HEADER HYDROLASE 07-NOV-97 8PCH
TITLE CRYSTAL STRUCTURE OF PORCINE CATHEPSIN H DETERMINED AT 2.1 ANGSTROM
TITLE 2 RESOLUTION: LOCATION OF THE MINI-CHAIN C-TERMINAL CARBOXYL GROUP
TITLE 3 DEFINES CATHEPSIN H AMINOPEPTIDASE FUNCTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATHEPSIN H;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.4.22.16;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: CATHEPSIN H;
COMPND 7 CHAIN: P;
COMPND 8 EC: 3.4.22.16
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGANISM_TAXID: 9823;
SOURCE 5 ORGAN: SPLEEN;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 8 ORGANISM_COMMON: PIG;
SOURCE 9 ORGANISM_TAXID: 9823;
SOURCE 10 ORGAN: SPLEEN
KEYWDS HYDROLASE, PROTEASE, CYSTEINE PROTEINASE, AMINOPEPTIDASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.GUNCAR,M.PODOBNIK,J.PUNGERCAR,B.STRUKELJ,V.TURK,D.TURK
REVDAT 6 09-AUG-23 8PCH 1 REMARK HETSYN
REVDAT 5 29-JUL-20 8PCH 1 COMPND REMARK HETNAM LINK
REVDAT 5 2 1 SITE ATOM
REVDAT 4 13-JUL-11 8PCH 1 VERSN
REVDAT 3 24-FEB-09 8PCH 1 VERSN
REVDAT 2 13-JAN-99 8PCH 3 REMARK TITLE HETATM TER
REVDAT 2 2 3 ATOM AUTHOR CONECT
REVDAT 1 09-DEC-98 8PCH 0
JRNL AUTH G.GUNCAR,M.PODOBNIK,J.PUNGERCAR,B.STRUKELJ,V.TURK,D.TURK
JRNL TITL CRYSTAL STRUCTURE OF PORCINE CATHEPSIN H DETERMINED AT 2.1 A
JRNL TITL 2 RESOLUTION: LOCATION OF THE MINI-CHAIN C-TERMINAL CARBOXYL
JRNL TITL 3 GROUP DEFINES CATHEPSIN H AMINOPEPTIDASE FUNCTION.
JRNL REF STRUCTURE V. 6 51 1998
JRNL REFN ISSN 0969-2126
JRNL PMID 9493267
JRNL DOI 10.1016/S0969-2126(98)00007-0
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : MAIN
REMARK 3 AUTHORS : TURK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 12932
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : R-FREE,KICKED OMIT MAP
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : NULL
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1308
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 : 1764
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 39
REMARK 3 SOLVENT ATOMS : 179
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) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
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 8PCH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000180011.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : JUL-96
REMARK 200 TEMPERATURE (KELVIN) : 289
REMARK 200 PH : 4.8
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 RUH2R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15946
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.980
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.11800
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MAIN
REMARK 200 STARTING MODEL: 2ACT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED USING SITTING
REMARK 280 DROP VAPOR DIFFUSION METHOD FROM 0.05M NA-ACETATE AND 5% MME PEG
REMARK 280 5K BUFFER, PH 4.8. CONCENTRATION OF APPLIED PROTEIN WAS 11 MG/
REMARK 280 ML., VAPOR DIFFUSION - SITTING DROP, VAPOR DIFFUSION, SITTING
REMARK 280 DROP
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 19.22100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 43.37850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.36500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 43.37850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 19.22100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.36500
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10090 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 6.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, P, B
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 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 TYR A 1
REMARK 475 GLU P 76
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS A 89 CG CD CE NZ
REMARK 480 HIS A 94 CB CG ND1 CD2 CE1 NE2
REMARK 480 GLU A 119 CG CD OE1 OE2
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 PRO A 99 C - N - CA ANGL. DEV. = 9.5 DEGREES
REMARK 500 PRO P 77 C - N - CA ANGL. DEV. = 9.1 DEGREES
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 PRO A 2 151.58 -38.22
REMARK 500 PRO P 77 171.89 -43.24
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ACT
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE.
DBREF 8PCH A 1 212 UNP O46427 CATH_PIG 116 335
DBREF 8PCH P 76 83 PDB 8PCH 8PCH 76 83
SEQRES 1 A 220 TYR PRO PRO SER MET ASP TRP ARG LYS LYS GLY ASN PHE
SEQRES 2 A 220 VAL SER PRO VAL LYS ASN GLN GLY SER CYS GLY SER CYS
SEQRES 3 A 220 TRP THR PHE SER THR THR GLY ALA LEU GLU SER ALA VAL
SEQRES 4 A 220 ALA ILE ALA THR GLY LYS MET LEU SER LEU ALA GLU GLN
SEQRES 5 A 220 GLN LEU VAL ASP CYS ALA GLN ASN PHE ASN ASN HIS GLY
SEQRES 6 A 220 CYS GLN GLY GLY LEU PRO SER GLN ALA PHE GLU TYR ILE
SEQRES 7 A 220 ARG TYR ASN LYS GLY ILE MET GLY GLU ASP THR TYR PRO
SEQRES 8 A 220 TYR LYS GLY GLN ASP ASP HIS CYS LYS PHE GLN PRO ASP
SEQRES 9 A 220 LYS ALA ILE ALA PHE VAL LYS ASP VAL ALA ASN ILE THR
SEQRES 10 A 220 MET ASN ASP GLU GLU ALA MET VAL GLU ALA VAL ALA LEU
SEQRES 11 A 220 TYR ASN PRO VAL SER PHE ALA PHE GLU VAL THR ASN ASP
SEQRES 12 A 220 PHE LEU MET TYR ARG LYS GLY ILE TYR SER SER THR SER
SEQRES 13 A 220 CYS HIS LYS THR PRO ASP LYS VAL ASN HIS ALA VAL LEU
SEQRES 14 A 220 ALA VAL GLY TYR GLY GLU GLU ASN GLY ILE PRO TYR TRP
SEQRES 15 A 220 ILE VAL LYS ASN SER TRP GLY PRO GLN TRP GLY MET ASN
SEQRES 16 A 220 GLY TYR PHE LEU ILE GLU ARG GLY LYS ASN MET CYS GLY
SEQRES 17 A 220 LEU ALA ALA CYS ALA SER TYR PRO ILE PRO LEU VAL
SEQRES 1 P 8 GLU PRO GLN ASN CYS SER ALA THR
MODRES 8PCH ASN A 112 ASN GLYCOSYLATION SITE
HET NAG B 1 27
HET NAG B 2 27
HET BMA B 3 22
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
FORMUL 3 NAG 2(C8 H15 N O6)
FORMUL 3 BMA C6 H12 O6
FORMUL 4 HOH *179(H2 O)
HELIX 1 1 TRP A 7 LYS A 10 1 4
HELIX 2 2 CYS A 25 THR A 42 1 18
HELIX 3 3 GLU A 50 PHE A 58B 1 11
HELIX 4 4 GLY A 62 GLN A 64 5 3
HELIX 5 5 PRO A 68 ASN A 78 1 11
HELIX 6 6 PRO A 99 LYS A 102A 5 3
HELIX 7 7 GLU A 118 LEU A 126A 1 10
HELIX 8 8 ASN A 139 MET A 143 1 5
HELIX 9 9 MET A 199 GLY A 201 5 3
SHEET 1 A 4 VAL A 130 PHE A 134 0
SHEET 2 A 4 HIS A 159 GLU A 168A-1 N ALA A 163 O VAL A 130
SHEET 3 A 4 ILE A 168D LYS A 174 -1 N LYS A 174 O LEU A 162
SHEET 4 A 4 TYR A 186 GLU A 190 -1 N ILE A 189 O TRP A 171
SHEET 1 B 2 VAL A 107 ASN A 112 0
SHEET 2 B 2 SER A 207 PRO A 211 -1 N ILE A 210 O LYS A 108
SSBOND 1 CYS A 22 CYS A 63 1555 1555 2.03
SSBOND 2 CYS A 56 CYS A 95 1555 1555 2.03
SSBOND 3 CYS A 154 CYS A 200 1555 1555 2.03
SSBOND 4 CYS A 205 CYS P 80 1555 1555 2.02
LINK ND2 ASN A 112 C1 NAG B 1 1555 1555 1.45
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.39
LINK O4 NAG B 2 C1 BMA B 3 1555 1555 1.38
SITE 1 ACT 2 CYS A 25 HIS A 159
CRYST1 38.442 68.730 86.757 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 0.026013 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014550 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011526 0.00000
(ATOM LINES ARE NOT SHOWN.)
END