HEADER HYDROLASE 14-NOV-06 2NWD
TITLE STRUCTURE OF CHEMICALLY SYNTHESIZED HUMAN LYSOZYME AT 1 ANGSTROM
TITLE 2 RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYSOZYME C;
COMPND 3 CHAIN: X;
COMPND 4 SYNONYM: 1,4-BETA-N-ACETYLMURAMIDASE C;
COMPND 5 EC: 3.2.1.17;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: CHEMICAL PROTEIN SYNTHESIS
KEYWDS NATIVE CHEMICAL LIGATION, CHEMICAL PROTEIN SYNTHESIS, CONVERGENT
KEYWDS 2 SYNTHESIS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.DUREK,V.Y.TORBEEV,S.B.H.KENT
REVDAT 4 30-AUG-23 2NWD 1 REMARK
REVDAT 3 24-FEB-09 2NWD 1 VERSN
REVDAT 2 03-APR-07 2NWD 1 JRNL
REVDAT 1 19-DEC-06 2NWD 0
JRNL AUTH T.DUREK,V.Y.TORBEEV,S.B.KENT
JRNL TITL CONVERGENT CHEMICAL SYNTHESIS AND HIGH-RESOLUTION X-RAY
JRNL TITL 2 STRUCTURE OF HUMAN LYSOZYME.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 104 4846 2007
JRNL REFN ISSN 0027-8424
JRNL PMID 17360367
JRNL DOI 10.1073/PNAS.0610630104
REMARK 2
REMARK 2 RESOLUTION. 1.04 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.04
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 50848
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 + TEST SET) : 0.134
REMARK 3 R VALUE (WORKING SET) : 0.133
REMARK 3 FREE R VALUE : 0.152
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2721
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.04
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.07
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3566
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.17
REMARK 3 BIN R VALUE (WORKING SET) : 0.2050
REMARK 3 BIN FREE R VALUE SET COUNT : 172
REMARK 3 BIN FREE R VALUE : 0.2500
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1029
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 210
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 8.17
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.37000
REMARK 3 B22 (A**2) : 0.22000
REMARK 3 B33 (A**2) : 0.15000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.025
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.026
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.015
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.651
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.976
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.974
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1065 ; 0.017 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 751 ; 0.005 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1443 ; 1.716 ; 1.915
REMARK 3 BOND ANGLES OTHERS (DEGREES): 1777 ; 1.111 ; 3.009
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 129 ; 6.625 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 56 ;35.339 ;22.143
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 177 ;11.198 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 15 ;15.693 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 149 ; 0.113 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1214 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 248 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 216 ; 0.230 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 853 ; 0.209 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 530 ; 0.184 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 540 ; 0.087 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 94 ; 0.221 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 12 ; 0.089 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 47 ; 0.365 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 23 ; 0.183 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 822 ; 2.853 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 271 ; 1.556 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1025 ; 3.288 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 510 ; 3.946 ; 2.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 418 ; 4.847 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 2327 ; 2.076 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 210 ;14.635 ; 3.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 1792 ; 6.034 ; 3.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2NWD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-NOV-06.
REMARK 100 THE DEPOSITION ID IS D_1000040383.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-OCT-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97949
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53675
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.040
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CCP4
REMARK 200 STARTING MODEL: 1JSF, SEE REF. K. HARADA, Y. ABE, M. MURAKI,
REMARK 200 PROTEINS, 1998, 30, 232.
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: C 6 MG/ML, 60 MM LICL, 1.25 MM HEPES,
REMARK 280 15 MM SODIUM PHOSPHATE, 1.25 M NACL , PH 4.9, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
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 28.13050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 16.42550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.56650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 16.42550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.13050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 30.56650
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: X
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 OE1 GLN X 126 O HOH X 324 1.97
REMARK 500 O HOH X 274 O HOH X 282 2.16
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 X 7 CG GLU X 7 CD 0.122
REMARK 500 ARG X 21 CG ARG X 21 CD -0.179
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 GLU X 7 OE1 - CD - OE2 ANGL. DEV. = -8.2 DEGREES
REMARK 500 GLU X 7 CG - CD - OE1 ANGL. DEV. = 14.3 DEGREES
REMARK 500 ARG X 21 NE - CZ - NH1 ANGL. DEV. = -6.8 DEGREES
REMARK 500 ARG X 21 NE - CZ - NH2 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG X 119 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2NWD X 1 130 UNP P61626 LYSC_HUMAN 19 148
SEQRES 1 X 130 LYS VAL PHE GLU ARG CYS GLU LEU ALA ARG THR LEU LYS
SEQRES 2 X 130 ARG LEU GLY MET ASP GLY TYR ARG GLY ILE SER LEU ALA
SEQRES 3 X 130 ASN TRP MET CYS LEU ALA LYS TRP GLU SER GLY TYR ASN
SEQRES 4 X 130 THR ARG ALA THR ASN TYR ASN ALA GLY ASP ARG SER THR
SEQRES 5 X 130 ASP TYR GLY ILE PHE GLN ILE ASN SER ARG TYR TRP CYS
SEQRES 6 X 130 ASN ASP GLY LYS THR PRO GLY ALA VAL ASN ALA CYS HIS
SEQRES 7 X 130 LEU SER CYS SER ALA LEU LEU GLN ASP ASN ILE ALA ASP
SEQRES 8 X 130 ALA VAL ALA CYS ALA LYS ARG VAL VAL ARG ASP PRO GLN
SEQRES 9 X 130 GLY ILE ARG ALA TRP VAL ALA TRP ARG ASN ARG CYS GLN
SEQRES 10 X 130 ASN ARG ASP VAL ARG GLN TYR VAL GLN GLY CYS GLY VAL
FORMUL 2 HOH *210(H2 O)
HELIX 1 1 GLU X 4 LEU X 15 1 12
HELIX 2 2 GLY X 19 ILE X 23 5 5
HELIX 3 3 SER X 24 GLY X 37 1 14
HELIX 4 4 SER X 80 GLN X 86 5 7
HELIX 5 5 ILE X 89 ASP X 102 1 14
HELIX 6 6 GLN X 104 ALA X 108 5 5
HELIX 7 7 TRP X 109 CYS X 116 1 8
HELIX 8 8 VAL X 121 VAL X 125 5 5
SHEET 1 A 3 THR X 43 TYR X 45 0
SHEET 2 A 3 THR X 52 TYR X 54 -1 O ASP X 53 N ASN X 44
SHEET 3 A 3 ILE X 59 ASN X 60 -1 O ILE X 59 N TYR X 54
SSBOND 1 CYS X 6 CYS X 128 1555 1555 2.08
SSBOND 2 CYS X 30 CYS X 116 1555 1555 2.07
SSBOND 3 CYS X 65 CYS X 81 1555 1555 2.06
SSBOND 4 CYS X 77 CYS X 95 1555 1555 2.05
CRYST1 56.261 61.133 32.851 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 0.017774 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016358 0.000000 0.00000
SCALE3 0.000000 0.000000 0.030440 0.00000
(ATOM LINES ARE NOT SHOWN.)
END