AND HYDRATION OF HEN EGG-WHITE LYSOZYME DETERMINED BY NEUTRON
TITLE 2 DIFFRACTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYSOZYME C;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.2.1.17
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 TISSUE: EGG WHITE
KEYWDS HYDROGEN, HYDRATION, HYDROLASE
EXPDTA NEUTRON DIFFRACTION
AUTHOR N.NIIMURA,Y.MINEZAKI,T.NONAKA,J.C.CASTAGNA,F.CIPRIANI,P.HOEGHOEJ,
AUTHOR 2 M.S.LEHMANN,C.WILKINSON
REVDAT 8 25-OCT-23 1IO5 1 REMARK
REVDAT 7 07-MAR-18 1IO5 1 REMARK
REVDAT 6 04-OCT-17 1IO5 1 REMARK
REVDAT 5 13-JUL-11 1IO5 1 VERSN
REVDAT 4 24-FEB-09 1IO5 1 VERSN
REVDAT 3 01-APR-03 1IO5 1 JRNL
REVDAT 2 21-JAN-03 1IO5 1 REMARK
REVDAT 1 07-FEB-01 1IO5 0
JRNL AUTH N.NIIMURA,Y.MINEZAKI,T.NONAKA,J.C.CASTAGNA,F.CIPRIANI,
JRNL AUTH 2 P.HOGHOJ,M.S.LEHMANN,C.WILKINSON
JRNL TITL NEUTRON LAUE DIFFRACTOMETRY WITH AN IMAGING PLATE PROVIDES
JRNL TITL 2 AN EFFECTIVE DATA COLLECTION REGIME FOR NEUTRON PROTEIN
JRNL TITL 3 CRYSTALLOGRAPHY.
JRNL REF NAT.STRUCT.BIOL. V. 4 909 1997
JRNL REFN ISSN 1072-8368
JRNL PMID 9360606
JRNL DOI 10.1038/NSB1197-909
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH N.NIIMURA
REMARK 1 TITL NEUTRONS EXPAND THE FIELD OF STRUCTURAL BIOLOGY
REMARK 1 REF CURR.OPIN.STRUCT.BIOL. V. 9 602 1999
REMARK 1 REFN ISSN 0959-440X
REMARK 1 DOI 10.1016/S0959-440X(99)00012-3
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CCP4 LAUE SUITE MODIFIED FOR CYLINDER GEOMETRY (C. W
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.94
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 6700
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : 0.323
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1001
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 251
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 2.220
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1IO5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-JAN-01.
REMARK 100 THE DEPOSITION ID IS D_1000005112.
REMARK 230
REMARK 230 EXPERIMENTAL DETAILS
REMARK 230 EXPERIMENT TYPE : NEUTRON DIFFRACTION
REMARK 230 DATE OF DATA COLLECTION : 03-SEP-95
REMARK 230 TEMPERATURE (KELVIN) : NULL
REMARK 230 PH : 7.00
REMARK 230 NUMBER OF CRYSTALS USED : 1
REMARK 230
REMARK 230 NEUTRON SOURCE : NUCLEAR REACTOR
REMARK 230 BEAMLINE : NULL
REMARK 230 WAVELENGTH OR RANGE (A) : 2.9-4.0
REMARK 230 MONOCHROMATOR : NULL
REMARK 230 OPTICS : NULL
REMARK 230
REMARK 230 DETECTOR TYPE : IMAGE PLATE
REMARK 230 DETECTOR MANUFACTURER : LADI
REMARK 230 INTENSITY-INTEGRATION SOFTWARE : INTLDM, CCP4 LAUE SUITE MODIFIED
REMARK 230 FOR CYLINDER GEOMETRY (C.
REMARK 230 WILKINSON)
REMARK 230 DATA SCALING SOFTWARE : INTLDM
REMARK 230
REMARK 230 NUMBER OF UNIQUE REFLECTIONS : 6700
REMARK 230 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 230 RESOLUTION RANGE LOW (A) : 8.940
REMARK 230 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 230
REMARK 230 OVERALL.
REMARK 230 COMPLETENESS FOR RANGE (%) : 81.4
REMARK 230 DATA REDUNDANCY : 5.700
REMARK 230 R MERGE (I) : 0.16400
REMARK 230 R SYM (I) : NULL
REMARK 230 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 230
REMARK 230 IN THE HIGHEST RESOLUTION SHELL.
REMARK 230 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 230 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.48
REMARK 230 COMPLETENESS FOR SHELL (%) : 77.1
REMARK 230 DATA REDUNDANCY IN SHELL : NULL
REMARK 230 R MERGE FOR SHELL (I) : NULL
REMARK 230 R SYM FOR SHELL (I) : NULL
REMARK 230 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 230
REMARK 230 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 230 SOFTWARE USED : X-PLOR
REMARK 230 STARTING MODEL: PDB ENTRY 193L
REMARK 230
REMARK 230 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NICL2, PH 7.0, CONCENTRATION GRADIENT
REMARK 280 METHOD, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 18.55000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 40.40000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 40.40000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 27.82500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 40.40000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 40.40000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 9.27500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 40.40000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 40.40000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 27.82500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 40.40000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 40.40000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 9.27500
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 18.55000
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: 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 O DOD A 306 LIES ON A SPECIAL POSITION.
REMARK 375 O DOD A 362 LIES ON A SPECIAL POSITION.
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
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 D1 DOD A 171 D2 DOD A 197 0.44
REMARK 500 D1 DOD A 273 D2 DOD A 279 0.60
REMARK 500 D1 DOD A 267 D1 DOD A 285 0.62
REMARK 500 HZ2 TRP A 62 D2 DOD A 309 0.71
REMARK 500 D2 DOD A 326 D1 DOD A 358 0.72
REMARK 500 D2 DOD A 257 D1 DOD A 361 0.73
REMARK 500 D2 DOD A 159 D2 DOD A 218 0.82
REMARK 500 O DOD A 282 D1 DOD A 298 0.84
REMARK 500 D1 DOD A 283 D2 DOD A 361 0.88
REMARK 500 D2 DOD A 171 D2 DOD A 259 0.89
REMARK 500 D1 DOD A 219 D1 DOD A 224 0.91
REMARK 500 HD11 LEU A 8 D1 DOD A 370 0.92
REMARK 500 D1 DOD A 273 O DOD A 279 0.95
REMARK 500 D1 DOD A 139 D1 DOD A 223 0.96
REMARK 500 O DOD A 227 D2 DOD A 233 0.97
REMARK 500 D1 LYS A 1 D2 DOD A 132 0.98
REMARK 500 D2 DOD A 301 D2 DOD A 303 0.99
REMARK 500 DE ARG A 21 D1 DOD A 249 1.00
REMARK 500 D2 DOD A 232 D2 DOD A 294 1.03
REMARK 500 DE ARG A 112 O DOD A 369 1.05
REMARK 500 OE1 GLU A 7 D2 DOD A 270 1.06
REMARK 500 D2 DOD A 209 D2 DOD A 332 1.07
REMARK 500 D2 DOD A 312 D1 DOD A 315 1.08
REMARK 500 D1 DOD A 186 D2 DOD A 242 1.08
REMARK 500 D1 DOD A 183 O DOD A 376 1.11
REMARK 500 DH21 ARG A 112 D1 DOD A 369 1.12
REMARK 500 D2 DOD A 260 D2 DOD A 296 1.15
REMARK 500 D1 DOD A 165 D2 DOD A 311 1.15
REMARK 500 O DOD A 139 D1 DOD A 223 1.16
REMARK 500 D1 DOD A 155 D2 DOD A 278 1.17
REMARK 500 D2 DOD A 179 D1 DOD A 182 1.19
REMARK 500 O DOD A 283 D2 DOD A 361 1.20
REMARK 500 D2 DOD A 211 D1 DOD A 281 1.20
REMARK 500 DG1 THR A 51 DH21 ARG A 68 1.23
REMARK 500 D1 DOD A 140 O DOD A 271 1.24
REMARK 500 HZ2 TRP A 62 O DOD A 309 1.24
REMARK 500 D1 DOD A 152 O DOD A 341 1.25
REMARK 500 O DOD A 171 D2 DOD A 197 1.26
REMARK 500 D1 DOD A 331 O DOD A 340 1.27
REMARK 500 O DOD A 203 O DOD A 345 1.30
REMARK 500 HG LEU A 56 D2 DOD A 276 1.30
REMARK 500 O DOD A 302 D1 DOD A 365 1.30
REMARK 500 O DOD A 283 D2 DOD A 288 1.31
REMARK 500 O DOD A 273 D2 DOD A 279 1.31
REMARK 500 D1 DOD A 171 O DOD A 197 1.32
REMARK 500 HE3 LYS A 97 D1 DOD A 313 1.32
REMARK 500 D1 DOD A 257 D2 DOD A 298 1.32
REMARK 500 NE ARG A 21 D1 DOD A 249 1.32
REMARK 500 DE21 GLN A 121 D1 DOD A 155 1.33
REMARK 500 O DOD A 272 D1 DOD A 356 1.33
REMARK 500
REMARK 500 THIS ENTRY HAS 105 CLOSE CONTACTS
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 D1 DOD A 296 D2 DOD A 316 1554 0.58
REMARK 500 D2 DOD A 191 D2 DOD A 358 7556 0.80
REMARK 500 DH11 ARG A 61 D1 DOD A 143 3555 0.87
REMARK 500 O DOD A 201 D1 DOD A 329 8555 0.91
REMARK 500 HD11 LEU A 129 D1 DOD A 246 4454 1.09
REMARK 500 D1 DOD A 335 O DOD A 336 8555 1.14
REMARK 500 HD13 LEU A 129 O DOD A 246 4454 1.14
REMARK 500 O DOD A 296 D2 DOD A 316 1554 1.15
REMARK 500 D1 DOD A 296 O DOD A 316 1554 1.41
REMARK 500 D1 DOD A 142 O DOD A 184 6556 1.51
REMARK 500 O DOD A 350 D2 DOD A 350 8556 1.54
REMARK 500 CD1 LEU A 129 D1 DOD A 246 4454 1.58
REMARK 500 O DOD A 350 O DOD A 350 8556 1.59
REMARK 500 O DOD A 217 O DOD A 217 8555 1.68
REMARK 500 CD1 LEU A 129 O DOD A 246 4454 1.83
REMARK 500 O DOD A 201 O DOD A 329 8555 1.84
REMARK 500 O DOD A 296 O DOD A 316 1554 2.04
REMARK 500 O DOD A 335 O DOD A 336 8555 2.05
REMARK 500 O DOD A 175 O DOD A 175 7557 2.12
REMARK 500 O DOD A 378 O DOD A 378 8555 2.18
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 ALA A 9 -35.23 -39.03
REMARK 500 ASN A 19 26.92 97.25
REMARK 500 ARG A 21 -1.04 69.63
REMARK 500 SER A 36 -11.39 -164.39
REMARK 500 ASN A 44 114.69 -164.98
REMARK 500 ASP A 48 -14.40 -48.23
REMARK 500 GLN A 57 92.09 55.18
REMARK 500 ARG A 68 10.06 -161.91
REMARK 500 ASN A 77 68.04 67.84
REMARK 500 SER A 85 158.08 -46.53
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 ARG A 5 0.10 SIDE CHAIN
REMARK 500 ARG A 14 0.20 SIDE CHAIN
REMARK 500 ARG A 21 0.09 SIDE CHAIN
REMARK 500 ARG A 45 0.10 SIDE CHAIN
REMARK 500 ARG A 61 0.30 SIDE CHAIN
REMARK 500 ARG A 73 0.21 SIDE CHAIN
REMARK 500 ARG A 112 0.08 SIDE CHAIN
REMARK 500 ARG A 114 0.12 SIDE CHAIN
REMARK 500 ARG A 128 0.26 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 MET A 12 10.31
REMARK 500 ASP A 18 11.40
REMARK 500 SER A 24 -10.46
REMARK 500 LEU A 25 11.75
REMARK 500 TRP A 28 11.77
REMARK 500 ALA A 32 13.28
REMARK 500 GLN A 41 -16.00
REMARK 500 ALA A 42 -13.98
REMARK 500 ASN A 44 -12.80
REMARK 500 ASP A 52 10.01
REMARK 500 GLY A 54 -12.05
REMARK 500 ILE A 58 -11.19
REMARK 500 ASN A 59 -11.39
REMARK 500 SER A 60 10.08
REMARK 500 ASN A 65 -12.11
REMARK 500 ARG A 68 -12.63
REMARK 500 ARG A 73 -10.90
REMARK 500 ASN A 77 -10.51
REMARK 500 CYS A 80 13.85
REMARK 500 ASP A 87 -10.90
REMARK 500 ILE A 88 -12.25
REMARK 500 SER A 91 10.66
REMARK 500 ALA A 95 12.05
REMARK 500 LYS A 96 10.47
REMARK 500 GLY A 104 -10.06
REMARK 500 ALA A 110 15.46
REMARK 500 GLN A 121 10.64
REMARK 500 ARG A 125 12.46
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1IO5 A 1 129 UNP P00698 LYSC_CHICK 19 147
SEQRES 1 A 129 LYS VAL PHE GLY ARG CYS GLU LEU ALA ALA ALA MET LYS
SEQRES 2 A 129 ARG HIS GLY LEU ASP ASN TYR ARG GLY TYR SER LEU GLY
SEQRES 3 A 129 ASN TRP VAL CYS ALA ALA LYS PHE GLU SER ASN PHE ASN
SEQRES 4 A 129 THR GLN ALA THR ASN ARG ASN THR ASP GLY SER THR ASP
SEQRES 5 A 129 TYR GLY ILE LEU GLN ILE ASN SER ARG TRP TRP CYS ASN
SEQRES 6 A 129 ASP GLY ARG THR PRO GLY SER ARG ASN LEU CYS ASN ILE
SEQRES 7 A 129 PRO CYS SER ALA LEU LEU SER SER ASP ILE THR ALA SER
SEQRES 8 A 129 VAL ASN CYS ALA LYS LYS ILE VAL SER ASP GLY ASN GLY
SEQRES 9 A 129 MET ASN ALA TRP VAL ALA TRP ARG ASN ARG CYS LYS GLY
SEQRES 10 A 129 THR ASP VAL GLN ALA TRP ILE ARG GLY CYS ARG LEU
FORMUL 2 DOD *251(D2 O)
HELIX 1 1 GLY A 4 HIS A 15 1 12
HELIX 2 2 SER A 24 GLU A 35 1 12
HELIX 3 3 ASP A 87 VAL A 92 5 6
HELIX 4 4 CYS A 94 VAL A 99 1 6
HELIX 5 5 ASN A 103 ALA A 107 5 5
HELIX 6 6 TRP A 108 ASN A 113 1 6
HELIX 7 7 VAL A 120 ILE A 124 5 5
SHEET 1 A 2 THR A 43 ARG A 45 0
SHEET 2 A 2 THR A 51 TYR A 53 -1 N ASP A 52 O ASN A 44
SSBOND 1 CYS A 6 CYS A 127 1555 1555 2.02
SSBOND 2 CYS A 30 CYS A 115 1555 1555 2.02
SSBOND 3 CYS A 64 CYS A 80 1555 1555 2.02
SSBOND 4 CYS A 76 CYS A 94 1555 1555 2.02
CRYST1 80.800 80.800 37.100 90.00 90.00 90.00 P 43 21 2 8
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 0.012376 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012376 0.000000 0.00000
SCALE3 0.000000 0.000000 0.026954 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
