HEADER HYDROLASE/HYDROLASE INHIBITOR 22-APR-93 1LYB
TITLE CRYSTAL STRUCTURES OF NATIVE AND INHIBITED FORMS OF HUMAN CATHEPSIN D:
TITLE 2 IMPLICATIONS FOR LYSOSOMAL TARGETING AND DRUG DESIGN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATHEPSIN D;
COMPND 3 CHAIN: A, C;
COMPND 4 EC: 3.4.23.5;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: CATHEPSIN D;
COMPND 7 CHAIN: B, D;
COMPND 8 EC: 3.4.23.5;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: PEPSTATIN;
COMPND 11 CHAIN: I, J;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 ORGAN: LIVER;
SOURCE 6 TISSUE: LIVER;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 ORGAN: LIVER;
SOURCE 12 TISSUE: LIVER;
SOURCE 13 MOL_ID: 3;
SOURCE 14 ORGANISM_SCIENTIFIC: STREPTOMYCES ARGENTEOLUS SUBSP. TOYONAKENSIS;
SOURCE 15 ORGANISM_TAXID: 285516
KEYWDS LYSOSOMAL ASPARTIC PROTEASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR E.T.BALDWIN,T.N.BHAT,S.GULNIK,J.W.ERICKSON
REVDAT 7 15-NOV-23 1LYB 1 HETSYN ATOM
REVDAT 6 29-JUL-20 1LYB 1 COMPND REMARK HETNAM LINK
REVDAT 6 2 1 SITE ATOM
REVDAT 5 29-NOV-17 1LYB 1 HELIX
REVDAT 4 13-JUL-11 1LYB 1 VERSN
REVDAT 3 24-FEB-09 1LYB 1 VERSN
REVDAT 2 01-APR-03 1LYB 1 JRNL
REVDAT 1 31-JAN-94 1LYB 0
JRNL AUTH E.T.BALDWIN,T.N.BHAT,S.GULNIK,M.V.HOSUR,R.C.SOWDER 2ND.,
JRNL AUTH 2 R.E.CACHAU,J.COLLINS,A.M.SILVA,J.W.ERICKSON
JRNL TITL CRYSTAL STRUCTURES OF NATIVE AND INHIBITED FORMS OF HUMAN
JRNL TITL 2 CATHEPSIN D: IMPLICATIONS FOR LYSOSOMAL TARGETING AND DRUG
JRNL TITL 3 DESIGN.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 90 6796 1993
JRNL REFN ISSN 0027-8424
JRNL PMID 8393577
JRNL DOI 10.1073/PNAS.90.14.6796
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.GULNIK,E.T.BALDWIN,N.TARASOVA,J.ERICKSON
REMARK 1 TITL HUMAN LIVER CATHEPSIN D. PURIFICATION, CRYSTALLIZATION AND
REMARK 1 TITL 2 PRELIMINARY X-RAY DIFFRACTION ANALYSIS OF A LYSOSOMAL ENZYME
REMARK 1 REF J.MOL.BIOL. V. 227 265 1992
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.0
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
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) : 0.179
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 : 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 : 5282
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 128
REMARK 3 SOLVENT ATOMS : 44
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) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 3.200
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:
REMARK 3 THERE ARE TWO N-LINKED OLIGOSACCHARIDES ATTACHED AT
REMARK 3 RESIDUES ASN 70 AND ASN 199 OF EACH MOLECULE. FOUR SUGARS
REMARK 3 WERE INCLUDED FOR REFINEMENT AT ASN 70 AND A SINGLE
REMARK 3 N-LINKED NAG AT ASN 199. THE SUGARS ARE LINKED AS FOLLOWS:
REMARK 3
REMARK 3 ASN A 70 -- NAG A 1 -- NAG A 2 -- MAN A 3 -- MAN A 8
REMARK 3 ASN B 199 -- NAG B 1
REMARK 3 ASN C 70 -- NAG C 1 -- NAG C 2 -- MAN C 3 -- MAN C 8
REMARK 3 ASN D 199 -- NAG D 1
REMARK 4
REMARK 4 1LYB 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_1000174857.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR 3.0
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
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 69.40000
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 34.70000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 52.05000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 17.35000
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 86.75000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 300 REMARK: THE TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL
REMARK 300 YIELD APPROXIMATE COORDINATES FOR CHAINS *A* AND *B* WHEN
REMARK 300 APPLIED TO CHAINS *C* AND *D*, RESPECTIVELY.
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 20830 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26050 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -94.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, I, 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 APPLY THE FOLLOWING TO CHAINS: C, D, J, F
REMARK 350 BIOMT1 2 -0.500000 -0.866025 0.000000 62.95000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 109.03260
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 -34.70000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, I, 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: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, J, F
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 400
REMARK 400 COMPOUND
REMARK 400
REMARK 400 THE PEPSTATIN IS OLIGOPEPTIDE, A MEMBER OF ENZYME INHIBITOR CLASS.
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: PEPSTATIN
REMARK 400 CHAIN: I, J
REMARK 400 COMPONENT_1: PEPTIDE LIKE POLYMER
REMARK 400 DESCRIPTION: NULL
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLN A 97 CG CD OE1 NE2
REMARK 470 GLN C 97 CG CD OE1 NE2
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 HIS A 45 NE2 HIS A 45 CD2 -0.067
REMARK 500 HIS A 57 NE2 HIS A 57 CD2 -0.068
REMARK 500 HIS A 77 NE2 HIS A 77 CD2 -0.071
REMARK 500 HIS B 209 NE2 HIS B 209 CD2 -0.073
REMARK 500 HIS C 45 NE2 HIS C 45 CD2 -0.068
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 TRP A 40 CD1 - CG - CD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 TRP A 40 CE2 - CD2 - CG ANGL. DEV. = -5.8 DEGREES
REMARK 500 TRP A 54 CD1 - CG - CD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 TYR A 67 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 TRP B 206 CD1 - CG - CD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 TRP B 206 CE2 - CD2 - CG ANGL. DEV. = -5.0 DEGREES
REMARK 500 TRP B 319 CD1 - CG - CD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 TRP B 319 CE2 - CD2 - CG ANGL. DEV. = -6.0 DEGREES
REMARK 500 TRP B 319 CG - CD2 - CE3 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG B 335 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 TRP C 40 CD1 - CG - CD2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 TRP C 40 CB - CG - CD1 ANGL. DEV. = -10.1 DEGREES
REMARK 500 TRP C 40 CE2 - CD2 - CG ANGL. DEV. = -6.7 DEGREES
REMARK 500 TRP C 40 CG - CD2 - CE3 ANGL. DEV. = 7.7 DEGREES
REMARK 500 TYR C 59 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 ARG D 112 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG D 112 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 TRP D 206 CD1 - CG - CD2 ANGL. DEV. = 5.3 DEGREES
REMARK 500 TRP D 206 CE2 - CD2 - CG ANGL. DEV. = -5.3 DEGREES
REMARK 500 LEU D 256 N - CA - C ANGL. DEV. = -19.9 DEGREES
REMARK 500 TRP D 319 CD1 - CG - CD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 TRP D 319 CE2 - CD2 - CG ANGL. DEV. = -5.8 DEGREES
REMARK 500 ARG D 328 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG D 339 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG D 339 NE - CZ - NH2 ANGL. DEV. = -3.3 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 ASP A 12 2.17 57.96
REMARK 500 ASN A 70 -53.57 -141.56
REMARK 500 PRO A 95 -165.03 -65.65
REMARK 500 ASP B 174 58.73 -116.12
REMARK 500 THR B 201 -74.97 -89.23
REMARK 500 ALA B 204 -65.16 -135.79
REMARK 500 GLN B 212 155.91 179.97
REMARK 500 CYS B 222 55.87 39.62
REMARK 500 LEU B 256 -90.59 -106.41
REMARK 500 GLN B 258 77.53 29.08
REMARK 500 GLN B 296 -73.09 -128.41
REMARK 500 ALA B 297 -64.68 -92.39
REMARK 500 LYS B 299 166.56 61.55
REMARK 500 THR B 300 -19.05 61.55
REMARK 500 VAL I 2 113.63 82.53
REMARK 500 THR C 34 0.18 -66.16
REMARK 500 ASN C 70 -50.55 -152.11
REMARK 500 PRO C 95 -166.59 -76.12
REMARK 500 ALA D 204 -71.86 -129.77
REMARK 500 GLU D 224 -3.38 117.48
REMARK 500 LEU D 256 -110.32 -113.40
REMARK 500 SER D 269 -10.00 -52.26
REMARK 500 TYR D 290 31.85 -97.95
REMARK 500 ALA D 297 -77.62 68.87
REMARK 500 THR D 300 97.58 -56.91
REMARK 500 VAL J 2 113.26 121.03
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY A 1 PRO A 2 -33.56
REMARK 500 STA I 4 ALA I 5 -115.61
REMARK 500 PRO D 312 PRO D 313 149.72
REMARK 500 STA J 4 ALA J 5 -119.65
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 STA I 4 31.75
REMARK 500 STA J 4 27.81
REMARK 500
REMARK 500 REMARK: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 THERE ARE SEVERAL BIFURCATED SHEETS IN THIS STRUCTURE.
REMARK 700 THESE ARE REPRESENTED BY TWO SHEETS WHICH HAVE ONE OR MORE
REMARK 700 IDENTICAL STRANDS. SHEETS *1A1* AND *1B1* AND SHEETS *1A2*
REMARK 700 AND *1B2* REPRESENT ONE BIFURCATED SHEET IN EACH MOLECULE.
REMARK 700 SHEETS *2A1* AND *2B1* AND *2A2* AND *2B2* REPRESENT ONE
REMARK 700 BIFURCATED SHEET IN EACH MOLECULE.
DBREF 1LYB A 1 97 UNP P07339 CATD_HUMAN 65 161
DBREF 1LYB B 106 346 UNP P07339 CATD_HUMAN 170 410
DBREF 1LYB C 1 97 UNP P07339 CATD_HUMAN 65 161
DBREF 1LYB D 106 346 UNP P07339 CATD_HUMAN 170 410
DBREF 1LYB I 1 6 PDB 1LYB 1LYB 1 6
DBREF 1LYB J 1 6 PDB 1LYB 1LYB 1 6
SEQRES 1 A 97 GLY PRO ILE PRO GLU VAL LEU LYS ASN TYR MET ASP ALA
SEQRES 2 A 97 GLN TYR TYR GLY GLU ILE GLY ILE GLY THR PRO PRO GLN
SEQRES 3 A 97 CYS PHE THR VAL VAL PHE ASP THR GLY SER SER ASN LEU
SEQRES 4 A 97 TRP VAL PRO SER ILE HIS CYS LYS LEU LEU ASP ILE ALA
SEQRES 5 A 97 CYS TRP ILE HIS HIS LYS TYR ASN SER ASP LYS SER SER
SEQRES 6 A 97 THR TYR VAL LYS ASN GLY THR SER PHE ASP ILE HIS TYR
SEQRES 7 A 97 GLY SER GLY SER LEU SER GLY TYR LEU SER GLN ASP THR
SEQRES 8 A 97 VAL SER VAL PRO CYS GLN
SEQRES 1 B 241 GLY GLY VAL LYS VAL GLU ARG GLN VAL PHE GLY GLU ALA
SEQRES 2 B 241 THR LYS GLN PRO GLY ILE THR PHE ILE ALA ALA LYS PHE
SEQRES 3 B 241 ASP GLY ILE LEU GLY MET ALA TYR PRO ARG ILE SER VAL
SEQRES 4 B 241 ASN ASN VAL LEU PRO VAL PHE ASP ASN LEU MET GLN GLN
SEQRES 5 B 241 LYS LEU VAL ASP GLN ASN ILE PHE SER PHE TYR LEU SER
SEQRES 6 B 241 ARG ASP PRO ASP ALA GLN PRO GLY GLY GLU LEU MET LEU
SEQRES 7 B 241 GLY GLY THR ASP SER LYS TYR TYR LYS GLY SER LEU SER
SEQRES 8 B 241 TYR LEU ASN VAL THR ARG LYS ALA TYR TRP GLN VAL HIS
SEQRES 9 B 241 LEU ASP GLN VAL GLU VAL ALA SER GLY LEU THR LEU CYS
SEQRES 10 B 241 LYS GLU GLY CYS GLU ALA ILE VAL ASP THR GLY THR SER
SEQRES 11 B 241 LEU MET VAL GLY PRO VAL ASP GLU VAL ARG GLU LEU GLN
SEQRES 12 B 241 LYS ALA ILE GLY ALA VAL PRO LEU ILE GLN GLY GLU TYR
SEQRES 13 B 241 MET ILE PRO CYS GLU LYS VAL SER THR LEU PRO ALA ILE
SEQRES 14 B 241 THR LEU LYS LEU GLY GLY LYS GLY TYR LYS LEU SER PRO
SEQRES 15 B 241 GLU ASP TYR THR LEU LYS VAL SER GLN ALA GLY LYS THR
SEQRES 16 B 241 LEU CYS LEU SER GLY PHE MET GLY MET ASP ILE PRO PRO
SEQRES 17 B 241 PRO SER GLY PRO LEU TRP ILE LEU GLY ASP VAL PHE ILE
SEQRES 18 B 241 GLY ARG TYR TYR THR VAL PHE ASP ARG ASP ASN ASN ARG
SEQRES 19 B 241 VAL GLY PHE ALA GLU ALA ALA
SEQRES 1 I 6 IVA VAL VAL STA ALA STA
SEQRES 1 C 97 GLY PRO ILE PRO GLU VAL LEU LYS ASN TYR MET ASP ALA
SEQRES 2 C 97 GLN TYR TYR GLY GLU ILE GLY ILE GLY THR PRO PRO GLN
SEQRES 3 C 97 CYS PHE THR VAL VAL PHE ASP THR GLY SER SER ASN LEU
SEQRES 4 C 97 TRP VAL PRO SER ILE HIS CYS LYS LEU LEU ASP ILE ALA
SEQRES 5 C 97 CYS TRP ILE HIS HIS LYS TYR ASN SER ASP LYS SER SER
SEQRES 6 C 97 THR TYR VAL LYS ASN GLY THR SER PHE ASP ILE HIS TYR
SEQRES 7 C 97 GLY SER GLY SER LEU SER GLY TYR LEU SER GLN ASP THR
SEQRES 8 C 97 VAL SER VAL PRO CYS GLN
SEQRES 1 D 241 GLY GLY VAL LYS VAL GLU ARG GLN VAL PHE GLY GLU ALA
SEQRES 2 D 241 THR LYS GLN PRO GLY ILE THR PHE ILE ALA ALA LYS PHE
SEQRES 3 D 241 ASP GLY ILE LEU GLY MET ALA TYR PRO ARG ILE SER VAL
SEQRES 4 D 241 ASN ASN VAL LEU PRO VAL PHE ASP ASN LEU MET GLN GLN
SEQRES 5 D 241 LYS LEU VAL ASP GLN ASN ILE PHE SER PHE TYR LEU SER
SEQRES 6 D 241 ARG ASP PRO ASP ALA GLN PRO GLY GLY GLU LEU MET LEU
SEQRES 7 D 241 GLY GLY THR ASP SER LYS TYR TYR LYS GLY SER LEU SER
SEQRES 8 D 241 TYR LEU ASN VAL THR ARG LYS ALA TYR TRP GLN VAL HIS
SEQRES 9 D 241 LEU ASP GLN VAL GLU VAL ALA SER GLY LEU THR LEU CYS
SEQRES 10 D 241 LYS GLU GLY CYS GLU ALA ILE VAL ASP THR GLY THR SER
SEQRES 11 D 241 LEU MET VAL GLY PRO VAL ASP GLU VAL ARG GLU LEU GLN
SEQRES 12 D 241 LYS ALA ILE GLY ALA VAL PRO LEU ILE GLN GLY GLU TYR
SEQRES 13 D 241 MET ILE PRO CYS GLU LYS VAL SER THR LEU PRO ALA ILE
SEQRES 14 D 241 THR LEU LYS LEU GLY GLY LYS GLY TYR LYS LEU SER PRO
SEQRES 15 D 241 GLU ASP TYR THR LEU LYS VAL SER GLN ALA GLY LYS THR
SEQRES 16 D 241 LEU CYS LEU SER GLY PHE MET GLY MET ASP ILE PRO PRO
SEQRES 17 D 241 PRO SER GLY PRO LEU TRP ILE LEU GLY ASP VAL PHE ILE
SEQRES 18 D 241 GLY ARG TYR TYR THR VAL PHE ASP ARG ASP ASN ASN ARG
SEQRES 19 D 241 VAL GLY PHE ALA GLU ALA ALA
SEQRES 1 J 6 IVA VAL VAL STA ALA STA
MODRES 1LYB ASN A 70 ASN GLYCOSYLATION SITE
MODRES 1LYB ASN B 199 ASN GLYCOSYLATION SITE
MODRES 1LYB ASN C 70 ASN GLYCOSYLATION SITE
MODRES 1LYB ASN D 199 ASN GLYCOSYLATION SITE
HET IVA I 1 6
HET STA I 4 13
HET STA I 6 14
HET IVA J 1 6
HET STA J 4 13
HET STA J 6 14
HET NAG E 1 27
HET NAG E 2 27
HET BMA E 3 20
HET MAN E 4 22
HET NAG F 1 27
HET NAG F 2 27
HET BMA F 3 20
HET MAN F 4 22
HET NAG B 1 28
HET NAG D 1 28
HETNAM IVA ISOVALERIC ACID
HETNAM STA STATINE
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-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
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
FORMUL 3 IVA 2(C5 H10 O2)
FORMUL 3 STA 4(C8 H17 N O3)
FORMUL 7 NAG 6(C8 H15 N O6)
FORMUL 7 BMA 2(C6 H12 O6)
FORMUL 7 MAN 2(C6 H12 O6)
FORMUL 11 HOH *44(H2 O)
HELIX 1 A11 LYS A 47 ILE A 55 1 9
HELIX 2 A21 ILE B 124 ALA B 129 1 6
HELIX 3 A31 PRO B 149 LEU B 159 1 11
HELIX 4 A41 PRO B 240 GLY B 252 1 13
HELIX 5 A51 PRO B 264 LEU B 271 1 8
HELIX 6 A61 SER B 286 THR B 291 1 6
HELIX 7 A71 GLY B 322 GLY B 327 1 6
HELIX 8 A12 LYS C 47 ILE C 55 1 9
HELIX 9 A22 ILE D 124 ALA D 129 1 6
HELIX 10 A32 PRO D 149 LEU D 159 1 11
HELIX 11 A42 PRO D 240 GLY D 252 1 13
HELIX 12 A52 PRO D 264 LEU D 271 1 8
HELIX 13 A62 SER D 286 THR D 291 1 6
HELIX 14 A72 GLY D 322 GLY D 327 1 6
SHEET 1 I1 6 ILE A 3 LEU A 7 0
SHEET 2 I1 6 GLY B 178 GLY B 184 -1
SHEET 3 I1 6 ILE B 164 SER B 170 -1
SHEET 4 I1 6 TYR B 330 ASP B 334 -1
SHEET 5 I1 6 ASN B 337 ALA B 346 -1
SHEET 6 I1 6 TYR B 190 VAL B 200 -1
SHEET 1 II1 4 VAL B 254 LEU B 256 0
SHEET 2 II1 4 GLU B 260 ILE B 263 -1
SHEET 3 II1 4 LEU B 301 SER B 304 -1
SHEET 4 II1 4 GLN B 296 GLY B 298 -1
SHEET 1 1A1 9 VAL A 68 TYR A 78 0
SHEET 2 1A1 9 GLY A 81 ASP A 90 -1
SHEET 3 1A1 9 GLN B 113 LYS B 120 -1
SHEET 4 1A1 9 ASN A 38 SER A 43 1
SHEET 5 1A1 9 PHE B 131 MET B 137 -1
SHEET 6 1A1 9 GLN A 26 ASP A 33 1
SHEET 7 1A1 9 GLN A 14 GLY A 22 -1
SHEET 8 1A1 9 LYS A 8 TYR A 10 -1
SHEET 9 1A1 9 VAL B 110 ARG B 112 -1
SHEET 1 1B1 9 VAL A 68 TYR A 78 0
SHEET 2 1B1 9 GLY A 81 ASP A 90 -1
SHEET 3 1B1 9 GLN B 113 LYS B 120 -1
SHEET 4 1B1 9 ASN A 38 SER A 43 1
SHEET 5 1B1 9 PHE B 131 MET B 137 -1
SHEET 6 1B1 9 GLN A 26 ASP A 33 1
SHEET 7 1B1 9 GLN A 14 GLY A 22 -1
SHEET 8 1B1 9 THR A 91 CYS A 96 -1
SHEET 9 1B1 9 VAL B 110 ARG B 112 -1
SHEET 1 2A1 7 LYS B 281 LEU B 285 0
SHEET 2 2A1 7 ALA B 273 LEU B 278 -1
SHEET 3 2A1 7 TRP B 206 ALA B 216 -1
SHEET 4 2A1 7 LEU B 219 LEU B 221 -1
SHEET 5 2A1 7 LEU B 219 LYS B 223 1
SHEET 6 2A1 7 THR B 234 GLY B 239 -1
SHEET 7 2A1 7 GLY B 305 MET B 309 1
SHEET 1 2B1 7 LYS B 281 LEU B 285 0
SHEET 2 2B1 7 ALA B 273 LEU B 278 -1
SHEET 3 2B1 7 TRP B 206 ALA B 216 -1
SHEET 4 2B1 7 CYS B 226 ASP B 231 -1
SHEET 5 2B1 7 LEU B 219 LYS B 223 1
SHEET 6 2B1 7 THR B 234 GLY B 239 -1
SHEET 7 2B1 7 GLY B 305 MET B 309 1
SHEET 1 I2 6 ILE C 3 LEU C 7 0
SHEET 2 I2 6 GLY D 178 GLY D 184 -1
SHEET 3 I2 6 ILE D 164 SER D 170 -1
SHEET 4 I2 6 TYR D 330 ASP D 334 -1
SHEET 5 I2 6 ASN D 337 ALA D 346 -1
SHEET 6 I2 6 TYR D 190 VAL D 200 -1
SHEET 1 II2 4 VAL D 254 LEU D 256 0
SHEET 2 II2 4 GLU D 260 ILE D 263 -1
SHEET 3 II2 4 LEU D 301 SER D 304 -1
SHEET 4 II2 4 GLN D 296 GLY D 298 -1
SHEET 1 1A2 9 VAL C 68 TYR C 78 0
SHEET 2 1A2 9 GLY C 81 ASP C 90 -1
SHEET 3 1A2 9 GLN D 113 LYS D 120 -1
SHEET 4 1A2 9 ASN C 38 SER C 43 1
SHEET 5 1A2 9 PHE D 131 MET D 137 -1
SHEET 6 1A2 9 GLN C 26 ASP C 33 1
SHEET 7 1A2 9 GLN C 14 GLY C 22 -1
SHEET 8 1A2 9 LYS C 8 TYR C 10 -1
SHEET 9 1A2 9 VAL D 110 ARG D 112 -1
SHEET 1 1B2 9 VAL C 68 TYR C 78 0
SHEET 2 1B2 9 GLY C 81 ASP C 90 -1
SHEET 3 1B2 9 GLN D 113 LYS D 120 -1
SHEET 4 1B2 9 ASN C 38 SER C 43 1
SHEET 5 1B2 9 PHE D 131 MET D 137 -1
SHEET 6 1B2 9 GLN C 26 ASP C 33 1
SHEET 7 1B2 9 GLN C 14 GLY C 22 -1
SHEET 8 1B2 9 THR C 91 CYS C 96 -1
SHEET 9 1B2 9 VAL D 110 ARG D 112 -1
SHEET 1 2A2 7 LYS D 281 LEU D 285 0
SHEET 2 2A2 7 ALA D 273 LEU D 278 -1
SHEET 3 2A2 7 TRP D 206 ALA D 216 -1
SHEET 4 2A2 7 LEU D 219 LEU D 221 -1
SHEET 5 2A2 7 LEU D 219 LYS D 223 1
SHEET 6 2A2 7 THR D 234 GLY D 239 -1
SHEET 7 2A2 7 GLY D 305 MET D 309 1
SHEET 1 2B2 7 LYS D 281 LEU D 285 0
SHEET 2 2B2 7 ALA D 273 LEU D 278 -1
SHEET 3 2B2 7 TRP D 206 ALA D 216 -1
SHEET 4 2B2 7 CYS D 226 ASP D 231 -1
SHEET 5 2B2 7 LEU D 219 LYS D 223 1
SHEET 6 2B2 7 THR D 234 GLY D 239 -1
SHEET 7 2B2 7 GLY D 305 MET D 309 1
SSBOND 1 CYS A 27 CYS A 96 1555 1555 2.03
SSBOND 2 CYS A 46 CYS A 53 1555 1555 2.03
SSBOND 3 CYS B 222 CYS B 226 1555 1555 2.00
SSBOND 4 CYS B 265 CYS B 302 1555 1555 2.04
SSBOND 5 CYS C 27 CYS C 96 1555 1555 2.02
SSBOND 6 CYS C 46 CYS C 53 1555 1555 1.99
SSBOND 7 CYS D 222 CYS D 226 1555 1555 2.02
SSBOND 8 CYS D 265 CYS D 302 1555 1555 2.02
LINK ND2 ASN A 70 C1 NAG E 1 1555 1555 1.49
LINK C1 NAG B 1 ND2 ASN B 199 1555 1555 1.49
LINK C IVA I 1 N VAL I 2 1555 1555 1.34
LINK C VAL I 3 N STA I 4 1555 1555 1.32
LINK C STA I 4 N ALA I 5 1555 1555 1.33
LINK C ALA I 5 N STA I 6 1555 1555 1.34
LINK ND2 ASN C 70 C1 NAG F 1 1555 1555 1.46
LINK C1 NAG D 1 ND2 ASN D 199 1555 1555 1.48
LINK C IVA J 1 N VAL J 2 1555 1555 1.34
LINK C VAL J 3 N STA J 4 1555 1555 1.32
LINK C STA J 4 N ALA J 5 1555 1555 1.34
LINK C ALA J 5 N STA J 6 1555 1555 1.33
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.44
LINK O4 NAG E 2 C1 BMA E 3 1555 1555 1.41
LINK O6 BMA E 3 C1 MAN E 4 1555 1555 1.46
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.46
LINK O4 NAG F 2 C1 BMA F 3 1555 1555 1.45
LINK O6 BMA F 3 C1 MAN F 4 1555 1555 1.42
CISPEP 1 THR A 23 PRO A 24 0 -3.00
CISPEP 2 VAL A 94 PRO A 95 0 -6.94
CISPEP 3 GLN B 176 PRO B 177 0 -23.69
CISPEP 4 PRO B 313 PRO B 314 0 10.09
CISPEP 5 GLY B 316 PRO B 317 0 8.40
CISPEP 6 GLY C 1 PRO C 2 0 -1.44
CISPEP 7 THR C 23 PRO C 24 0 -11.14
CISPEP 8 VAL C 94 PRO C 95 0 -17.72
CISPEP 9 GLN D 176 PRO D 177 0 -11.29
CISPEP 10 PRO D 313 PRO D 314 0 14.65
CISPEP 11 GLY D 316 PRO D 317 0 -12.99
CRYST1 125.900 125.900 104.100 90.00 90.00 120.00 P 65 12
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 0.007943 0.004586 0.000000 0.00000
SCALE2 0.000000 0.009172 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009606 0.00000
MTRIX1 1 0.735300 0.674700 -0.064150 -9.57840 1
MTRIX2 1 0.608800 -0.699200 -0.374800 129.91299 1
MTRIX3 1 -0.297800 0.236600 -0.924900 10.65180 1
(ATOM LINES ARE NOT SHOWN.)
END