HEADER HYDROLASE 14-MAR-05 1Z3M
TITLE CRYSTAL STRUCTURE OF MUTANT RIBONUCLEASE S (F8NVA)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBONUCLEASE PANCREATIC, S-PEPTIDE;
COMPND 3 CHAIN: S;
COMPND 4 SYNONYM: RNASE 1, RNASE A;
COMPND 5 EC: 3.1.27.5;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: RIBONUCLEASE PANCREATIC, S-PROTEIN;
COMPND 10 CHAIN: E;
COMPND 11 SYNONYM: RNASE 1, RNASE A;
COMPND 12 EC: 3.1.27.5
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: S-PEPTIDE SYNTHESIZED BY SOLID PHASE PEPTIDE
SOURCE 4 SYNTHESIS;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 7 ORGANISM_COMMON: CATTLE;
SOURCE 8 ORGANISM_TAXID: 9913
KEYWDS RNASE S MUTANT (F8NVA), S-PEPTIDE, S-PROTEIN, CAVITY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.DAS,B.VASUDEVA RAO,S.GHOSH,R.VARADARAJAN
REVDAT 6 15-NOV-23 1Z3M 1 REMARK
REVDAT 5 25-OCT-23 1Z3M 1 REMARK
REVDAT 4 10-NOV-21 1Z3M 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1Z3M 1 VERSN
REVDAT 2 17-JAN-06 1Z3M 1 JRNL
REVDAT 1 29-MAR-05 1Z3M 0
JRNL AUTH M.DAS,B.V.RAO,S.GHOSH,R.VARADARAJAN
JRNL TITL ATTEMPTS TO DELINEATE THE RELATIVE CONTRIBUTIONS OF CHANGES
JRNL TITL 2 IN HYDROPHOBICITY AND PACKING TO CHANGES IN STABILITY OF
JRNL TITL 3 RIBONUCLEASE S MUTANTS.
JRNL REF BIOCHEMISTRY V. 44 5923 2005
JRNL REFN ISSN 0006-2960
JRNL PMID 15823052
JRNL DOI 10.1021/BI050001+
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 14.99
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 973406.820
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 7954
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) : 0.195
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.600
REMARK 3 FREE R VALUE TEST SET COUNT : 365
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.013
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 7
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.11
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1068
REMARK 3 BIN R VALUE (WORKING SET) : 0.1990
REMARK 3 BIN FREE R VALUE : 0.2320
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.40
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 49
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.033
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 919
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 55
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.40
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) : 0.22
REMARK 3 ESD FROM SIGMAA (A) : 0.08
REMARK 3 LOW RESOLUTION CUTOFF (A) : 15.0
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.29
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.15
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.690
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) : 1.570 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.590 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.390 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.710 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.38
REMARK 3 BSOL : 44.14
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 : PROT.PARAM
REMARK 3 PARAMETER FILE 2 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN1.TOP
REMARK 3 TOPOLOGY FILE 2 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1Z3M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-MAR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032255.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-DEC-03
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : 5.75
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 : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 7993
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 6.300
REMARK 200 R MERGE (I) : 0.10600
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) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.20300
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: CNS 1.1
REMARK 200 STARTING MODEL: PDB ENTRY 2RLN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, CESIUM CHLORIDE,
REMARK 280 SODIUM ACETATE, PH 5.75, BATCH METHOD, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 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+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 32.56567
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 65.13133
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 65.13133
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 32.56567
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1760 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 6700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: S, E
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11430 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -73.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: S, E
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 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 SER E 22 -155.87 -79.03
REMARK 500 ARG E 39 171.53 179.93
REMARK 500 GLN E 60 -133.78 -97.94
REMARK 500 ALA E 122 179.96 174.63
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 125
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 126
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1D5D RELATED DB: PDB
REMARK 900 RELATED ID: 1RBH RELATED DB: PDB
REMARK 900 RELATED ID: 1D5E RELATED DB: PDB
REMARK 900 RELATED ID: 1D5H RELATED DB: PDB
REMARK 900 RELATED ID: 1RBC RELATED DB: PDB
REMARK 900 RELATED ID: 1RBD RELATED DB: PDB
REMARK 900 RELATED ID: 1Z3L RELATED DB: PDB
REMARK 900 MUTANT RIBONUCLEASE S (F8ANB)
REMARK 900 RELATED ID: 1Z3P RELATED DB: PDB
REMARK 900 MUTANT RIBONUCLEASE S (M13NVA)
DBREF 1Z3M S 1 15 UNP P61823 RNP_BOVIN 27 41
DBREF 1Z3M E 21 124 UNP P61823 RNP_BOVIN 47 150
SEQADV 1Z3M NVA S 8 UNP P61823 PHE 34 ENGINEERED MUTATION
SEQADV 1Z3M NLE S 13 UNP P61823 MET 39 ENGINEERED MUTATION
SEQRES 1 S 15 LYS GLU THR ALA ALA ALA LYS NVA GLU ARG GLN HIS NLE
SEQRES 2 S 15 ASP SER
SEQRES 1 E 104 SER SER SER ASN TYR CYS ASN GLN MET MET LYS SER ARG
SEQRES 2 E 104 ASN LEU THR LYS ASP ARG CYS LYS PRO VAL ASN THR PHE
SEQRES 3 E 104 VAL HIS GLU SER LEU ALA ASP VAL GLN ALA VAL CYS SER
SEQRES 4 E 104 GLN LYS ASN VAL ALA CYS LYS ASN GLY GLN THR ASN CYS
SEQRES 5 E 104 TYR GLN SER TYR SER THR MET SER ILE THR ASP CYS ARG
SEQRES 6 E 104 GLU THR GLY SER SER LYS TYR PRO ASN CYS ALA TYR LYS
SEQRES 7 E 104 THR THR GLN ALA ASN LYS HIS ILE ILE VAL ALA CYS GLU
SEQRES 8 E 104 GLY ASN PRO TYR VAL PRO VAL HIS PHE ASP ALA SER VAL
MODRES 1Z3M NVA S 8 VAL NORVALINE
MODRES 1Z3M NLE S 13 LEU NORLEUCINE
HET NVA S 8 7
HET NLE S 13 8
HET SO4 E 125 5
HET SO4 E 126 5
HETNAM NVA NORVALINE
HETNAM NLE NORLEUCINE
HETNAM SO4 SULFATE ION
FORMUL 1 NVA C5 H11 N O2
FORMUL 1 NLE C6 H13 N O2
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 5 HOH *55(H2 O)
HELIX 1 1 THR S 3 NLE S 13 1 11
HELIX 2 2 ASN E 24 ARG E 33 1 10
HELIX 3 3 SER E 50 ALA E 56 1 7
HELIX 4 4 VAL E 57 GLN E 60 5 4
SHEET 1 A 3 VAL E 43 VAL E 47 0
SHEET 2 A 3 MET E 79 GLU E 86 -1 O CYS E 84 N ASN E 44
SHEET 3 A 3 TYR E 97 LYS E 104 -1 O ALA E 102 N ILE E 81
SHEET 1 B 4 LYS E 61 VAL E 63 0
SHEET 2 B 4 CYS E 72 GLN E 74 -1 O GLN E 74 N LYS E 61
SHEET 3 B 4 ILE E 106 GLU E 111 -1 O VAL E 108 N TYR E 73
SHEET 4 B 4 VAL E 116 SER E 123 -1 O VAL E 118 N ALA E 109
SSBOND 1 CYS E 26 CYS E 84 1555 1555 2.03
SSBOND 2 CYS E 40 CYS E 95 1555 1555 2.03
SSBOND 3 CYS E 58 CYS E 110 1555 1555 2.03
SSBOND 4 CYS E 65 CYS E 72 1555 1555 2.03
LINK C LYS S 7 N NVA S 8 1555 1555 1.33
LINK C NVA S 8 N GLU S 9 1555 1555 1.33
LINK C HIS S 12 N NLE S 13 1555 1555 1.32
LINK C NLE S 13 N ASP S 14 1555 1555 1.33
CISPEP 1 TYR E 92 PRO E 93 0 0.38
CISPEP 2 ASN E 113 PRO E 114 0 0.09
SITE 1 AC1 4 HIS E 119 PHE E 120 HOH E 246 HIS S 12
SITE 1 AC2 7 SER E 50 LEU E 51 LYS E 61 LYS E 98
SITE 2 AC2 7 HOH E 207 HOH E 249 SER S 15
CRYST1 44.391 44.391 97.697 90.00 90.00 120.00 P 31 2 1 6
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 0.022527 0.013006 0.000000 0.00000
SCALE2 0.000000 0.026012 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010236 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
