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HEADER HYDROLASE 25-SEP-13 4MWS
TITLE CRYSTAL STRUCTURE OF HUMAN PPCA (TRIGONAL CRYSTAL FORM 1)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYSOSOMAL PROTECTIVE PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CARBOXYPEPTIDASE C, CARBOXYPEPTIDASE L, CATHEPSIN A,
COMPND 5 PROTECTIVE PROTEIN CATHEPSIN A, PPCA, PROTECTIVE PROTEIN FOR BETA-
COMPND 6 GALACTOSIDASE;
COMPND 7 EC: 3.4.16.5;
COMPND 8 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: CTSA, PPGB;
SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: HI-FIVE;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: STABLE CELL LINE;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PIB/V5-HIS-TOPO TA
KEYWDS CATHEPSIN A, GLYCOPROTEIN, SERINE PROTEASE, CARBOXYPEPTIDASE,
KEYWDS 2 PROTECTIVE PROTEIN, N-LINKED GLYCOSYLATION, PROTEOLYTICALLY
KEYWDS 3 ACTIVATED FORM, LYSOSOMAL ENZYME, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.KOLLI,S.C.GARMAN
REVDAT 2 15-APR-15 4MWS 1 JRNL
REVDAT 1 12-MAR-14 4MWS 0
JRNL AUTH N.KOLLI,S.C.GARMAN
JRNL TITL PROTEOLYTIC ACTIVATION OF HUMAN CATHEPSIN A.
JRNL REF J.BIOL.CHEM. V. 289 11592 2014
JRNL REFN ISSN 0021-9258
JRNL PMID 24599961
JRNL DOI 10.1074/JBC.M113.524280
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.89
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 25868
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) : 0.149
REMARK 3 R VALUE (WORKING SET) : 0.146
REMARK 3 FREE R VALUE : 0.195
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1258
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1781
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.38
REMARK 3 BIN R VALUE (WORKING SET) : 0.2450
REMARK 3 BIN FREE R VALUE SET COUNT : 98
REMARK 3 BIN FREE R VALUE : 0.3590
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6596
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 149
REMARK 3 SOLVENT ATOMS : 4
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 75.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 67.87
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -19.15000
REMARK 3 B22 (A**2) : -19.15000
REMARK 3 B33 (A**2) : 38.29000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.062
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.186
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.907
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.927
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6950 ; 0.008 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 6309 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9466 ; 1.164 ; 1.978
REMARK 3 BOND ANGLES OTHERS (DEGREES): 14475 ; 0.785 ; 3.002
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 822 ; 6.186 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 340 ;38.429 ;24.824
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1076 ;14.270 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 26 ;15.916 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1017 ; 0.063 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7916 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1670 ; 0.002 ; 0.020
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 ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 1 452 B 1 452 25478 0.040 0.050
REMARK 3
REMARK 3 TWIN DETAILS
REMARK 3 NUMBER OF TWIN DOMAINS : 2
REMARK 3 TWIN DOMAIN : 1
REMARK 3 TWIN OPERATOR : H, K, L
REMARK 3 TWIN FRACTION : 0.530
REMARK 3 TWIN DOMAIN : 2
REMARK 3 TWIN OPERATOR : -H, -K, L
REMARK 3 TWIN FRACTION : 0.470
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 182
REMARK 3 RESIDUE RANGE : A 183 A 303
REMARK 3 RESIDUE RANGE : A 304 A 452
REMARK 3 ORIGIN FOR THE GROUP (A): 16.9560 -26.5930 -6.4880
REMARK 3 T TENSOR
REMARK 3 T11: 0.1246 T22: 0.2069
REMARK 3 T33: 0.0045 T12: -0.0033
REMARK 3 T13: -0.0040 T23: 0.0139
REMARK 3 L TENSOR
REMARK 3 L11: 0.2639 L22: 1.0286
REMARK 3 L33: 0.3084 L12: -0.0568
REMARK 3 L13: -0.1089 L23: -0.0344
REMARK 3 S TENSOR
REMARK 3 S11: -0.0010 S12: 0.0322 S13: -0.0077
REMARK 3 S21: -0.0365 S22: 0.0185 S23: -0.0310
REMARK 3 S31: -0.0376 S32: -0.0617 S33: -0.0175
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 182
REMARK 3 RESIDUE RANGE : B 183 B 303
REMARK 3 RESIDUE RANGE : B 304 B 452
REMARK 3 ORIGIN FOR THE GROUP (A): 38.7210 -62.8870 -10.2820
REMARK 3 T TENSOR
REMARK 3 T11: 0.1834 T22: 0.1815
REMARK 3 T33: 0.0210 T12: 0.0428
REMARK 3 T13: 0.0385 T23: 0.0227
REMARK 3 L TENSOR
REMARK 3 L11: 0.9145 L22: 0.9212
REMARK 3 L33: 0.3251 L12: -0.6097
REMARK 3 L13: -0.4171 L23: 0.1581
REMARK 3 S TENSOR
REMARK 3 S11: -0.1472 S12: -0.1046 S13: -0.0456
REMARK 3 S21: 0.0448 S22: 0.0782 S23: -0.0383
REMARK 3 S31: 0.1546 S32: 0.0931 S33: 0.0690
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 4MWS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-OCT-13.
REMARK 100 THE RCSB ID CODE IS RCSB082463.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-AUG-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : SI(111) DOUBLE CRYSTAL
REMARK 200 OPTICS : FOCUSING MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : PILATUS CBF
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25989
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : 0.14900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 5.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.20
REMARK 200 R MERGE FOR SHELL (I) : 0.88400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 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: PHASER
REMARK 200 STARTING MODEL: 1IVY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 3350, 0.1M SODIUM FORMATE, PH
REMARK 280 7.0, VAPOR DIFFUSION, SITTING DROP, 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 33.26833
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 66.53667
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 66.53667
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 33.26833
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: 6240 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33220 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 20.0 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER A 289
REMARK 465 HIS A 290
REMARK 465 PHE A 291
REMARK 465 ARG A 292
REMARK 465 SER A 293
REMARK 465 GLY A 294
REMARK 465 ASP A 295
REMARK 465 LYS A 296
REMARK 465 VAL A 297
REMARK 465 HIS A 453
REMARK 465 HIS A 454
REMARK 465 HIS A 455
REMARK 465 HIS A 456
REMARK 465 HIS A 457
REMARK 465 HIS A 458
REMARK 465 SER B 289
REMARK 465 HIS B 290
REMARK 465 PHE B 291
REMARK 465 ARG B 292
REMARK 465 SER B 293
REMARK 465 GLY B 294
REMARK 465 ASP B 295
REMARK 465 LYS B 296
REMARK 465 VAL B 297
REMARK 465 HIS B 453
REMARK 465 HIS B 454
REMARK 465 HIS B 455
REMARK 465 HIS B 456
REMARK 465 HIS B 457
REMARK 465 HIS B 458
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 GLN A 8 -79.48 -86.28
REMARK 500 ASP A 44 75.34 59.76
REMARK 500 HIS A 70 23.34 -144.33
REMARK 500 LYS A 112 16.21 59.56
REMARK 500 PHE A 136 64.68 -119.90
REMARK 500 SER A 150 -131.88 61.63
REMARK 500 ASN A 170 59.61 -91.06
REMARK 500 ASN A 178 59.94 34.02
REMARK 500 GLN A 215 85.20 35.23
REMARK 500 ASN A 216 13.52 83.27
REMARK 500 SER A 242 13.66 -144.68
REMARK 500 ASN A 248 100.09 -161.67
REMARK 500 ASN A 388 74.51 47.32
REMARK 500 GLU A 392 -83.37 -108.27
REMARK 500 ASP A 404 -48.71 79.58
REMARK 500 HIS A 418 -6.21 76.67
REMARK 500 GLN B 8 -78.93 -85.61
REMARK 500 ASP B 44 75.86 58.31
REMARK 500 HIS B 70 23.77 -144.61
REMARK 500 LYS B 112 17.43 59.39
REMARK 500 SER B 150 -131.94 61.86
REMARK 500 ASN B 170 59.09 -90.33
REMARK 500 ASN B 178 60.95 33.38
REMARK 500 SER B 242 13.69 -144.25
REMARK 500 ASN B 248 99.99 -161.45
REMARK 500 ASN B 388 74.44 48.16
REMARK 500 GLU B 392 -83.48 -108.77
REMARK 500 ASP B 404 -47.40 78.75
REMARK 500 HIS B 418 -3.08 73.04
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 NAG A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 506
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1IVY RELATED DB: PDB
REMARK 900 ZYMOGEN FORM
REMARK 900 RELATED ID: 4MWT RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 AN UNIDENTIFIED PROTEASE CONVERTED THE ZYMOGEN INTO ACTIVE ENZYME.
REMARK 999 PUTATIVE TERMINI ASSUME PROTEOLYTIC REMOVAL OF 263-292, CONSISTENT
REMARK 999 WITH MASS SPECTROMETRY AND N-TERMINAL SEQUENCING DATA.
DBREF 4MWS A 1 452 UNP P10619 PPGB_HUMAN 29 480
DBREF 4MWS B 1 452 UNP P10619 PPGB_HUMAN 29 480
SEQADV 4MWS A UNP P10619 TYR 291 DELETION
SEQADV 4MWS A UNP P10619 GLU 292 DELETION
SEQADV 4MWS A UNP P10619 LYS 293 DELETION
SEQADV 4MWS A UNP P10619 ASP 294 DELETION
SEQADV 4MWS A UNP P10619 THR 295 DELETION
SEQADV 4MWS A UNP P10619 VAL 296 DELETION
SEQADV 4MWS A UNP P10619 VAL 297 DELETION
SEQADV 4MWS A UNP P10619 VAL 298 DELETION
SEQADV 4MWS A UNP P10619 GLN 299 DELETION
SEQADV 4MWS A UNP P10619 ASP 300 DELETION
SEQADV 4MWS A UNP P10619 LEU 301 DELETION
SEQADV 4MWS A UNP P10619 GLY 302 DELETION
SEQADV 4MWS A UNP P10619 ASN 303 DELETION
SEQADV 4MWS A UNP P10619 ILE 304 DELETION
SEQADV 4MWS A UNP P10619 PHE 305 DELETION
SEQADV 4MWS A UNP P10619 THR 306 DELETION
SEQADV 4MWS A UNP P10619 ARG 307 DELETION
SEQADV 4MWS A UNP P10619 LEU 308 DELETION
SEQADV 4MWS A UNP P10619 PRO 309 DELETION
SEQADV 4MWS A UNP P10619 LEU 310 DELETION
SEQADV 4MWS A UNP P10619 LYS 311 DELETION
SEQADV 4MWS A UNP P10619 ARG 312 DELETION
SEQADV 4MWS A UNP P10619 MET 313 DELETION
SEQADV 4MWS A UNP P10619 TRP 314 DELETION
SEQADV 4MWS A UNP P10619 HIS 315 DELETION
SEQADV 4MWS A UNP P10619 GLN 316 DELETION
SEQADV 4MWS A UNP P10619 ALA 317 DELETION
SEQADV 4MWS A UNP P10619 LEU 318 DELETION
SEQADV 4MWS A UNP P10619 LEU 319 DELETION
SEQADV 4MWS A UNP P10619 ARG 320 DELETION
SEQADV 4MWS HIS A 453 UNP P10619 EXPRESSION TAG
SEQADV 4MWS HIS A 454 UNP P10619 EXPRESSION TAG
SEQADV 4MWS HIS A 455 UNP P10619 EXPRESSION TAG
SEQADV 4MWS HIS A 456 UNP P10619 EXPRESSION TAG
SEQADV 4MWS HIS A 457 UNP P10619 EXPRESSION TAG
SEQADV 4MWS HIS A 458 UNP P10619 EXPRESSION TAG
SEQADV 4MWS B UNP P10619 TYR 291 DELETION
SEQADV 4MWS B UNP P10619 GLU 292 DELETION
SEQADV 4MWS B UNP P10619 LYS 293 DELETION
SEQADV 4MWS B UNP P10619 ASP 294 DELETION
SEQADV 4MWS B UNP P10619 THR 295 DELETION
SEQADV 4MWS B UNP P10619 VAL 296 DELETION
SEQADV 4MWS B UNP P10619 VAL 297 DELETION
SEQADV 4MWS B UNP P10619 VAL 298 DELETION
SEQADV 4MWS B UNP P10619 GLN 299 DELETION
SEQADV 4MWS B UNP P10619 ASP 300 DELETION
SEQADV 4MWS B UNP P10619 LEU 301 DELETION
SEQADV 4MWS B UNP P10619 GLY 302 DELETION
SEQADV 4MWS B UNP P10619 ASN 303 DELETION
SEQADV 4MWS B UNP P10619 ILE 304 DELETION
SEQADV 4MWS B UNP P10619 PHE 305 DELETION
SEQADV 4MWS B UNP P10619 THR 306 DELETION
SEQADV 4MWS B UNP P10619 ARG 307 DELETION
SEQADV 4MWS B UNP P10619 LEU 308 DELETION
SEQADV 4MWS B UNP P10619 PRO 309 DELETION
SEQADV 4MWS B UNP P10619 LEU 310 DELETION
SEQADV 4MWS B UNP P10619 LYS 311 DELETION
SEQADV 4MWS B UNP P10619 ARG 312 DELETION
SEQADV 4MWS B UNP P10619 MET 313 DELETION
SEQADV 4MWS B UNP P10619 TRP 314 DELETION
SEQADV 4MWS B UNP P10619 HIS 315 DELETION
SEQADV 4MWS B UNP P10619 GLN 316 DELETION
SEQADV 4MWS B UNP P10619 ALA 317 DELETION
SEQADV 4MWS B UNP P10619 LEU 318 DELETION
SEQADV 4MWS B UNP P10619 LEU 319 DELETION
SEQADV 4MWS B UNP P10619 ARG 320 DELETION
SEQADV 4MWS HIS B 453 UNP P10619 EXPRESSION TAG
SEQADV 4MWS HIS B 454 UNP P10619 EXPRESSION TAG
SEQADV 4MWS HIS B 455 UNP P10619 EXPRESSION TAG
SEQADV 4MWS HIS B 456 UNP P10619 EXPRESSION TAG
SEQADV 4MWS HIS B 457 UNP P10619 EXPRESSION TAG
SEQADV 4MWS HIS B 458 UNP P10619 EXPRESSION TAG
SEQRES 1 A 428 ALA PRO ASP GLN ASP GLU ILE GLN ARG LEU PRO GLY LEU
SEQRES 2 A 428 ALA LYS GLN PRO SER PHE ARG GLN TYR SER GLY TYR LEU
SEQRES 3 A 428 LYS GLY SER GLY SER LYS HIS LEU HIS TYR TRP PHE VAL
SEQRES 4 A 428 GLU SER GLN LYS ASP PRO GLU ASN SER PRO VAL VAL LEU
SEQRES 5 A 428 TRP LEU ASN GLY GLY PRO GLY CYS SER SER LEU ASP GLY
SEQRES 6 A 428 LEU LEU THR GLU HIS GLY PRO PHE LEU VAL GLN PRO ASP
SEQRES 7 A 428 GLY VAL THR LEU GLU TYR ASN PRO TYR SER TRP ASN LEU
SEQRES 8 A 428 ILE ALA ASN VAL LEU TYR LEU GLU SER PRO ALA GLY VAL
SEQRES 9 A 428 GLY PHE SER TYR SER ASP ASP LYS PHE TYR ALA THR ASN
SEQRES 10 A 428 ASP THR GLU VAL ALA GLN SER ASN PHE GLU ALA LEU GLN
SEQRES 11 A 428 ASP PHE PHE ARG LEU PHE PRO GLU TYR LYS ASN ASN LYS
SEQRES 12 A 428 LEU PHE LEU THR GLY GLU SER TYR ALA GLY ILE TYR ILE
SEQRES 13 A 428 PRO THR LEU ALA VAL LEU VAL MET GLN ASP PRO SER MET
SEQRES 14 A 428 ASN LEU GLN GLY LEU ALA VAL GLY ASN GLY LEU SER SER
SEQRES 15 A 428 TYR GLU GLN ASN ASP ASN SER LEU VAL TYR PHE ALA TYR
SEQRES 16 A 428 TYR HIS GLY LEU LEU GLY ASN ARG LEU TRP SER SER LEU
SEQRES 17 A 428 GLN THR HIS CYS CYS SER GLN ASN LYS CYS ASN PHE TYR
SEQRES 18 A 428 ASP ASN LYS ASP LEU GLU CYS VAL THR ASN LEU GLN GLU
SEQRES 19 A 428 VAL ALA ARG ILE VAL GLY ASN SER GLY LEU ASN ILE TYR
SEQRES 20 A 428 ASN LEU TYR ALA PRO CYS ALA GLY GLY VAL PRO SER HIS
SEQRES 21 A 428 PHE ARG SER GLY ASP LYS VAL ARG MET ASP PRO PRO CYS
SEQRES 22 A 428 THR ASN THR THR ALA ALA SER THR TYR LEU ASN ASN PRO
SEQRES 23 A 428 TYR VAL ARG LYS ALA LEU ASN ILE PRO GLU GLN LEU PRO
SEQRES 24 A 428 GLN TRP ASP MET CYS ASN PHE LEU VAL ASN LEU GLN TYR
SEQRES 25 A 428 ARG ARG LEU TYR ARG SER MET ASN SER GLN TYR LEU LYS
SEQRES 26 A 428 LEU LEU SER SER GLN LYS TYR GLN ILE LEU LEU TYR ASN
SEQRES 27 A 428 GLY ASP VAL ASP MET ALA CYS ASN PHE MET GLY ASP GLU
SEQRES 28 A 428 TRP PHE VAL ASP SER LEU ASN GLN LYS MET GLU VAL GLN
SEQRES 29 A 428 ARG ARG PRO TRP LEU VAL LYS TYR GLY ASP SER GLY GLU
SEQRES 30 A 428 GLN ILE ALA GLY PHE VAL LYS GLU PHE SER HIS ILE ALA
SEQRES 31 A 428 PHE LEU THR ILE LYS GLY ALA GLY HIS MET VAL PRO THR
SEQRES 32 A 428 ASP LYS PRO LEU ALA ALA PHE THR MET PHE SER ARG PHE
SEQRES 33 A 428 LEU ASN LYS GLN PRO TYR HIS HIS HIS HIS HIS HIS
SEQRES 1 B 428 ALA PRO ASP GLN ASP GLU ILE GLN ARG LEU PRO GLY LEU
SEQRES 2 B 428 ALA LYS GLN PRO SER PHE ARG GLN TYR SER GLY TYR LEU
SEQRES 3 B 428 LYS GLY SER GLY SER LYS HIS LEU HIS TYR TRP PHE VAL
SEQRES 4 B 428 GLU SER GLN LYS ASP PRO GLU ASN SER PRO VAL VAL LEU
SEQRES 5 B 428 TRP LEU ASN GLY GLY PRO GLY CYS SER SER LEU ASP GLY
SEQRES 6 B 428 LEU LEU THR GLU HIS GLY PRO PHE LEU VAL GLN PRO ASP
SEQRES 7 B 428 GLY VAL THR LEU GLU TYR ASN PRO TYR SER TRP ASN LEU
SEQRES 8 B 428 ILE ALA ASN VAL LEU TYR LEU GLU SER PRO ALA GLY VAL
SEQRES 9 B 428 GLY PHE SER TYR SER ASP ASP LYS PHE TYR ALA THR ASN
SEQRES 10 B 428 ASP THR GLU VAL ALA GLN SER ASN PHE GLU ALA LEU GLN
SEQRES 11 B 428 ASP PHE PHE ARG LEU PHE PRO GLU TYR LYS ASN ASN LYS
SEQRES 12 B 428 LEU PHE LEU THR GLY GLU SER TYR ALA GLY ILE TYR ILE
SEQRES 13 B 428 PRO THR LEU ALA VAL LEU VAL MET GLN ASP PRO SER MET
SEQRES 14 B 428 ASN LEU GLN GLY LEU ALA VAL GLY ASN GLY LEU SER SER
SEQRES 15 B 428 TYR GLU GLN ASN ASP ASN SER LEU VAL TYR PHE ALA TYR
SEQRES 16 B 428 TYR HIS GLY LEU LEU GLY ASN ARG LEU TRP SER SER LEU
SEQRES 17 B 428 GLN THR HIS CYS CYS SER GLN ASN LYS CYS ASN PHE TYR
SEQRES 18 B 428 ASP ASN LYS ASP LEU GLU CYS VAL THR ASN LEU GLN GLU
SEQRES 19 B 428 VAL ALA ARG ILE VAL GLY ASN SER GLY LEU ASN ILE TYR
SEQRES 20 B 428 ASN LEU TYR ALA PRO CYS ALA GLY GLY VAL PRO SER HIS
SEQRES 21 B 428 PHE ARG SER GLY ASP LYS VAL ARG MET ASP PRO PRO CYS
SEQRES 22 B 428 THR ASN THR THR ALA ALA SER THR TYR LEU ASN ASN PRO
SEQRES 23 B 428 TYR VAL ARG LYS ALA LEU ASN ILE PRO GLU GLN LEU PRO
SEQRES 24 B 428 GLN TRP ASP MET CYS ASN PHE LEU VAL ASN LEU GLN TYR
SEQRES 25 B 428 ARG ARG LEU TYR ARG SER MET ASN SER GLN TYR LEU LYS
SEQRES 26 B 428 LEU LEU SER SER GLN LYS TYR GLN ILE LEU LEU TYR ASN
SEQRES 27 B 428 GLY ASP VAL ASP MET ALA CYS ASN PHE MET GLY ASP GLU
SEQRES 28 B 428 TRP PHE VAL ASP SER LEU ASN GLN LYS MET GLU VAL GLN
SEQRES 29 B 428 ARG ARG PRO TRP LEU VAL LYS TYR GLY ASP SER GLY GLU
SEQRES 30 B 428 GLN ILE ALA GLY PHE VAL LYS GLU PHE SER HIS ILE ALA
SEQRES 31 B 428 PHE LEU THR ILE LYS GLY ALA GLY HIS MET VAL PRO THR
SEQRES 32 B 428 ASP LYS PRO LEU ALA ALA PHE THR MET PHE SER ARG PHE
SEQRES 33 B 428 LEU ASN LYS GLN PRO TYR HIS HIS HIS HIS HIS HIS
MODRES 4MWS ASN B 305 ASN GLYCOSYLATION SITE
MODRES 4MWS ASN A 117 ASN GLYCOSYLATION SITE
MODRES 4MWS ASN B 117 ASN GLYCOSYLATION SITE
MODRES 4MWS ASN A 305 ASN GLYCOSYLATION SITE
HET NAG A 501 14
HET NAG A 502 14
HET BMA A 503 11
HET MAN A 504 11
HET FUC A 505 10
HET NAG A 506 14
HET GOL A 507 6
HET NAG B 501 14
HET NAG B 502 14
HET BMA B 503 11
HET FUC B 504 10
HET NAG B 505 14
HET GOL B 506 6
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM BMA BETA-D-MANNOSE
HETNAM MAN ALPHA-D-MANNOSE
HETNAM FUC ALPHA-L-FUCOSE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 NAG 6(C8 H15 N O6)
FORMUL 3 BMA 2(C6 H12 O6)
FORMUL 3 MAN C6 H12 O6
FORMUL 3 FUC 2(C6 H12 O5)
FORMUL 5 GOL 2(C3 H8 O3)
FORMUL 9 HOH *4(H2 O)
HELIX 1 1 PRO A 2 GLU A 6 5 5
HELIX 2 2 ASP A 44 SER A 48 5 5
HELIX 3 3 SER A 62 GLU A 69 1 8
HELIX 4 4 SER A 88 ILE A 92 5 5
HELIX 5 5 ASN A 117 PHE A 136 1 20
HELIX 6 6 PRO A 137 LYS A 140 5 4
HELIX 7 7 TYR A 151 GLN A 165 1 15
HELIX 8 8 SER A 182 HIS A 197 1 16
HELIX 9 9 LEU A 200 CYS A 213 1 14
HELIX 10 10 ASP A 225 ASN A 241 1 17
HELIX 11 11 THR A 306 ASN A 315 1 10
HELIX 12 12 ASN A 315 LEU A 322 1 8
HELIX 13 13 ASN A 335 GLN A 341 1 7
HELIX 14 14 MET A 349 GLN A 360 1 12
HELIX 15 15 ASN A 376 SER A 386 1 11
HELIX 16 16 MET A 430 LYS A 435 1 6
HELIX 17 17 LYS A 435 ASN A 448 1 14
HELIX 18 18 PRO B 2 GLU B 6 5 5
HELIX 19 19 ASP B 44 SER B 48 5 5
HELIX 20 20 SER B 62 GLU B 69 1 8
HELIX 21 21 SER B 88 ILE B 92 5 5
HELIX 22 22 ASN B 117 PHE B 136 1 20
HELIX 23 23 PRO B 137 LYS B 140 5 4
HELIX 24 24 TYR B 151 GLN B 165 1 15
HELIX 25 25 SER B 182 HIS B 197 1 16
HELIX 26 26 GLY B 201 CYS B 212 1 12
HELIX 27 27 ASP B 225 ASN B 241 1 17
HELIX 28 28 THR B 306 ASN B 315 1 10
HELIX 29 29 ASN B 315 LEU B 322 1 8
HELIX 30 30 ASN B 335 GLN B 341 1 7
HELIX 31 31 MET B 349 GLN B 360 1 12
HELIX 32 32 ASN B 376 SER B 386 1 11
HELIX 33 33 MET B 430 LYS B 435 1 6
HELIX 34 34 LYS B 435 ASN B 448 1 14
SHEET 1 A 3 GLN A 21 LYS A 27 0
SHEET 2 A 3 LYS A 32 VAL A 39 -1 O TYR A 36 N GLY A 24
SHEET 3 A 3 TYR A 108 SER A 109 -1 O TYR A 108 N HIS A 33
SHEET 1 B10 GLN A 21 LYS A 27 0
SHEET 2 B10 LYS A 32 VAL A 39 -1 O TYR A 36 N GLY A 24
SHEET 3 B10 ASN A 94 LEU A 98 -1 O TYR A 97 N TRP A 37
SHEET 4 B10 VAL A 50 LEU A 54 1 N VAL A 51 O LEU A 96
SHEET 5 B10 LEU A 144 GLU A 149 1 O PHE A 145 N VAL A 50
SHEET 6 B10 LEU A 171 GLY A 177 1 O GLN A 172 N LEU A 144
SHEET 7 B10 GLN A 363 GLY A 369 1 O LEU A 365 N VAL A 176
SHEET 8 B10 ILE A 419 ILE A 424 1 O ILE A 424 N ASN A 368
SHEET 9 B10 GLY A 406 PHE A 416 -1 N PHE A 412 O THR A 423
SHEET 10 B10 ARG A 396 TYR A 402 -1 N ARG A 396 O VAL A 413
SHEET 1 C 2 PHE A 73 VAL A 75 0
SHEET 2 C 2 LEU A 82 TYR A 84 -1 O GLU A 83 N LEU A 74
SHEET 1 D 3 GLN B 21 LYS B 27 0
SHEET 2 D 3 LYS B 32 VAL B 39 -1 O TYR B 36 N GLY B 24
SHEET 3 D 3 TYR B 108 SER B 109 -1 O TYR B 108 N HIS B 33
SHEET 1 E10 GLN B 21 LYS B 27 0
SHEET 2 E10 LYS B 32 VAL B 39 -1 O TYR B 36 N GLY B 24
SHEET 3 E10 ASN B 94 LEU B 98 -1 O TYR B 97 N TRP B 37
SHEET 4 E10 VAL B 50 LEU B 54 1 N VAL B 51 O LEU B 96
SHEET 5 E10 LEU B 144 GLU B 149 1 O PHE B 145 N VAL B 50
SHEET 6 E10 LEU B 171 GLY B 177 1 O GLN B 172 N LEU B 144
SHEET 7 E10 GLN B 363 GLY B 369 1 O LEU B 365 N VAL B 176
SHEET 8 E10 ILE B 419 ILE B 424 1 O ILE B 424 N ASN B 368
SHEET 9 E10 GLY B 406 PHE B 416 -1 N LYS B 414 O PHE B 421
SHEET 10 E10 ARG B 396 TYR B 402 -1 N ARG B 396 O VAL B 413
SHEET 1 F 2 PHE B 73 VAL B 75 0
SHEET 2 F 2 LEU B 82 TYR B 84 -1 O GLU B 83 N LEU B 74
SHEET 1 G 2 CYS B 213 SER B 214 0
SHEET 2 G 2 LYS B 217 CYS B 218 -1 O LYS B 217 N SER B 214
SSBOND 1 CYS A 60 CYS A 334 1555 1555 2.06
SSBOND 2 CYS A 212 CYS A 228 1555 1555 2.02
SSBOND 3 CYS A 213 CYS A 218 1555 1555 2.05
SSBOND 4 CYS A 253 CYS A 303 1555 1555 2.06
SSBOND 5 CYS B 60 CYS B 334 1555 1555 2.05
SSBOND 6 CYS B 212 CYS B 228 1555 1555 2.05
SSBOND 7 CYS B 213 CYS B 218 1555 1555 2.05
SSBOND 8 CYS B 253 CYS B 303 1555 1555 2.05
LINK O4 NAG A 501 C1 NAG A 502 1555 1555 1.43
LINK O3 BMA A 503 C1 MAN A 504 1555 1555 1.44
LINK ND2 ASN B 305 C1 NAG B 505 1555 1555 1.44
LINK O4 NAG B 501 C1 NAG B 502 1555 1555 1.44
LINK O4 NAG A 502 C1 BMA A 503 1555 1555 1.44
LINK ND2 ASN A 117 C1 NAG A 501 1555 1555 1.44
LINK O3 NAG A 501 C1 FUC A 505 1555 1555 1.44
LINK ND2 ASN B 117 C1 NAG B 501 1555 1555 1.44
LINK O3 NAG B 501 C1 FUC B 504 1555 1555 1.45
LINK O4 NAG B 502 C1 BMA B 503 1555 1555 1.46
LINK ND2 ASN A 305 C1 NAG A 506 1555 1555 1.47
CISPEP 1 GLY A 57 PRO A 58 0 -8.07
CISPEP 2 SER A 100 PRO A 101 0 -0.41
CISPEP 3 GLY B 57 PRO B 58 0 -7.97
CISPEP 4 SER B 100 PRO B 101 0 -2.78
SITE 1 AC1 6 ASN A 117 GLU A 120 ARG A 343 LEU A 345
SITE 2 AC1 6 NAG A 502 FUC A 505
SITE 1 AC2 3 NAG A 501 BMA A 503 FUC A 505
SITE 1 AC3 3 GLN A 165 NAG A 502 MAN A 504
SITE 1 AC4 2 GLN A 165 BMA A 503
SITE 1 AC5 2 NAG A 501 NAG A 502
SITE 1 AC6 4 PRO A 77 GLY A 255 ASN A 305 THR A 307
SITE 1 AC7 1 ARG A 344
SITE 1 AC8 6 ASN B 117 GLU B 120 ARG B 343 LEU B 345
SITE 2 AC8 6 NAG B 502 FUC B 504
SITE 1 AC9 3 NAG B 501 BMA B 503 FUC B 504
SITE 1 BC1 1 NAG B 502
SITE 1 BC2 2 NAG B 501 NAG B 502
SITE 1 BC3 3 PRO B 77 ASN B 305 THR B 307
SITE 1 BC4 3 GLY B 57 ASN B 339 ARG B 344
CRYST1 134.889 134.889 99.805 90.00 90.00 120.00 P 31 2 1 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 0.007414 0.004280 0.000000 0.00000
SCALE2 0.000000 0.008560 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010020 0.00000
TER 3299 TYR A 452
TER 6598 TYR B 452
MASTER 444 0 13 34 32 0 15 6 6749 2 169 66
END |