HEADER HYDROLASE 25-JAN-99 1B7O
TITLE VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (LYSOZYME);
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.2.1.17;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: 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: SACCHAROMYCES CEREVISIAE;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4932
KEYWDS MUTANT STABILITY, HUMAN LYSOZYME, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.TAKANO,M.OTA,K.OGASAHARA,Y.YAMAGATA,K.NISHIKAWA,K.YUTANI
REVDAT 7 03-APR-24 1B7O 1 REMARK
REVDAT 6 27-DEC-23 1B7O 1 REMARK
REVDAT 5 03-NOV-21 1B7O 1 REMARK SEQADV LINK
REVDAT 4 24-FEB-09 1B7O 1 VERSN
REVDAT 3 01-APR-03 1B7O 1 JRNL
REVDAT 2 29-DEC-99 1B7O 4 HEADER COMPND REMARK JRNL
REVDAT 2 2 4 ATOM SOURCE SEQRES
REVDAT 1 02-FEB-99 1B7O 0
JRNL AUTH K.TAKANO,M.OTA,K.OGASAHARA,Y.YAMAGATA,K.NISHIKAWA,K.YUTANI
JRNL TITL EXPERIMENTAL VERIFICATION OF THE 'STABILITY PROFILE OF
JRNL TITL 2 MUTANT PROTEIN' (SPMP) DATA USING MUTANT HUMAN LYSOZYMES.
JRNL REF PROTEIN ENG. V. 12 663 1999
JRNL REFN ISSN 0269-2139
JRNL PMID 10469827
JRNL DOI 10.1093/PROTEIN/12.8.663
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH K.TAKANO,Y.YAMAGATA,K.YUTANI
REMARK 1 TITL A GENERAL RULE FOR THE RELATIONSHIP BETWEEN HYDROPHOBIC
REMARK 1 TITL 2 EFFECT AND CONFORMATIONAL STABILITY OF A PROTEIN: STABILITY
REMARK 1 TITL 3 AND STRUCTURE OF A SERIES OF HYDROPHOBIC MUTANTS OF HUMAN
REMARK 1 TITL 4 LYSOZYME
REMARK 1 REF J.MOL.BIOL. V. 280 749 1998
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 2
REMARK 1 AUTH Y.YAMAGATA,M.KUBOTA,Y.SUMIKAWA,J.FUNAHASHI,K.TAKANO,S.FUJII,
REMARK 1 AUTH 2 K.YUTANI
REMARK 1 TITL CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL
REMARK 1 TITL 2 STABILITY OF HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS
REMARK 1 TITL 3 OF SIX TYROSINE->PHENYLALANINE MUTANTS
REMARK 1 REF BIOCHEMISTRY V. 37 9355 1998
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 3
REMARK 1 AUTH K.TAKANO,Y.YAMAGATA,S.FUJII,K.YUTANI
REMARK 1 TITL CONTRIBUTION OF THE HYDROPHOBIC EFFECT TO THE STABILITY OF
REMARK 1 TITL 2 HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL
REMARK 1 TITL 3 ANALYSES OF THE NINE VALINE TO ALANINE MUTANTS
REMARK 1 REF BIOCHEMISTRY V. 36 688 1997
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 4
REMARK 1 AUTH K.TAKANO,J.FUNAHASHI,Y.YAMAGATA,S.FUJII,K.YUTANI
REMARK 1 TITL CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN
REMARK 1 TITL 2 TO THE CONFORMATIONAL STABILITY
REMARK 1 REF J.MOL.BIOL. V. 274 132 1997
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 5
REMARK 1 AUTH K.TAKANO,K.OGASAWAHA,H.KANEDA,Y.YAMAGATA,S.FUJII,E.KANAYA,
REMARK 1 AUTH 2 M.KIKUCHI,M.OOBATAKE,K.YUTANI
REMARK 1 TITL CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF
REMARK 1 TITL 2 HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL
REMARK 1 TITL 3 ANALYSIS OF THE FIVE ISOLEUCINE TO VALINE MUTANTS
REMARK 1 REF J.MOL.BIOL. V. 254 62 1995
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 3.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 83.5
REMARK 3 NUMBER OF REFLECTIONS : 9098
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : NULL
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 : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.88
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 58.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 784
REMARK 3 BIN R VALUE (WORKING SET) : 0.2330
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 : 1034
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 266
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) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.570
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 1B7O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JAN-99.
REMARK 100 THE DEPOSITION ID IS D_1000000368.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-AUG-98
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : PROCESS
REMARK 200 DATA SCALING SOFTWARE : PROCESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29226
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.5
REMARK 200 DATA REDUNDANCY : 2.500
REMARK 200 R MERGE (I) : 0.07600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 75.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.19000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: WILD-TYPE HUMAN LYSOZYME
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 4.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
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 28.23500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 16.34500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.73500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 16.34500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.23500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 30.73500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 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 NH2 ARG A 50 O HOH A 217 0.66
REMARK 500 O HOH A 213 O HOH A 224 0.84
REMARK 500 NE2 GLN A 37 O HOH A 212 1.04
REMARK 500 NE ARG A 119 O HOH A 376 1.15
REMARK 500 CD1 TRP A 109 O HOH A 201 1.15
REMARK 500 CD ARG A 119 O HOH A 376 1.36
REMARK 500 O ASN A 88 O HOH A 135 1.36
REMARK 500 NZ LYS A 1 O HOH A 154 1.42
REMARK 500 OG SER A 82 O HOH A 143 1.45
REMARK 500 CG ARG A 119 O HOH A 376 1.45
REMARK 500 N LYS A 1 O HOH A 162 1.45
REMARK 500 OE1 GLU A 35 O HOH A 228 1.52
REMARK 500 NH2 ARG A 115 O HOH A 271 1.55
REMARK 500 CD GLU A 35 O HOH A 228 1.57
REMARK 500 CG LYS A 13 O HOH A 325 1.57
REMARK 500 OE1 GLU A 35 O HOH A 344 1.58
REMARK 500 CB ALA A 111 O HOH A 150 1.58
REMARK 500 O HOH A 296 O HOH A 336 1.70
REMARK 500 O HOH A 297 O HOH A 357 1.73
REMARK 500 OD2 ASP A 91 O HOH A 248 1.74
REMARK 500 CG TRP A 109 O HOH A 201 1.77
REMARK 500 NH1 ARG A 50 O HOH A 268 1.78
REMARK 500 CG ARG A 122 O HOH A 151 1.80
REMARK 500 CZ ARG A 115 O HOH A 271 1.80
REMARK 500 CZ ARG A 50 O HOH A 217 1.82
REMARK 500 CD ARG A 115 O HOH A 271 1.85
REMARK 500 NE1 TRP A 109 O HOH A 201 1.86
REMARK 500 NE ARG A 115 O HOH A 271 1.86
REMARK 500 O HOH A 249 O HOH A 298 1.88
REMARK 500 OE2 GLU A 35 O HOH A 150 1.88
REMARK 500 OD1 ASP A 87 O HOH A 162 1.88
REMARK 500 O HOH A 197 O HOH A 310 1.89
REMARK 500 OE2 GLU A 35 O HOH A 228 1.91
REMARK 500 CG2 ILE A 56 O HOH A 137 1.93
REMARK 500 O HOH A 229 O HOH A 278 1.97
REMARK 500 N ILE A 56 O HOH A 137 1.98
REMARK 500 ND2 ASN A 75 O HOH A 326 1.98
REMARK 500 O HOH A 230 O HOH A 264 1.98
REMARK 500 CA ILE A 89 O HOH A 135 1.98
REMARK 500 CD ARG A 21 O HOH A 255 1.98
REMARK 500 OH TYR A 20 O HOH A 262 1.99
REMARK 500 C ASN A 88 O HOH A 135 2.01
REMARK 500 O ARG A 50 O HOH A 379 2.02
REMARK 500 O ALA A 90 O HOH A 203 2.02
REMARK 500 ND2 ASN A 66 O HOH A 132 2.02
REMARK 500 CZ ARG A 50 O HOH A 268 2.03
REMARK 500 CB HIS A 78 O HOH A 185 2.04
REMARK 500 N SER A 80 O HOH A 131 2.04
REMARK 500 N ARG A 21 O HOH A 208 2.06
REMARK 500 O HOH A 372 O HOH A 394 2.07
REMARK 500
REMARK 500 THIS ENTRY HAS 62 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 OE1 GLN A 117 O HOH A 339 4557 1.11
REMARK 500 ND2 ASN A 118 O HOH A 374 4557 1.21
REMARK 500 NH1 ARG A 14 O HOH A 186 2565 1.34
REMARK 500 NH1 ARG A 113 O HOH A 350 2554 1.56
REMARK 500 CG2 VAL A 110 O HOH A 369 2554 1.57
REMARK 500 O THR A 70 O HOH A 141 1556 1.57
REMARK 500 O HOH A 334 O HOH A 396 4557 1.60
REMARK 500 NH1 ARG A 122 O HOH A 138 4556 1.62
REMARK 500 NH1 ARG A 21 NE ARG A 41 4557 1.63
REMARK 500 CZ ARG A 14 O HOH A 186 2565 1.82
REMARK 500 OD1 ASN A 118 O HOH A 342 2554 1.85
REMARK 500 NH1 ARG A 41 O HOH A 280 4456 1.85
REMARK 500 NH1 ARG A 21 CZ ARG A 41 4557 1.89
REMARK 500 CD GLN A 117 O HOH A 339 4557 1.96
REMARK 500 NE ARG A 14 O HOH A 186 2565 2.00
REMARK 500 O HOH A 263 O HOH A 286 2564 2.04
REMARK 500 OE1 GLN A 86 NE ARG A 107 4457 2.09
REMARK 500 CZ ARG A 21 CZ ARG A 41 4557 2.11
REMARK 500 NH2 ARG A 41 O HOH A 280 4456 2.15
REMARK 500 NH1 ARG A 21 NH2 ARG A 41 4557 2.15
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 NA A 601 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 61 O
REMARK 620 2 HOH A 146 O 161.0
REMARK 620 3 HOH A 189 O 102.3 76.4
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 601
DBREF 1B7O A 1 130 UNP P61626 LYSC_HUMAN 19 148
SEQADV 1B7O GLN A 37 UNP P61626 GLY 55 ENGINEERED MUTATION
SEQRES 1 A 130 LYS VAL PHE GLU ARG CYS GLU LEU ALA ARG THR LEU LYS
SEQRES 2 A 130 ARG LEU GLY MET ASP GLY TYR ARG GLY ILE SER LEU ALA
SEQRES 3 A 130 ASN TRP MET CYS LEU ALA LYS TRP GLU SER GLN TYR ASN
SEQRES 4 A 130 THR ARG ALA THR ASN TYR ASN ALA GLY ASP ARG SER THR
SEQRES 5 A 130 ASP TYR GLY ILE PHE GLN ILE ASN SER ARG TYR TRP CYS
SEQRES 6 A 130 ASN ASP GLY LYS THR PRO GLY ALA VAL ASN ALA CYS HIS
SEQRES 7 A 130 LEU SER CYS SER ALA LEU LEU GLN ASP ASN ILE ALA ASP
SEQRES 8 A 130 ALA VAL ALA CYS ALA LYS ARG VAL VAL ARG ASP PRO GLN
SEQRES 9 A 130 GLY ILE ARG ALA TRP VAL ALA TRP ARG ASN ARG CYS GLN
SEQRES 10 A 130 ASN ARG ASP VAL ARG GLN TYR VAL GLN GLY CYS GLY VAL
HET NA A 601 1
HETNAM NA SODIUM ION
FORMUL 2 NA NA 1+
FORMUL 3 HOH *266(H2 O)
HELIX 1 1 ARG A 5 ARG A 14 1 10
HELIX 2 2 TYR A 20 GLY A 22 5 3
HELIX 3 3 LEU A 25 SER A 36 1 12
HELIX 4 4 CYS A 81 LEU A 85 5 5
HELIX 5 5 ALA A 90 ARG A 101 1 12
HELIX 6 6 GLY A 105 ALA A 108 5 4
HELIX 7 7 VAL A 110 ARG A 115 1 6
HELIX 8 8 ARG A 122 TYR A 124 5 3
SHEET 1 A 2 THR A 43 ASN A 46 0
SHEET 2 A 2 SER A 51 TYR A 54 -1 N ASP A 53 O ASN A 44
SSBOND 1 CYS A 6 CYS A 128 1555 1555 2.03
SSBOND 2 CYS A 30 CYS A 116 1555 1555 2.04
SSBOND 3 CYS A 65 CYS A 81 1555 1555 2.02
SSBOND 4 CYS A 77 CYS A 95 1555 1555 2.03
LINK O SER A 61 NA NA A 601 1554 1555 1.90
LINK O HOH A 146 NA NA A 601 1555 1555 2.35
LINK O HOH A 189 NA NA A 601 1555 1555 2.31
SITE 1 AC1 7 SER A 61 ARG A 62 CYS A 65 ALA A 73
SITE 2 AC1 7 VAL A 74 HOH A 146 HOH A 189
CRYST1 56.470 61.470 32.690 90.00 90.00 90.00 P 21 21 21 4
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 0.017708 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016268 0.000000 0.00000
SCALE3 0.000000 0.000000 0.030590 0.00000
(ATOM LINES ARE NOT SHOWN.)
END