HEADER HYDROLASE INHIBITOR 06-OCT-03 1R4C
TITLE N-TRUNCATED HUMAN CYSTATIN C; DIMERIC FORM WITH 3D DOMAIN SWAPPING
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYSTATIN C;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 FRAGMENT: HUMAN CYSTATIN C WITHOUT 10 N-TERMINAL RESIDUES;
COMPND 5 SYNONYM: NEUROENDOCRINE BASIC POLYPEPTIDE, GAMMA-TRACE, POST-GAMMA-
COMPND 6 GLOBULIN;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CST3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: MC1061;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PHD 313
KEYWDS HUMAN CYSTATIN C, N-TRUNCATION, 3D DOMAIN SWAPPING, AMYLOID
KEYWDS 2 FORMATION, INHIBITOR OF C1 AND C13 CYSTEINE PROTEASES, AMYLOID
KEYWDS 3 ANGIOPATHY AND CEREBRAL HEMORRHAGE, HYDROLASE INHIBITOR
EXPDTA X-RAY DIFFRACTION
AUTHOR R.JANOWSKI,M.ABRAHAMSON,A.GRUBB,M.JASKOLSKI
REVDAT 5 23-AUG-23 1R4C 1 REMARK
REVDAT 4 07-MAR-18 1R4C 1 REMARK
REVDAT 3 13-JUL-11 1R4C 1 VERSN
REVDAT 2 24-FEB-09 1R4C 1 VERSN
REVDAT 1 21-SEP-04 1R4C 0
JRNL AUTH R.JANOWSKI,M.ABRAHAMSON,A.GRUBB,M.JASKOLSKI
JRNL TITL DOMAIN SWAPPING IN N-TRUNCATED HUMAN CYSTATIN C.
JRNL REF J.MOL.BIOL. V. 341 151 2004
JRNL REFN ISSN 0022-2836
JRNL PMID 15312769
JRNL DOI 10.1016/J.JMB.2004.06.013
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.JANOWSKI,M.KOZAK,E.JANKOWSKA,Z.GRZONKA,A.GRUBB,
REMARK 1 AUTH 2 M.ABRAHAMSON,M.JASKOLSKI
REMARK 1 TITL HUMAN CYSTATIN C, AN AMYLOIDOGENIC PROTEIN, DIMERIZES
REMARK 1 TITL 2 THROUGH THREE-DIMENSIONAL DOMAIN SWAPPING
REMARK 1 REF NAT.STRUCT.BIOL. V. 8 316 2001
REMARK 1 REFN ISSN 1072-8368
REMARK 1 DOI 10.1038/86188
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.KOZAK,E.JANKOWSKA,R.JANOWSKI,Z.GRZONKA,A.GRUBB,
REMARK 1 AUTH 2 M.ALVAREZ FERNANDEZ,M.ABRAHAMSON,M.JASKOLSKI
REMARK 1 TITL EXPRESSION OF A SELENOMETHIONYL DERIVATIVE AND PRELIMINARY
REMARK 1 TITL 2 CRYSTALLOGRAPHIC STUDIES OF HUMAN CYSTATIN C
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 55 1939 1999
REMARK 1 REFN ISSN 0907-4449
REMARK 1 DOI 10.1107/S090744499901121X
REMARK 1 REFERENCE 3
REMARK 1 AUTH I.EKIEL,M.ABRAHAMSON,D.B.FULTON,P.LINDAHL,A.C.STORER,
REMARK 1 AUTH 2 W.LEVADOUX,M.LAFRANCE,S.LABELLE,Y.POMERLEAU,D.GROLEAU,
REMARK 1 AUTH 3 L.LESAUTEUR,K.GEHRING
REMARK 1 TITL NMR STRUCTURAL STUDIES OF HUMAN CYSTATIN C DIMERS AND
REMARK 1 TITL 2 MONOMERS
REMARK 1 REF J.MOL.BIOL. V. 271 266 1997
REMARK 1 REFN ISSN 0022-2836
REMARK 1 DOI 10.1006/JMBI.1997.1150
REMARK 2
REMARK 2 RESOLUTION. 2.18 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5
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) : 2.18
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 51566
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) : 0.220
REMARK 3 R VALUE (WORKING SET) : 0.218
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2632
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 REFLECTION IN BIN (WORKING SET) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE SET COUNT : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6912
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 205
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 36.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.75
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.84000
REMARK 3 B22 (A**2) : -0.47000
REMARK 3 B33 (A**2) : -0.36000
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): 0.284
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.219
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.226
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.514
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : NULL
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; 0.014 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; 1.635 ; 1.937
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; 4.519 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ;15.416 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; 0.102 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; 0.988 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; 1.849 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; 2.381 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; 4.096 ; 4.500
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): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
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 : 8
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 11 A 120
REMARK 3 ORIGIN FOR THE GROUP (A): 3.8134 12.3388 12.7846
REMARK 3 T TENSOR
REMARK 3 T11: 0.0781 T22: 0.0778
REMARK 3 T33: 0.0918 T12: -0.0010
REMARK 3 T13: 0.0320 T23: -0.0212
REMARK 3 L TENSOR
REMARK 3 L11: 0.8020 L22: 0.6842
REMARK 3 L33: 0.4648 L12: -0.5847
REMARK 3 L13: 0.2659 L23: -0.1455
REMARK 3 S TENSOR
REMARK 3 S11: -0.0252 S12: -0.0116 S13: -0.0307
REMARK 3 S21: -0.0299 S22: 0.0971 S23: 0.0073
REMARK 3 S31: -0.0362 S32: -0.0060 S33: 0.0067
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 11 B 120
REMARK 3 ORIGIN FOR THE GROUP (A): 7.7399 8.5143 15.3265
REMARK 3 T TENSOR
REMARK 3 T11: 0.0534 T22: 0.0962
REMARK 3 T33: 0.0882 T12: 0.0039
REMARK 3 T13: 0.0376 T23: -0.0111
REMARK 3 L TENSOR
REMARK 3 L11: 0.4035 L22: 0.5303
REMARK 3 L33: 0.7526 L12: -0.3001
REMARK 3 L13: 0.4550 L23: 0.0220
REMARK 3 S TENSOR
REMARK 3 S11: -0.0740 S12: 0.0818 S13: 0.0367
REMARK 3 S21: 0.0714 S22: 0.1170 S23: -0.0601
REMARK 3 S31: -0.0571 S32: 0.0094 S33: 0.0061
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 11 C 120
REMARK 3 ORIGIN FOR THE GROUP (A): 7.7762 -15.5213 8.5673
REMARK 3 T TENSOR
REMARK 3 T11: 0.1136 T22: 0.0581
REMARK 3 T33: 0.0950 T12: -0.0149
REMARK 3 T13: 0.0123 T23: 0.0075
REMARK 3 L TENSOR
REMARK 3 L11: 1.2607 L22: 0.4479
REMARK 3 L33: 0.9341 L12: -0.7461
REMARK 3 L13: -0.6287 L23: 0.3858
REMARK 3 S TENSOR
REMARK 3 S11: -0.0615 S12: 0.0017 S13: -0.0086
REMARK 3 S21: -0.0143 S22: -0.0005 S23: -0.0020
REMARK 3 S31: 0.0416 S32: 0.0527 S33: -0.0607
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 11 D 120
REMARK 3 ORIGIN FOR THE GROUP (A): 3.7328 -12.6671 12.2501
REMARK 3 T TENSOR
REMARK 3 T11: 0.0740 T22: 0.0739
REMARK 3 T33: 0.0551 T12: -0.0333
REMARK 3 T13: -0.0291 T23: 0.0062
REMARK 3 L TENSOR
REMARK 3 L11: 1.3179 L22: 0.5765
REMARK 3 L33: 0.8333 L12: -0.4522
REMARK 3 L13: -0.7610 L23: 0.1338
REMARK 3 S TENSOR
REMARK 3 S11: -0.0472 S12: 0.0130 S13: -0.0822
REMARK 3 S21: 0.0352 S22: -0.0446 S23: 0.0269
REMARK 3 S31: 0.0126 S32: 0.0183 S33: -0.0393
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 11 E 120
REMARK 3 ORIGIN FOR THE GROUP (A): 52.574 -10.884 37.7577
REMARK 3 T TENSOR
REMARK 3 T11: 0.0662 T22: 0.0853
REMARK 3 T33: 0.0769 T12: 0.0408
REMARK 3 T13: -0.0560 T23: 0.0077
REMARK 3 L TENSOR
REMARK 3 L11: 1.3047 L22: 0.9080
REMARK 3 L33: 0.7212 L12: 0.5938
REMARK 3 L13: -0.4690 L23: 0.1503
REMARK 3 S TENSOR
REMARK 3 S11: -0.0815 S12: -0.0925 S13: 0.0007
REMARK 3 S21: -0.1012 S22: 0.0525 S23: -0.0422
REMARK 3 S31: -0.0020 S32: 0.0416 S33: 0.0947
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 11 F 120
REMARK 3 ORIGIN FOR THE GROUP (A): 51.646 14.886 41.2682
REMARK 3 T TENSOR
REMARK 3 T11: 0.0878 T22: 0.0916
REMARK 3 T33: 0.0991 T12: 0.0147
REMARK 3 T13: -0.0029 T23: 0.0223
REMARK 3 L TENSOR
REMARK 3 L11: 0.5169 L22: 0.6311
REMARK 3 L33: 0.5723 L12: 0.5064
REMARK 3 L13: 0.3300 L23: 0.4234
REMARK 3 S TENSOR
REMARK 3 S11: -0.0491 S12: -0.0303 S13: -0.0477
REMARK 3 S21: -0.0256 S22: 0.0271 S23: 0.0255
REMARK 3 S31: -0.0750 S32: 0.0472 S33: 0.0576
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 11 G 120
REMARK 3 ORIGIN FOR THE GROUP (A): 48.401 -14.446 40.6937
REMARK 3 T TENSOR
REMARK 3 T11: 0.0834 T22: 0.0713
REMARK 3 T33: 0.1205 T12: 0.0460
REMARK 3 T13: -0.0209 T23: -0.0017
REMARK 3 L TENSOR
REMARK 3 L11: 0.7799 L22: 0.4005
REMARK 3 L33: 0.7171 L12: -0.2563
REMARK 3 L13: -0.2563 L23: -0.0763
REMARK 3 S TENSOR
REMARK 3 S11: -0.0341 S12: 0.0054 S13: 0.0320
REMARK 3 S21: 0.0385 S22: 0.0432 S23: 0.0141
REMARK 3 S31: 0.0530 S32: 0.0194 S33: 0.0283
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 11 H 120
REMARK 3 ORIGIN FOR THE GROUP (A): 49.099 11.311 37.3525
REMARK 3 T TENSOR
REMARK 3 T11: 0.0848 T22: 0.1124
REMARK 3 T33: 0.0973 T12: 0.0115
REMARK 3 T13: 0.0229 T23: 0.0196
REMARK 3 L TENSOR
REMARK 3 L11: 0.5952 L22: 0.5676
REMARK 3 L33: 0.4859 L12: 0.3492
REMARK 3 L13: 0.4573 L23: 0.2984
REMARK 3 S TENSOR
REMARK 3 S11: -0.0422 S12: -0.0112 S13: -0.0519
REMARK 3 S21: -0.0496 S22: -0.0087 S23: 0.0067
REMARK 3 S31: -0.0235 S32: 0.0519 S33: 0.0519
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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: THE REFINEMENT INCLUDED TLS PARAMETERS,
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIGID POSITIONS
REMARK 4
REMARK 4 1R4C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-OCT-03.
REMARK 100 THE DEPOSITION ID IS D_1000020420.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-MAR-99
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.1
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MAX II
REMARK 200 BEAMLINE : I711
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.104
REMARK 200 MONOCHROMATOR : SINGLE CRYSTAL
REMARK 200 OPTICS : NULL
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 : 52404
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.180
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 9.300
REMARK 200 R MERGE (I) : 0.04100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 33.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.18
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.26
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.12600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 10.90
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: HUMAN CYSTATIN C DIMER WITH SWAPPED DOMAINS (PDB
REMARK 200 ENTRY 1G96)
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.4M (NH4)H2PO4, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 292K, PH 8.1
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 103.03300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 103.03300
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 48.57350
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 49.81950
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 48.57350
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 49.81950
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 103.03300
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 48.57350
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 49.81950
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 103.03300
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 48.57350
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 49.81950
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8
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 EIGHT POLYPEPTIDE CHAINS ARE ASSEMBLED INTO 3D DOMAIN
REMARK 300 SWAPPED DIMERS IN THE FOLLOWING WAY: AB, CB, EF, GH
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: 5920 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350
REMARK 350 BIOMOLECULE: 2
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: 5960 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14000 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6030 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, 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 350
REMARK 350 BIOMOLECULE: 4
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: 5780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13920 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H
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: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 38700 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40600 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -193.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 38250 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -195.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H
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 -1.000000 0.000000 0.000000 97.14700
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 103.03300
REMARK 350
REMARK 350 BIOMOLECULE: 7
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -100.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350 APPLY THE FOLLOWING TO CHAINS: E, F
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 -48.57350
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 49.81950
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 8
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13720 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -100.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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: G, H
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 -48.57350
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -49.81950
REMARK 350 BIOMT3 2 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 GLY B 11
REMARK 475 GLY E 11
REMARK 475 GLY E 12
REMARK 475 GLY F 11
REMARK 475 GLY F 12
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 ARG E 24 CD NE CZ NH1 NH2
REMARK 480 LYS E 92 CD CE NZ
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 PRO E 78 N PRO E 78 CA 0.105
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 ASP A 15 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP A 81 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP A 87 CB - CG - OD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ASP B 28 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG B 45 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ARG B 45 NE - CZ - NH2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 ASP B 119 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP C 15 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP C 28 CB - CG - OD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ASP C 40 CB - CG - OD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 PRO C 78 N - CA - C ANGL. DEV. = 15.8 DEGREES
REMARK 500 ASP E 28 CB - CG - OD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ASP E 40 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG E 53 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ASP E 65 CB - CG - OD2 ANGL. DEV. = 6.9 DEGREES
REMARK 500 PRO E 78 C - N - CA ANGL. DEV. = 9.1 DEGREES
REMARK 500 PRO E 78 C - N - CD ANGL. DEV. = -14.5 DEGREES
REMARK 500 PRO E 78 N - CA - C ANGL. DEV. = 17.1 DEGREES
REMARK 500 ASP F 40 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 PRO F 78 C - N - CA ANGL. DEV. = 9.1 DEGREES
REMARK 500 PRO F 78 N - CA - C ANGL. DEV. = 17.6 DEGREES
REMARK 500 LEU F 80 N - CA - C ANGL. DEV. = 16.4 DEGREES
REMARK 500 ASP F 81 CB - CG - OD2 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ASP F 119 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP G 28 CB - CG - OD2 ANGL. DEV. = 6.9 DEGREES
REMARK 500 ASP G 40 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ARG G 45 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ASP H 15 CB - CG - OD2 ANGL. DEV. = 5.5 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 GLU B 19 16.09 -65.79
REMARK 500 THR B 76 37.14 -94.12
REMARK 500 ASN B 82 79.66 -118.40
REMARK 500 PRO B 84 141.39 -35.26
REMARK 500 ASN C 39 31.15 -98.65
REMARK 500 PRO C 78 -83.79 -42.83
REMARK 500 SER C 115 118.71 -168.08
REMARK 500 PRO D 13 123.76 -36.77
REMARK 500 LYS D 75 20.69 -78.56
REMARK 500 PRO D 78 160.80 -48.10
REMARK 500 PRO D 89 -77.77 -31.41
REMARK 500 SER D 115 119.03 -160.80
REMARK 500 GLN E 48 149.86 -176.52
REMARK 500 PRO E 78 -95.09 -52.22
REMARK 500 PRO E 89 -79.86 -26.55
REMARK 500 PRO F 13 102.11 -37.66
REMARK 500 ASN F 79 31.36 -84.52
REMARK 500 PRO F 89 -66.12 -27.79
REMARK 500 PRO G 13 102.97 -38.11
REMARK 500 THR G 76 5.27 -68.79
REMARK 500 ASN G 79 87.86 -49.06
REMARK 500 ASP G 119 107.96 -59.15
REMARK 500 PRO H 13 92.28 -48.37
REMARK 500 ASP H 15 162.01 -46.42
REMARK 500 VAL H 18 -32.55 -36.20
REMARK 500 PRO H 89 -79.40 -24.28
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1G96 RELATED DB: PDB
REMARK 900 HUMAN CYSTATIN C; DIMERIC FORM WITH 3D DOMAIN SWAPPING
REMARK 900 RELATED ID: 1CEW RELATED DB: PDB
REMARK 900 N-TERMINALLY TRUNCATED CHICKEN CYSTATIN
REMARK 900 RELATED ID: 1N9J RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF 3D DOMAIN SWAPPED DIMER OF STEFIN A
REMARK 900 RELATED ID: 1STF RELATED DB: PDB
REMARK 900 STEFIN B IN COMPLEX WITH PAPAIN
REMARK 900 RELATED ID: 1DVC RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF STEFIN A
REMARK 900 RELATED ID: 1A67 RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF CHICKEN CYSTATIN
DBREF 1R4C A 11 120 UNP P01034 CYTC_HUMAN 37 146
DBREF 1R4C B 11 120 UNP P01034 CYTC_HUMAN 37 146
DBREF 1R4C C 11 120 UNP P01034 CYTC_HUMAN 37 146
DBREF 1R4C D 11 120 UNP P01034 CYTC_HUMAN 37 146
DBREF 1R4C E 11 120 UNP P01034 CYTC_HUMAN 37 146
DBREF 1R4C F 11 120 UNP P01034 CYTC_HUMAN 37 146
DBREF 1R4C G 11 120 UNP P01034 CYTC_HUMAN 37 146
DBREF 1R4C H 11 120 UNP P01034 CYTC_HUMAN 37 146
SEQRES 1 A 110 GLY GLY PRO MET ASP ALA SER VAL GLU GLU GLU GLY VAL
SEQRES 2 A 110 ARG ARG ALA LEU ASP PHE ALA VAL GLY GLU TYR ASN LYS
SEQRES 3 A 110 ALA SER ASN ASP MET TYR HIS SER ARG ALA LEU GLN VAL
SEQRES 4 A 110 VAL ARG ALA ARG LYS GLN ILE VAL ALA GLY VAL ASN TYR
SEQRES 5 A 110 PHE LEU ASP VAL GLU LEU GLY ARG THR THR CYS THR LYS
SEQRES 6 A 110 THR GLN PRO ASN LEU ASP ASN CYS PRO PHE HIS ASP GLN
SEQRES 7 A 110 PRO HIS LEU LYS ARG LYS ALA PHE CYS SER PHE GLN ILE
SEQRES 8 A 110 TYR ALA VAL PRO TRP GLN GLY THR MET THR LEU SER LYS
SEQRES 9 A 110 SER THR CYS GLN ASP ALA
SEQRES 1 B 110 GLY GLY PRO MET ASP ALA SER VAL GLU GLU GLU GLY VAL
SEQRES 2 B 110 ARG ARG ALA LEU ASP PHE ALA VAL GLY GLU TYR ASN LYS
SEQRES 3 B 110 ALA SER ASN ASP MET TYR HIS SER ARG ALA LEU GLN VAL
SEQRES 4 B 110 VAL ARG ALA ARG LYS GLN ILE VAL ALA GLY VAL ASN TYR
SEQRES 5 B 110 PHE LEU ASP VAL GLU LEU GLY ARG THR THR CYS THR LYS
SEQRES 6 B 110 THR GLN PRO ASN LEU ASP ASN CYS PRO PHE HIS ASP GLN
SEQRES 7 B 110 PRO HIS LEU LYS ARG LYS ALA PHE CYS SER PHE GLN ILE
SEQRES 8 B 110 TYR ALA VAL PRO TRP GLN GLY THR MET THR LEU SER LYS
SEQRES 9 B 110 SER THR CYS GLN ASP ALA
SEQRES 1 C 110 GLY GLY PRO MET ASP ALA SER VAL GLU GLU GLU GLY VAL
SEQRES 2 C 110 ARG ARG ALA LEU ASP PHE ALA VAL GLY GLU TYR ASN LYS
SEQRES 3 C 110 ALA SER ASN ASP MET TYR HIS SER ARG ALA LEU GLN VAL
SEQRES 4 C 110 VAL ARG ALA ARG LYS GLN ILE VAL ALA GLY VAL ASN TYR
SEQRES 5 C 110 PHE LEU ASP VAL GLU LEU GLY ARG THR THR CYS THR LYS
SEQRES 6 C 110 THR GLN PRO ASN LEU ASP ASN CYS PRO PHE HIS ASP GLN
SEQRES 7 C 110 PRO HIS LEU LYS ARG LYS ALA PHE CYS SER PHE GLN ILE
SEQRES 8 C 110 TYR ALA VAL PRO TRP GLN GLY THR MET THR LEU SER LYS
SEQRES 9 C 110 SER THR CYS GLN ASP ALA
SEQRES 1 D 110 GLY GLY PRO MET ASP ALA SER VAL GLU GLU GLU GLY VAL
SEQRES 2 D 110 ARG ARG ALA LEU ASP PHE ALA VAL GLY GLU TYR ASN LYS
SEQRES 3 D 110 ALA SER ASN ASP MET TYR HIS SER ARG ALA LEU GLN VAL
SEQRES 4 D 110 VAL ARG ALA ARG LYS GLN ILE VAL ALA GLY VAL ASN TYR
SEQRES 5 D 110 PHE LEU ASP VAL GLU LEU GLY ARG THR THR CYS THR LYS
SEQRES 6 D 110 THR GLN PRO ASN LEU ASP ASN CYS PRO PHE HIS ASP GLN
SEQRES 7 D 110 PRO HIS LEU LYS ARG LYS ALA PHE CYS SER PHE GLN ILE
SEQRES 8 D 110 TYR ALA VAL PRO TRP GLN GLY THR MET THR LEU SER LYS
SEQRES 9 D 110 SER THR CYS GLN ASP ALA
SEQRES 1 E 110 GLY GLY PRO MET ASP ALA SER VAL GLU GLU GLU GLY VAL
SEQRES 2 E 110 ARG ARG ALA LEU ASP PHE ALA VAL GLY GLU TYR ASN LYS
SEQRES 3 E 110 ALA SER ASN ASP MET TYR HIS SER ARG ALA LEU GLN VAL
SEQRES 4 E 110 VAL ARG ALA ARG LYS GLN ILE VAL ALA GLY VAL ASN TYR
SEQRES 5 E 110 PHE LEU ASP VAL GLU LEU GLY ARG THR THR CYS THR LYS
SEQRES 6 E 110 THR GLN PRO ASN LEU ASP ASN CYS PRO PHE HIS ASP GLN
SEQRES 7 E 110 PRO HIS LEU LYS ARG LYS ALA PHE CYS SER PHE GLN ILE
SEQRES 8 E 110 TYR ALA VAL PRO TRP GLN GLY THR MET THR LEU SER LYS
SEQRES 9 E 110 SER THR CYS GLN ASP ALA
SEQRES 1 F 110 GLY GLY PRO MET ASP ALA SER VAL GLU GLU GLU GLY VAL
SEQRES 2 F 110 ARG ARG ALA LEU ASP PHE ALA VAL GLY GLU TYR ASN LYS
SEQRES 3 F 110 ALA SER ASN ASP MET TYR HIS SER ARG ALA LEU GLN VAL
SEQRES 4 F 110 VAL ARG ALA ARG LYS GLN ILE VAL ALA GLY VAL ASN TYR
SEQRES 5 F 110 PHE LEU ASP VAL GLU LEU GLY ARG THR THR CYS THR LYS
SEQRES 6 F 110 THR GLN PRO ASN LEU ASP ASN CYS PRO PHE HIS ASP GLN
SEQRES 7 F 110 PRO HIS LEU LYS ARG LYS ALA PHE CYS SER PHE GLN ILE
SEQRES 8 F 110 TYR ALA VAL PRO TRP GLN GLY THR MET THR LEU SER LYS
SEQRES 9 F 110 SER THR CYS GLN ASP ALA
SEQRES 1 G 110 GLY GLY PRO MET ASP ALA SER VAL GLU GLU GLU GLY VAL
SEQRES 2 G 110 ARG ARG ALA LEU ASP PHE ALA VAL GLY GLU TYR ASN LYS
SEQRES 3 G 110 ALA SER ASN ASP MET TYR HIS SER ARG ALA LEU GLN VAL
SEQRES 4 G 110 VAL ARG ALA ARG LYS GLN ILE VAL ALA GLY VAL ASN TYR
SEQRES 5 G 110 PHE LEU ASP VAL GLU LEU GLY ARG THR THR CYS THR LYS
SEQRES 6 G 110 THR GLN PRO ASN LEU ASP ASN CYS PRO PHE HIS ASP GLN
SEQRES 7 G 110 PRO HIS LEU LYS ARG LYS ALA PHE CYS SER PHE GLN ILE
SEQRES 8 G 110 TYR ALA VAL PRO TRP GLN GLY THR MET THR LEU SER LYS
SEQRES 9 G 110 SER THR CYS GLN ASP ALA
SEQRES 1 H 110 GLY GLY PRO MET ASP ALA SER VAL GLU GLU GLU GLY VAL
SEQRES 2 H 110 ARG ARG ALA LEU ASP PHE ALA VAL GLY GLU TYR ASN LYS
SEQRES 3 H 110 ALA SER ASN ASP MET TYR HIS SER ARG ALA LEU GLN VAL
SEQRES 4 H 110 VAL ARG ALA ARG LYS GLN ILE VAL ALA GLY VAL ASN TYR
SEQRES 5 H 110 PHE LEU ASP VAL GLU LEU GLY ARG THR THR CYS THR LYS
SEQRES 6 H 110 THR GLN PRO ASN LEU ASP ASN CYS PRO PHE HIS ASP GLN
SEQRES 7 H 110 PRO HIS LEU LYS ARG LYS ALA PHE CYS SER PHE GLN ILE
SEQRES 8 H 110 TYR ALA VAL PRO TRP GLN GLY THR MET THR LEU SER LYS
SEQRES 9 H 110 SER THR CYS GLN ASP ALA
FORMUL 9 HOH *205(H2 O)
HELIX 1 1 GLU A 20 SER A 38 1 19
HELIX 2 2 ASN A 79 CYS A 83 5 5
HELIX 3 3 PRO A 105 GLY A 108 5 4
HELIX 4 4 GLU B 20 SER B 38 1 19
HELIX 5 5 PRO B 105 GLY B 108 5 4
HELIX 6 6 GLU C 20 SER C 38 1 19
HELIX 7 7 ASN C 79 CYS C 83 5 5
HELIX 8 8 GLU D 20 SER D 38 1 19
HELIX 9 9 ASN D 79 CYS D 83 5 5
HELIX 10 10 GLU E 20 SER E 38 1 19
HELIX 11 11 PRO E 105 GLY E 108 5 4
HELIX 12 12 GLU F 20 SER F 38 1 19
HELIX 13 13 ASN F 79 CYS F 83 5 5
HELIX 14 14 GLU G 20 SER G 38 1 19
HELIX 15 15 PRO G 105 GLY G 108 5 4
HELIX 16 16 GLU H 20 SER H 38 1 19
HELIX 17 17 GLN H 88 LYS H 92 5 5
HELIX 18 18 PRO H 105 GLY H 108 5 4
SHEET 1 A 4 MET A 14 ASP A 15 0
SHEET 2 A 4 TYR A 42 THR A 74 -1 O LYS A 54 N MET A 14
SHEET 3 A 4 TYR B 42 THR B 74 -1 O ASN B 61 N GLN A 55
SHEET 4 A 4 MET B 14 ASP B 15 -1 N MET B 14 O LYS B 54
SHEET 1 B 6 THR A 109 ASP A 119 0
SHEET 2 B 6 LYS A 94 VAL A 104 -1 N PHE A 96 O GLN A 118
SHEET 3 B 6 TYR A 42 THR A 74 -1 N LEU A 68 O ALA A 95
SHEET 4 B 6 TYR B 42 THR B 74 -1 O ASN B 61 N GLN A 55
SHEET 5 B 6 LYS B 94 VAL B 104 -1 O CYS B 97 N VAL B 66
SHEET 6 B 6 THR B 109 ALA B 120 -1 O ALA B 120 N LYS B 94
SHEET 1 C 4 MET C 14 ASP C 15 0
SHEET 2 C 4 TYR C 42 THR C 74 -1 O LYS C 54 N MET C 14
SHEET 3 C 4 TYR D 42 THR D 74 -1 O PHE D 63 N ARG C 53
SHEET 4 C 4 MET D 14 ASP D 15 -1 N MET D 14 O LYS D 54
SHEET 1 D 6 MET C 110 ASP C 119 0
SHEET 2 D 6 LYS C 94 ALA C 103 -1 N PHE C 96 O GLN C 118
SHEET 3 D 6 TYR C 42 THR C 74 -1 N LEU C 68 O ALA C 95
SHEET 4 D 6 TYR D 42 THR D 74 -1 O PHE D 63 N ARG C 53
SHEET 5 D 6 LYS D 94 VAL D 104 -1 O CYS D 97 N VAL D 66
SHEET 6 D 6 THR D 109 ASP D 119 -1 O THR D 111 N TYR D 102
SHEET 1 E 4 MET E 14 ASP E 15 0
SHEET 2 E 4 TYR E 42 THR E 74 -1 O LYS E 54 N MET E 14
SHEET 3 E 4 TYR F 42 THR F 74 -1 O GLY F 59 N VAL E 57
SHEET 4 E 4 MET F 14 ASP F 15 -1 N MET F 14 O LYS F 54
SHEET 1 F 6 THR E 109 ASP E 119 0
SHEET 2 F 6 LYS E 94 VAL E 104 -1 N PHE E 96 O GLN E 118
SHEET 3 F 6 TYR E 42 THR E 74 -1 N LEU E 68 O ALA E 95
SHEET 4 F 6 TYR F 42 THR F 74 -1 O GLY F 59 N VAL E 57
SHEET 5 F 6 LYS F 94 VAL F 104 -1 O PHE F 99 N LEU F 64
SHEET 6 F 6 THR F 109 ASP F 119 -1 O THR F 111 N TYR F 102
SHEET 1 G 4 MET G 14 ASP G 15 0
SHEET 2 G 4 TYR G 42 THR G 74 -1 O LYS G 54 N MET G 14
SHEET 3 G 4 TYR H 42 THR H 74 -1 O ARG H 53 N PHE G 63
SHEET 4 G 4 MET H 14 ASP H 15 -1 N MET H 14 O LYS H 54
SHEET 1 H 6 THR G 109 ASP G 119 0
SHEET 2 H 6 LYS G 94 VAL G 104 -1 N PHE G 96 O GLN G 118
SHEET 3 H 6 TYR G 42 THR G 74 -1 N VAL G 60 O ALA G 103
SHEET 4 H 6 TYR H 42 THR H 74 -1 O ARG H 53 N PHE G 63
SHEET 5 H 6 ALA H 95 VAL H 104 -1 O ALA H 103 N VAL H 60
SHEET 6 H 6 THR H 109 ASP H 119 -1 O THR H 111 N TYR H 102
SSBOND 1 CYS A 73 CYS A 83 1555 1555 2.04
SSBOND 2 CYS A 97 CYS A 117 1555 1555 2.08
SSBOND 3 CYS B 73 CYS B 83 1555 1555 2.02
SSBOND 4 CYS B 97 CYS B 117 1555 1555 2.07
SSBOND 5 CYS C 73 CYS C 83 1555 1555 2.04
SSBOND 6 CYS C 97 CYS C 117 1555 1555 2.07
SSBOND 7 CYS D 73 CYS D 83 1555 1555 2.05
SSBOND 8 CYS D 97 CYS D 117 1555 1555 2.07
SSBOND 9 CYS E 73 CYS E 83 1555 1555 2.05
SSBOND 10 CYS E 97 CYS E 117 1555 1555 2.06
SSBOND 11 CYS F 73 CYS F 83 1555 1555 2.06
SSBOND 12 CYS F 97 CYS F 117 1555 1555 2.06
SSBOND 13 CYS G 73 CYS G 83 1555 1555 2.06
SSBOND 14 CYS G 97 CYS G 117 1555 1555 2.10
SSBOND 15 CYS H 73 CYS H 83 1555 1555 2.08
SSBOND 16 CYS H 97 CYS H 117 1555 1555 2.09
CRYST1 97.147 99.639 206.066 90.00 90.00 90.00 C 2 2 21 64
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 0.010294 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010036 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004853 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
