HEADER HYDROLASE 05-FEB-01 1I1Z
TITLE MUTANT HUMAN LYSOZYME (Q86D)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYSOZYME C;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.2.2.17;
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;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: AH22R-;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PERI8811
KEYWDS CALCIUM BINDING SITE, MUTANT HUMAN LYSOZYME, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.KUROKI
REVDAT 5 03-APR-24 1I1Z 1 REMARK
REVDAT 4 10-NOV-21 1I1Z 1 SEQADV SSBOND
REVDAT 3 24-FEB-09 1I1Z 1 VERSN
REVDAT 2 31-DEC-02 1I1Z 1 REMARK
REVDAT 1 28-FEB-01 1I1Z 0
JRNL AUTH R.KUROKI,K.YUTANI
JRNL TITL STRUCTURAL AND THERMODYNAMIC RESPONSES OF MUTATIONS AT A
JRNL TITL 2 CA2+ BINDING SITE ENGINEERED INTO HUMAN LYSOZYME.
JRNL REF J.BIOL.CHEM. V. 273 34310 1998
JRNL REFN ISSN 0021-9258
JRNL PMID 9852096
JRNL DOI 10.1074/JBC.273.51.34310
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.KUROKI,K.NITTA,K.YUTANI
REMARK 1 TITL THERMODYNAMIC CHANGES IN THE BINDING OF CA2+ TO A MUTANT
REMARK 1 TITL 2 HUMAN LYSOZYME (D86/92). ENTHALPY-ENTROPY COMPENSATION
REMARK 1 TITL 3 OBSERVED UPON CA2+ BINDING TO PROTEINS.
REMARK 1 REF J.BIOL.CHEM. V. 267 24297 1992
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 2
REMARK 1 AUTH R.KUROKI,S.KAWAKITA,H.NAKAMURA,K.YUTANI
REMARK 1 TITL ENTROPIC STABILIZATION OF A MUTANT HUMAN LYSOZYME INDUCED BY
REMARK 1 TITL 2 CALCIUM BINDING
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 89 6803 1992
REMARK 1 REFN ISSN 0027-8424
REMARK 1 REFERENCE 3
REMARK 1 AUTH K.INAKA,R.KUROKI,M.KIKUCHI,M.MATSUSHIMA
REMARK 1 TITL CRYSTAL STRUCTURE OF THE APO- AND HOLOMUTANT HUMAN LYSOZYMES
REMARK 1 TITL 2 WITH AN INTRODUCED CA2+ BINDING SITE
REMARK 1 REF J.BIOL.CHEM. V. 266 20666 1991
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 4
REMARK 1 AUTH R.KUROKI,Y.TANIYAM,C.SEKO,H.NAKAMURA,M.KIKUCHI,M.IKEHARA
REMARK 1 TITL DESIGN AND CREATION OF A CA2+ BINDING SITE IN HUMAN LYSOZYME
REMARK 1 TITL 2 TO ENHANCE STRUCTURAL STABILITY
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 86 6903 1989
REMARK 1 REFN ISSN 0027-8424
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TNT
REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.0
REMARK 3 NUMBER OF REFLECTIONS : 10022
REMARK 3
REMARK 3 USING DATA ABOVE SIGMA CUTOFF.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.161
REMARK 3 R VALUE (WORKING SET) : NULL
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
REMARK 3 USING ALL DATA, NO SIGMA CUTOFF.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.1610
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 10022
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1028
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 120
REMARK 3
REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : 0.015 ; 1.000 ; 1052
REMARK 3 BOND ANGLES (DEGREES) : 2.633 ; 1.250 ; 1422
REMARK 3 TORSION ANGLES (DEGREES) : 15.416; 0.000 ; 631
REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES (A) : 0.013 ; 2.000 ; 28
REMARK 3 GENERAL PLANES (A) : 0.015 ; 6.000 ; 157
REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS (A) : 0.022 ; 10.000; 13
REMARK 3
REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 RESTRAINT LIBRARIES.
REMARK 3 STEREOCHEMISTRY : NULL
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1I1Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-FEB-01.
REMARK 100 THE DEPOSITION ID IS D_1000012802.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 293.0
REMARK 200 PH : 6.00
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 RU200
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 : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : SDMS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SDMS
REMARK 200 DATA SCALING SOFTWARE : SDMS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43723
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06900
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: TNT
REMARK 200 STARTING MODEL: WILD TYPE HUMAN LYSOZYME
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.88
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PHOSPHATE, SODIUM CHLORIDE, CALCIUM
REMARK 280 CHLORIDE, PH 6.00, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 277.0K
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 28.31000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 16.91500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.41000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 16.91500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.31000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 30.41000
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 C ALA A 83 O HOH A 311 1.36
REMARK 500 N ASP A 91 O HOH A 310 1.40
REMARK 500 O ALA A 83 O HOH A 311 1.41
REMARK 500 O HOH A 266 O HOH A 306 1.46
REMARK 500 N LEU A 84 O HOH A 311 1.49
REMARK 500 N ALA A 92 O HOH A 310 1.55
REMARK 500 O HOH A 266 O HOH A 309 1.56
REMARK 500 O HOH A 304 O HOH A 305 1.66
REMARK 500 CA ASP A 91 O HOH A 310 1.70
REMARK 500 O HOH A 303 O HOH A 315 1.76
REMARK 500 CA LEU A 84 O HOH A 311 1.78
REMARK 500 O HOH A 164 O HOH A 306 1.80
REMARK 500 C ASP A 91 O HOH A 310 1.84
REMARK 500 SD MET A 17 O HOH A 302 1.85
REMARK 500 SD MET A 17 O HOH A 304 1.91
REMARK 500 CG2 VAL A 74 O HOH A 301 1.93
REMARK 500 N LEU A 85 O HOH A 311 2.00
REMARK 500 SD MET A 17 O HOH A 305 2.03
REMARK 500 C LEU A 84 O HOH A 311 2.06
REMARK 500 CG MET A 17 O HOH A 304 2.11
REMARK 500 O HOH A 302 O HOH A 304 2.13
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 O HOH A 162 O HOH A 314 2555 1.46
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 GLU A 7 CD GLU A 7 OE2 0.066
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 ARG A 14 NE - CZ - NH1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 ARG A 14 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ASP A 18 CB - CG - OD1 ANGL. DEV. = 7.7 DEGREES
REMARK 500 ASP A 18 CB - CG - OD2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 TYR A 38 CB - CG - CD1 ANGL. DEV. = -4.6 DEGREES
REMARK 500 ARG A 50 NE - CZ - NH1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 ARG A 50 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ASP A 53 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ASP A 67 CB - CG - OD2 ANGL. DEV. = -7.6 DEGREES
REMARK 500 LEU A 79 CB - CA - C ANGL. DEV. = -12.9 DEGREES
REMARK 500 ASP A 87 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ASP A 87 CB - CG - OD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 ARG A 98 NE - CZ - NH2 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG A 101 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 113 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ASP A 120 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP A 120 CB - CG - OD2 ANGL. DEV. = -8.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1LZ1 RELATED DB: PDB
REMARK 900 1LZ1 CONTAINS NATURAL HUMAN LYSOZYME
REMARK 900 RELATED ID: 1I20 RELATED DB: PDB
REMARK 900 1I20 CONTAINS MUTANT HUMAN LYSOZYME (A92D)
REMARK 900 RELATED ID: 1I22 RELATED DB: PDB
REMARK 900 1I22 CONTAINS MUTANT HUMAN LYSOZYME (A83K/Q86D/A92D)
REMARK 900 RELATED ID: 2LHM RELATED DB: PDB
REMARK 900 2LHM CONTAINS MUTANT HUMAN LYSOZYME (APO-Q86D/A92D)
REMARK 900 RELATED ID: 3LHM RELATED DB: PDB
REMARK 900 3LHM CONTAINS MUTANT HUMAN LYSOZYME (HOLO-Q86D/A92D)
DBREF 1I1Z A 1 130 UNP P61626 LYSC_HUMAN 19 148
SEQADV 1I1Z ASP A 86 UNP P61626 GLN 104 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 GLY 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 ASP 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
FORMUL 2 HOH *120(H2 O)
HELIX 1 1 GLU A 4 LEU A 15 1 12
HELIX 2 2 SER A 24 GLY A 37 1 14
HELIX 3 3 CYS A 81 ASP A 86 5 6
HELIX 4 4 ILE A 89 VAL A 100 1 12
HELIX 5 5 GLN A 104 ALA A 108 5 5
HELIX 6 6 TRP A 109 CYS A 116 1 8
HELIX 7 7 VAL A 121 GLN A 126 5 6
SHEET 1 A 3 THR A 43 TYR A 45 0
SHEET 2 A 3 THR A 52 TYR A 54 -1 N ASP A 53 O ASN A 44
SHEET 3 A 3 ILE A 59 ASN A 60 -1 N ILE A 59 O TYR A 54
SSBOND 1 CYS A 6 CYS A 128 1555 1555 2.07
SSBOND 2 CYS A 30 CYS A 116 1555 1555 2.02
SSBOND 3 CYS A 65 CYS A 81 1555 1555 2.07
SSBOND 4 CYS A 77 CYS A 95 1555 1555 1.99
CRYST1 56.620 60.820 33.830 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 0.017662 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016442 0.000000 0.00000
SCALE3 0.000000 0.000000 0.029560 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
