HEADER REPLICATION 17-JUN-15 5C3I
TITLE CRYSTAL STRUCTURE OF THE QUATERNARY COMPLEX OF HISTONE H3-H4
TITLE 2 HETERODIMER WITH CHAPERONE ASF1 AND THE REPLICATIVE HELICASE SUBUNIT
TITLE 3 MCM2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE CHAPERONE ASF1A;
COMPND 3 CHAIN: A, E, I, M, Q, U;
COMPND 4 FRAGMENT: UNP RESIDUES 1-175;
COMPND 5 SYNONYM: ANTI-SILENCING FUNCTION PROTEIN 1 HOMOLOG A,HASF1A,CCG1-
COMPND 6 INTERACTING FACTOR A,HCIA;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: HISTONE H3.1;
COMPND 10 CHAIN: B, F, J, N, R, V;
COMPND 11 SYNONYM: HISTONE H3/A,HISTONE H3/B,HISTONE H3/C,HISTONE H3/D,HISTONE
COMPND 12 H3/F,HISTONE H3/H,HISTONE H3/I,HISTONE H3/J,HISTONE H3/K,HISTONE
COMPND 13 H3/L;
COMPND 14 ENGINEERED: YES;
COMPND 15 MOL_ID: 3;
COMPND 16 MOLECULE: HISTONE H4;
COMPND 17 CHAIN: C, G, K, O, S, W;
COMPND 18 ENGINEERED: YES;
COMPND 19 MOL_ID: 4;
COMPND 20 MOLECULE: DNA REPLICATION LICENSING FACTOR MCM2,MCM2;
COMPND 21 CHAIN: D, H, L, P, T, X;
COMPND 22 FRAGMENT: UNP RESIDUES 63-154;
COMPND 23 SYNONYM: MINICHROMOSOME MAINTENANCE PROTEIN 2 HOMOLOG,NUCLEAR PROTEIN
COMPND 24 BM28;
COMPND 25 EC: 3.6.4.12;
COMPND 26 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: ASF1A, CGI-98, HSPC146;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PRSFDUET;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: HIST1H3A, H3FA, HIST1H3B, H3FL, HIST1H3C, H3FC, HIST1H3D,
SOURCE 16 H3FB, HIST1H3E, H3FD, HIST1H3F, H3FI, HIST1H3G, H3FH, HIST1H3H,
SOURCE 17 H3FK, HIST1H3I, H3FF, HIST1H3J, H3FJ;
SOURCE 18 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 19 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 20 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 21 EXPRESSION_SYSTEM_PLASMID: PCDFDUET;
SOURCE 22 MOL_ID: 3;
SOURCE 23 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 24 ORGANISM_COMMON: HUMAN;
SOURCE 25 ORGANISM_TAXID: 9606;
SOURCE 26 GENE: HIST1H4A, H4/A, H4FA, HIST1H4B, H4/I, H4FI, HIST1H4C, H4/G,
SOURCE 27 H4FG, HIST1H4D, H4/B, H4FB, HIST1H4E, H4/J, H4FJ, HIST1H4F, H4/C,
SOURCE 28 H4FC, HIST1H4H, H4/H, H4FH, HIST1H4I, H4/M, H4FM, HIST1H4J, H4/E,
SOURCE 29 H4FE, HIST1H4K, H4/D, H4FD, HIST1H4L, H4/K, H4FK, HIST2H4A, H4/N,
SOURCE 30 H4F2, H4FN, HIST2H4, HIST2H4B, H4/O, H4FO, HIST4H4;
SOURCE 31 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 32 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 33 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 34 EXPRESSION_SYSTEM_PLASMID: PCDFDUET;
SOURCE 35 MOL_ID: 4;
SOURCE 36 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 37 ORGANISM_COMMON: HUMAN;
SOURCE 38 ORGANISM_TAXID: 9606;
SOURCE 39 GENE: MCM2, BM28, CCNL1, CDCL1, KIAA0030;
SOURCE 40 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 41 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 42 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 43 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 44 EXPRESSION_SYSTEM_PLASMID: PET-28A-SMT3
KEYWDS REPLICATION, HISTONE, CHAPERONE, ASF1, MCM PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR H.WANG,M.WANG,N.YANG,R.M.XU
REVDAT 4 08-NOV-23 5C3I 1 REMARK
REVDAT 3 18-OCT-17 5C3I 1 REMARK
REVDAT 2 02-SEP-15 5C3I 1 JRNL
REVDAT 1 29-JUL-15 5C3I 0
JRNL AUTH H.WANG,M.WANG,N.YANG,R.M.XU
JRNL TITL STRUCTURE OF THE QUATERNARY COMPLEX OF HISTONE H3-H4
JRNL TITL 2 HETERODIMER WITH CHAPERONE ASF1 AND THE REPLICATIVE HELICASE
JRNL TITL 3 SUBUNIT MCM2
JRNL REF PROTEIN CELL V. 6 693 2015
JRNL REFN ESSN 1674-8018
JRNL PMID 26186914
JRNL DOI 10.1007/S13238-015-0190-0
REMARK 2
REMARK 2 RESOLUTION. 3.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 3.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.99
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.8
REMARK 3 NUMBER OF REFLECTIONS : 37994
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) : 0.218
REMARK 3 R VALUE (WORKING SET) : 0.216
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1987
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) : 3.48
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.57
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1873
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 62.95
REMARK 3 BIN R VALUE (WORKING SET) : 0.2540
REMARK 3 BIN FREE R VALUE SET COUNT : 96
REMARK 3 BIN FREE R VALUE : 0.3200
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 17655
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.32
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -7.15000
REMARK 3 B22 (A**2) : -7.15000
REMARK 3 B33 (A**2) : 14.30000
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): 0.132
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.380
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 24.455
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.857
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.811
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 17949 ; 0.005 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 24267 ; 0.915 ; 1.968
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2173 ; 4.851 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 940 ;29.313 ;23.468
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3152 ;16.220 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 201 ;18.550 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2706 ; 0.060 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 13769 ; 0.004 ; 0.021
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 ; 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 NUMBER OF DIFFERENT NCS GROUPS : NULL
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 : 0.787
REMARK 3 TWIN DOMAIN : 2
REMARK 3 TWIN OPERATOR : -H,-K,L
REMARK 3 TWIN FRACTION : 0.213
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 USED IF PRESENT IN
REMARK 3 THE INPUT U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 5C3I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-JUL-15.
REMARK 100 THE DEPOSITION ID IS D_1000210966.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-APR-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
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 : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42834
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 9.100
REMARK 200 R MERGE (I) : 0.16100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 9.20
REMARK 200 R MERGE FOR SHELL (I) : 0.69000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER, PHASER
REMARK 200 STARTING MODEL: 2IO5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.25
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 2% TACSIMATE,0.1 M TRIS
REMARK 280 -HCL PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K
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 87.26533
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 174.53067
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 174.53067
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 87.26533
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J, K, L
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -56.0 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
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19240 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 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
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17180 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -63.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, N, O, P
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 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: Q, R, S, T
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: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -58.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: U, V, W, X
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 MET A -12
REMARK 465 GLY A -11
REMARK 465 SER A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 SER A -3
REMARK 465 ASN A -2
REMARK 465 ASP A -1
REMARK 465 PRO A 0
REMARK 465 MET A 1
REMARK 465 GLU A 154
REMARK 465 ASP A 155
REMARK 465 ASN A 156
REMARK 465 THR A 157
REMARK 465 GLU A 158
REMARK 465 LYS A 159
REMARK 465 LEU A 160
REMARK 465 GLU A 161
REMARK 465 ASP A 162
REMARK 465 ALA A 163
REMARK 465 GLU A 164
REMARK 465 SER A 165
REMARK 465 SER A 166
REMARK 465 ASN A 167
REMARK 465 PRO A 168
REMARK 465 ASN A 169
REMARK 465 LEU A 170
REMARK 465 GLN A 171
REMARK 465 SER A 172
REMARK 465 LEU A 173
REMARK 465 LEU A 174
REMARK 465 SER A 175
REMARK 465 MET B 0
REMARK 465 ALA B 1
REMARK 465 ARG B 2
REMARK 465 THR B 3
REMARK 465 LYS B 4
REMARK 465 GLN B 5
REMARK 465 THR B 6
REMARK 465 ALA B 7
REMARK 465 ARG B 8
REMARK 465 LYS B 9
REMARK 465 SER B 10
REMARK 465 THR B 11
REMARK 465 GLY B 12
REMARK 465 GLY B 13
REMARK 465 LYS B 14
REMARK 465 ALA B 15
REMARK 465 PRO B 16
REMARK 465 ARG B 17
REMARK 465 LYS B 18
REMARK 465 GLN B 19
REMARK 465 LEU B 20
REMARK 465 ALA B 21
REMARK 465 THR B 22
REMARK 465 LYS B 23
REMARK 465 ALA B 24
REMARK 465 ALA B 25
REMARK 465 ARG B 26
REMARK 465 LYS B 27
REMARK 465 SER B 28
REMARK 465 ALA B 29
REMARK 465 PRO B 30
REMARK 465 ALA B 31
REMARK 465 THR B 32
REMARK 465 GLY B 33
REMARK 465 GLY B 34
REMARK 465 VAL B 35
REMARK 465 LYS B 36
REMARK 465 LYS B 37
REMARK 465 PRO B 38
REMARK 465 HIS B 39
REMARK 465 ARG B 40
REMARK 465 TYR B 41
REMARK 465 ARG B 42
REMARK 465 PRO B 43
REMARK 465 GLY B 44
REMARK 465 THR B 45
REMARK 465 VAL B 46
REMARK 465 ALA B 47
REMARK 465 ALA B 135
REMARK 465 MET C 0
REMARK 465 SER C 1
REMARK 465 GLY C 2
REMARK 465 ARG C 3
REMARK 465 GLY C 4
REMARK 465 LYS C 5
REMARK 465 GLY C 6
REMARK 465 GLY C 7
REMARK 465 LYS C 8
REMARK 465 GLY C 9
REMARK 465 LEU C 10
REMARK 465 GLY C 11
REMARK 465 LYS C 12
REMARK 465 GLY C 13
REMARK 465 GLY C 14
REMARK 465 ALA C 15
REMARK 465 LYS C 16
REMARK 465 ARG C 17
REMARK 465 HIS C 18
REMARK 465 ARG C 19
REMARK 465 LYS C 20
REMARK 465 VAL C 21
REMARK 465 LEU C 22
REMARK 465 ARG C 23
REMARK 465 GLY C 102
REMARK 465 SER D 62
REMARK 465 LEU D 63
REMARK 465 GLU D 64
REMARK 465 GLU D 65
REMARK 465 GLU D 66
REMARK 465 GLU D 67
REMARK 465 ALA D 126
REMARK 465 UNK D 127
REMARK 465 UNK D 128
REMARK 465 UNK D 129
REMARK 465 UNK D 130
REMARK 465 UNK D 131
REMARK 465 UNK D 132
REMARK 465 UNK D 133
REMARK 465 UNK D 141
REMARK 465 UNK D 142
REMARK 465 UNK D 143
REMARK 465 UNK D 144
REMARK 465 UNK D 145
REMARK 465 UNK D 146
REMARK 465 UNK D 147
REMARK 465 UNK D 148
REMARK 465 UNK D 149
REMARK 465 UNK D 150
REMARK 465 UNK D 151
REMARK 465 UNK D 152
REMARK 465 UNK D 153
REMARK 465 UNK D 154
REMARK 465 UNK D 155
REMARK 465 UNK D 156
REMARK 465 MET E -12
REMARK 465 GLY E -11
REMARK 465 SER E -10
REMARK 465 HIS E -9
REMARK 465 HIS E -8
REMARK 465 HIS E -7
REMARK 465 HIS E -6
REMARK 465 HIS E -5
REMARK 465 HIS E -4
REMARK 465 SER E -3
REMARK 465 ASN E -2
REMARK 465 ASP E -1
REMARK 465 PRO E 0
REMARK 465 MET E 1
REMARK 465 ASP E 155
REMARK 465 ASN E 156
REMARK 465 THR E 157
REMARK 465 GLU E 158
REMARK 465 LYS E 159
REMARK 465 LEU E 160
REMARK 465 GLU E 161
REMARK 465 ASP E 162
REMARK 465 ALA E 163
REMARK 465 GLU E 164
REMARK 465 SER E 165
REMARK 465 SER E 166
REMARK 465 ASN E 167
REMARK 465 PRO E 168
REMARK 465 ASN E 169
REMARK 465 LEU E 170
REMARK 465 GLN E 171
REMARK 465 SER E 172
REMARK 465 LEU E 173
REMARK 465 LEU E 174
REMARK 465 SER E 175
REMARK 465 MET F 0
REMARK 465 ALA F 1
REMARK 465 ARG F 2
REMARK 465 THR F 3
REMARK 465 LYS F 4
REMARK 465 GLN F 5
REMARK 465 THR F 6
REMARK 465 ALA F 7
REMARK 465 ARG F 8
REMARK 465 LYS F 9
REMARK 465 SER F 10
REMARK 465 THR F 11
REMARK 465 GLY F 12
REMARK 465 GLY F 13
REMARK 465 LYS F 14
REMARK 465 ALA F 15
REMARK 465 PRO F 16
REMARK 465 ARG F 17
REMARK 465 LYS F 18
REMARK 465 GLN F 19
REMARK 465 LEU F 20
REMARK 465 ALA F 21
REMARK 465 THR F 22
REMARK 465 LYS F 23
REMARK 465 ALA F 24
REMARK 465 ALA F 25
REMARK 465 ARG F 26
REMARK 465 LYS F 27
REMARK 465 SER F 28
REMARK 465 ALA F 29
REMARK 465 PRO F 30
REMARK 465 ALA F 31
REMARK 465 THR F 32
REMARK 465 GLY F 33
REMARK 465 GLY F 34
REMARK 465 VAL F 35
REMARK 465 LYS F 36
REMARK 465 LYS F 37
REMARK 465 PRO F 38
REMARK 465 HIS F 39
REMARK 465 ARG F 40
REMARK 465 TYR F 41
REMARK 465 ARG F 42
REMARK 465 PRO F 43
REMARK 465 GLY F 44
REMARK 465 THR F 45
REMARK 465 VAL F 46
REMARK 465 ALA F 135
REMARK 465 MET G 0
REMARK 465 SER G 1
REMARK 465 GLY G 2
REMARK 465 ARG G 3
REMARK 465 GLY G 4
REMARK 465 LYS G 5
REMARK 465 GLY G 6
REMARK 465 GLY G 7
REMARK 465 LYS G 8
REMARK 465 GLY G 9
REMARK 465 LEU G 10
REMARK 465 GLY G 11
REMARK 465 LYS G 12
REMARK 465 GLY G 13
REMARK 465 GLY G 14
REMARK 465 ALA G 15
REMARK 465 LYS G 16
REMARK 465 ARG G 17
REMARK 465 HIS G 18
REMARK 465 ARG G 19
REMARK 465 LYS G 20
REMARK 465 VAL G 21
REMARK 465 LEU G 22
REMARK 465 ARG G 23
REMARK 465 GLY G 101
REMARK 465 GLY G 102
REMARK 465 SER H 62
REMARK 465 LEU H 63
REMARK 465 GLU H 64
REMARK 465 GLU H 65
REMARK 465 GLU H 66
REMARK 465 GLU H 67
REMARK 465 ALA H 124
REMARK 465 UNK H 125
REMARK 465 UNK H 126
REMARK 465 UNK H 127
REMARK 465 UNK H 128
REMARK 465 UNK H 129
REMARK 465 UNK H 130
REMARK 465 UNK H 131
REMARK 465 UNK H 132
REMARK 465 UNK H 133
REMARK 465 UNK H 134
REMARK 465 UNK H 135
REMARK 465 UNK H 136
REMARK 465 UNK H 137
REMARK 465 UNK H 138
REMARK 465 UNK H 139
REMARK 465 UNK H 140
REMARK 465 UNK H 141
REMARK 465 UNK H 142
REMARK 465 UNK H 143
REMARK 465 UNK H 144
REMARK 465 UNK H 145
REMARK 465 UNK H 146
REMARK 465 UNK H 147
REMARK 465 UNK H 148
REMARK 465 UNK H 149
REMARK 465 UNK H 150
REMARK 465 UNK H 151
REMARK 465 UNK H 152
REMARK 465 UNK H 153
REMARK 465 UNK H 154
REMARK 465 MET I -12
REMARK 465 GLY I -11
REMARK 465 SER I -10
REMARK 465 HIS I -9
REMARK 465 HIS I -8
REMARK 465 HIS I -7
REMARK 465 HIS I -6
REMARK 465 HIS I -5
REMARK 465 HIS I -4
REMARK 465 SER I -3
REMARK 465 ASN I -2
REMARK 465 ASP I -1
REMARK 465 PRO I 0
REMARK 465 MET I 1
REMARK 465 ASP I 155
REMARK 465 ASN I 156
REMARK 465 THR I 157
REMARK 465 GLU I 158
REMARK 465 LYS I 159
REMARK 465 LEU I 160
REMARK 465 GLU I 161
REMARK 465 ASP I 162
REMARK 465 ALA I 163
REMARK 465 GLU I 164
REMARK 465 SER I 165
REMARK 465 SER I 166
REMARK 465 ASN I 167
REMARK 465 PRO I 168
REMARK 465 ASN I 169
REMARK 465 LEU I 170
REMARK 465 GLN I 171
REMARK 465 SER I 172
REMARK 465 LEU I 173
REMARK 465 LEU I 174
REMARK 465 SER I 175
REMARK 465 MET J 0
REMARK 465 ALA J 1
REMARK 465 ARG J 2
REMARK 465 THR J 3
REMARK 465 LYS J 4
REMARK 465 GLN J 5
REMARK 465 THR J 6
REMARK 465 ALA J 7
REMARK 465 ARG J 8
REMARK 465 LYS J 9
REMARK 465 SER J 10
REMARK 465 THR J 11
REMARK 465 GLY J 12
REMARK 465 GLY J 13
REMARK 465 LYS J 14
REMARK 465 ALA J 15
REMARK 465 PRO J 16
REMARK 465 ARG J 17
REMARK 465 LYS J 18
REMARK 465 GLN J 19
REMARK 465 LEU J 20
REMARK 465 ALA J 21
REMARK 465 THR J 22
REMARK 465 LYS J 23
REMARK 465 ALA J 24
REMARK 465 ALA J 25
REMARK 465 ARG J 26
REMARK 465 LYS J 27
REMARK 465 SER J 28
REMARK 465 ALA J 29
REMARK 465 PRO J 30
REMARK 465 ALA J 31
REMARK 465 THR J 32
REMARK 465 GLY J 33
REMARK 465 GLY J 34
REMARK 465 VAL J 35
REMARK 465 LYS J 36
REMARK 465 LYS J 37
REMARK 465 PRO J 38
REMARK 465 HIS J 39
REMARK 465 ARG J 40
REMARK 465 TYR J 41
REMARK 465 ARG J 42
REMARK 465 PRO J 43
REMARK 465 GLY J 44
REMARK 465 THR J 45
REMARK 465 VAL J 46
REMARK 465 ALA J 47
REMARK 465 LEU J 48
REMARK 465 ARG J 49
REMARK 465 GLU J 50
REMARK 465 ALA J 135
REMARK 465 MET K 0
REMARK 465 SER K 1
REMARK 465 GLY K 2
REMARK 465 ARG K 3
REMARK 465 GLY K 4
REMARK 465 LYS K 5
REMARK 465 GLY K 6
REMARK 465 GLY K 7
REMARK 465 LYS K 8
REMARK 465 GLY K 9
REMARK 465 LEU K 10
REMARK 465 GLY K 11
REMARK 465 LYS K 12
REMARK 465 GLY K 13
REMARK 465 GLY K 14
REMARK 465 ALA K 15
REMARK 465 LYS K 16
REMARK 465 ARG K 17
REMARK 465 HIS K 18
REMARK 465 ARG K 19
REMARK 465 LYS K 20
REMARK 465 VAL K 21
REMARK 465 LEU K 22
REMARK 465 ARG K 23
REMARK 465 ASP K 24
REMARK 465 ASN K 25
REMARK 465 GLY K 102
REMARK 465 SER L 62
REMARK 465 LEU L 63
REMARK 465 GLU L 64
REMARK 465 GLU L 65
REMARK 465 GLU L 66
REMARK 465 GLU L 67
REMARK 465 ALA L 124
REMARK 465 UNK L 125
REMARK 465 UNK L 126
REMARK 465 UNK L 127
REMARK 465 UNK L 128
REMARK 465 UNK L 129
REMARK 465 UNK L 130
REMARK 465 UNK L 131
REMARK 465 UNK L 132
REMARK 465 UNK L 133
REMARK 465 UNK L 134
REMARK 465 UNK L 135
REMARK 465 UNK L 136
REMARK 465 UNK L 137
REMARK 465 UNK L 138
REMARK 465 UNK L 139
REMARK 465 UNK L 140
REMARK 465 UNK L 141
REMARK 465 UNK L 142
REMARK 465 UNK L 143
REMARK 465 UNK L 144
REMARK 465 UNK L 145
REMARK 465 UNK L 146
REMARK 465 UNK L 147
REMARK 465 UNK L 148
REMARK 465 UNK L 149
REMARK 465 UNK L 150
REMARK 465 UNK L 151
REMARK 465 UNK L 152
REMARK 465 UNK L 153
REMARK 465 UNK L 154
REMARK 465 MET M -12
REMARK 465 GLY M -11
REMARK 465 SER M -10
REMARK 465 HIS M -9
REMARK 465 HIS M -8
REMARK 465 HIS M -7
REMARK 465 HIS M -6
REMARK 465 HIS M -5
REMARK 465 HIS M -4
REMARK 465 SER M -3
REMARK 465 ASN M -2
REMARK 465 ASP M -1
REMARK 465 PRO M 0
REMARK 465 MET M 1
REMARK 465 GLU M 154
REMARK 465 ASP M 155
REMARK 465 ASN M 156
REMARK 465 THR M 157
REMARK 465 GLU M 158
REMARK 465 LYS M 159
REMARK 465 LEU M 160
REMARK 465 GLU M 161
REMARK 465 ASP M 162
REMARK 465 ALA M 163
REMARK 465 GLU M 164
REMARK 465 SER M 165
REMARK 465 SER M 166
REMARK 465 ASN M 167
REMARK 465 PRO M 168
REMARK 465 ASN M 169
REMARK 465 LEU M 170
REMARK 465 GLN M 171
REMARK 465 SER M 172
REMARK 465 LEU M 173
REMARK 465 LEU M 174
REMARK 465 SER M 175
REMARK 465 MET N 0
REMARK 465 ALA N 1
REMARK 465 ARG N 2
REMARK 465 THR N 3
REMARK 465 LYS N 4
REMARK 465 GLN N 5
REMARK 465 THR N 6
REMARK 465 ALA N 7
REMARK 465 ARG N 8
REMARK 465 LYS N 9
REMARK 465 SER N 10
REMARK 465 THR N 11
REMARK 465 GLY N 12
REMARK 465 GLY N 13
REMARK 465 LYS N 14
REMARK 465 ALA N 15
REMARK 465 PRO N 16
REMARK 465 ARG N 17
REMARK 465 LYS N 18
REMARK 465 GLN N 19
REMARK 465 LEU N 20
REMARK 465 ALA N 21
REMARK 465 THR N 22
REMARK 465 LYS N 23
REMARK 465 ALA N 24
REMARK 465 ALA N 25
REMARK 465 ARG N 26
REMARK 465 LYS N 27
REMARK 465 SER N 28
REMARK 465 ALA N 29
REMARK 465 PRO N 30
REMARK 465 ALA N 31
REMARK 465 THR N 32
REMARK 465 GLY N 33
REMARK 465 GLY N 34
REMARK 465 VAL N 35
REMARK 465 LYS N 36
REMARK 465 LYS N 37
REMARK 465 PRO N 38
REMARK 465 HIS N 39
REMARK 465 ARG N 40
REMARK 465 TYR N 41
REMARK 465 ARG N 42
REMARK 465 PRO N 43
REMARK 465 GLY N 44
REMARK 465 THR N 45
REMARK 465 VAL N 46
REMARK 465 ALA N 47
REMARK 465 LEU N 48
REMARK 465 ARG N 49
REMARK 465 GLU N 50
REMARK 465 ILE N 51
REMARK 465 ARG N 52
REMARK 465 ARG N 53
REMARK 465 TYR N 54
REMARK 465 GLN N 55
REMARK 465 LYS N 56
REMARK 465 SER N 57
REMARK 465 THR N 58
REMARK 465 ALA N 135
REMARK 465 MET O 0
REMARK 465 SER O 1
REMARK 465 GLY O 2
REMARK 465 ARG O 3
REMARK 465 GLY O 4
REMARK 465 LYS O 5
REMARK 465 GLY O 6
REMARK 465 GLY O 7
REMARK 465 LYS O 8
REMARK 465 GLY O 9
REMARK 465 LEU O 10
REMARK 465 GLY O 11
REMARK 465 LYS O 12
REMARK 465 GLY O 13
REMARK 465 GLY O 14
REMARK 465 ALA O 15
REMARK 465 LYS O 16
REMARK 465 ARG O 17
REMARK 465 HIS O 18
REMARK 465 ARG O 19
REMARK 465 LYS O 20
REMARK 465 VAL O 21
REMARK 465 LEU O 22
REMARK 465 ARG O 23
REMARK 465 GLY O 102
REMARK 465 SER P 62
REMARK 465 LEU P 63
REMARK 465 GLU P 64
REMARK 465 GLU P 65
REMARK 465 GLU P 66
REMARK 465 GLU P 67
REMARK 465 ASP P 68
REMARK 465 MET P 117
REMARK 465 ARG P 118
REMARK 465 GLN P 119
REMARK 465 ARG P 120
REMARK 465 ASP P 121
REMARK 465 ARG P 122
REMARK 465 GLU P 123
REMARK 465 ALA P 124
REMARK 465 UNK P 125
REMARK 465 UNK P 126
REMARK 465 UNK P 127
REMARK 465 UNK P 128
REMARK 465 UNK P 129
REMARK 465 UNK P 130
REMARK 465 UNK P 131
REMARK 465 UNK P 132
REMARK 465 UNK P 133
REMARK 465 UNK P 134
REMARK 465 UNK P 135
REMARK 465 UNK P 136
REMARK 465 UNK P 137
REMARK 465 UNK P 138
REMARK 465 UNK P 139
REMARK 465 UNK P 140
REMARK 465 UNK P 141
REMARK 465 UNK P 142
REMARK 465 UNK P 143
REMARK 465 UNK P 144
REMARK 465 UNK P 145
REMARK 465 UNK P 146
REMARK 465 UNK P 147
REMARK 465 UNK P 148
REMARK 465 UNK P 149
REMARK 465 UNK P 150
REMARK 465 UNK P 151
REMARK 465 UNK P 152
REMARK 465 UNK P 153
REMARK 465 UNK P 154
REMARK 465 MET Q -12
REMARK 465 GLY Q -11
REMARK 465 SER Q -10
REMARK 465 HIS Q -9
REMARK 465 HIS Q -8
REMARK 465 HIS Q -7
REMARK 465 HIS Q -6
REMARK 465 HIS Q -5
REMARK 465 HIS Q -4
REMARK 465 SER Q -3
REMARK 465 ASN Q -2
REMARK 465 ASP Q -1
REMARK 465 PRO Q 0
REMARK 465 MET Q 1
REMARK 465 ASN Q 156
REMARK 465 THR Q 157
REMARK 465 GLU Q 158
REMARK 465 LYS Q 159
REMARK 465 LEU Q 160
REMARK 465 GLU Q 161
REMARK 465 ASP Q 162
REMARK 465 ALA Q 163
REMARK 465 GLU Q 164
REMARK 465 SER Q 165
REMARK 465 SER Q 166
REMARK 465 ASN Q 167
REMARK 465 PRO Q 168
REMARK 465 ASN Q 169
REMARK 465 LEU Q 170
REMARK 465 GLN Q 171
REMARK 465 SER Q 172
REMARK 465 LEU Q 173
REMARK 465 LEU Q 174
REMARK 465 SER Q 175
REMARK 465 MET R 0
REMARK 465 ALA R 1
REMARK 465 ARG R 2
REMARK 465 THR R 3
REMARK 465 LYS R 4
REMARK 465 GLN R 5
REMARK 465 THR R 6
REMARK 465 ALA R 7
REMARK 465 ARG R 8
REMARK 465 LYS R 9
REMARK 465 SER R 10
REMARK 465 THR R 11
REMARK 465 GLY R 12
REMARK 465 GLY R 13
REMARK 465 LYS R 14
REMARK 465 ALA R 15
REMARK 465 PRO R 16
REMARK 465 ARG R 17
REMARK 465 LYS R 18
REMARK 465 GLN R 19
REMARK 465 LEU R 20
REMARK 465 ALA R 21
REMARK 465 THR R 22
REMARK 465 LYS R 23
REMARK 465 ALA R 24
REMARK 465 ALA R 25
REMARK 465 ARG R 26
REMARK 465 LYS R 27
REMARK 465 SER R 28
REMARK 465 ALA R 29
REMARK 465 PRO R 30
REMARK 465 ALA R 31
REMARK 465 THR R 32
REMARK 465 GLY R 33
REMARK 465 GLY R 34
REMARK 465 VAL R 35
REMARK 465 LYS R 36
REMARK 465 LYS R 37
REMARK 465 PRO R 38
REMARK 465 HIS R 39
REMARK 465 ARG R 40
REMARK 465 TYR R 41
REMARK 465 ARG R 42
REMARK 465 PRO R 43
REMARK 465 GLY R 44
REMARK 465 THR R 45
REMARK 465 VAL R 46
REMARK 465 ALA R 47
REMARK 465 LEU R 48
REMARK 465 ARG R 49
REMARK 465 GLU R 50
REMARK 465 ILE R 51
REMARK 465 ARG R 52
REMARK 465 ARG R 53
REMARK 465 TYR R 54
REMARK 465 GLN R 55
REMARK 465 LYS R 56
REMARK 465 SER R 57
REMARK 465 THR R 58
REMARK 465 GLU R 59
REMARK 465 ARG R 134
REMARK 465 ALA R 135
REMARK 465 MET S 0
REMARK 465 SER S 1
REMARK 465 GLY S 2
REMARK 465 ARG S 3
REMARK 465 GLY S 4
REMARK 465 LYS S 5
REMARK 465 GLY S 6
REMARK 465 GLY S 7
REMARK 465 LYS S 8
REMARK 465 GLY S 9
REMARK 465 LEU S 10
REMARK 465 GLY S 11
REMARK 465 LYS S 12
REMARK 465 GLY S 13
REMARK 465 GLY S 14
REMARK 465 ALA S 15
REMARK 465 LYS S 16
REMARK 465 ARG S 17
REMARK 465 HIS S 18
REMARK 465 ARG S 19
REMARK 465 LYS S 20
REMARK 465 VAL S 21
REMARK 465 LEU S 22
REMARK 465 ARG S 23
REMARK 465 GLY S 102
REMARK 465 SER T 62
REMARK 465 LEU T 63
REMARK 465 GLU T 64
REMARK 465 GLU T 65
REMARK 465 GLU T 66
REMARK 465 GLU T 67
REMARK 465 ASP T 68
REMARK 465 UNK T 125
REMARK 465 UNK T 126
REMARK 465 UNK T 127
REMARK 465 UNK T 128
REMARK 465 UNK T 129
REMARK 465 UNK T 130
REMARK 465 UNK T 131
REMARK 465 UNK T 132
REMARK 465 UNK T 133
REMARK 465 UNK T 134
REMARK 465 UNK T 135
REMARK 465 UNK T 136
REMARK 465 UNK T 137
REMARK 465 UNK T 138
REMARK 465 UNK T 139
REMARK 465 UNK T 140
REMARK 465 UNK T 141
REMARK 465 UNK T 142
REMARK 465 UNK T 143
REMARK 465 UNK T 144
REMARK 465 UNK T 145
REMARK 465 UNK T 146
REMARK 465 UNK T 147
REMARK 465 UNK T 148
REMARK 465 UNK T 149
REMARK 465 UNK T 150
REMARK 465 UNK T 151
REMARK 465 UNK T 152
REMARK 465 UNK T 153
REMARK 465 UNK T 154
REMARK 465 MET U -12
REMARK 465 GLY U -11
REMARK 465 SER U -10
REMARK 465 HIS U -9
REMARK 465 HIS U -8
REMARK 465 HIS U -7
REMARK 465 HIS U -6
REMARK 465 HIS U -5
REMARK 465 HIS U -4
REMARK 465 SER U -3
REMARK 465 ASN U -2
REMARK 465 ASP U -1
REMARK 465 PRO U 0
REMARK 465 MET U 1
REMARK 465 ALA U 2
REMARK 465 TRP U 153
REMARK 465 GLU U 154
REMARK 465 ASP U 155
REMARK 465 ASN U 156
REMARK 465 THR U 157
REMARK 465 GLU U 158
REMARK 465 LYS U 159
REMARK 465 LEU U 160
REMARK 465 GLU U 161
REMARK 465 ASP U 162
REMARK 465 ALA U 163
REMARK 465 GLU U 164
REMARK 465 SER U 165
REMARK 465 SER U 166
REMARK 465 ASN U 167
REMARK 465 PRO U 168
REMARK 465 ASN U 169
REMARK 465 LEU U 170
REMARK 465 GLN U 171
REMARK 465 SER U 172
REMARK 465 LEU U 173
REMARK 465 LEU U 174
REMARK 465 SER U 175
REMARK 465 MET V 0
REMARK 465 ALA V 1
REMARK 465 ARG V 2
REMARK 465 THR V 3
REMARK 465 LYS V 4
REMARK 465 GLN V 5
REMARK 465 THR V 6
REMARK 465 ALA V 7
REMARK 465 ARG V 8
REMARK 465 LYS V 9
REMARK 465 SER V 10
REMARK 465 THR V 11
REMARK 465 GLY V 12
REMARK 465 GLY V 13
REMARK 465 LYS V 14
REMARK 465 ALA V 15
REMARK 465 PRO V 16
REMARK 465 ARG V 17
REMARK 465 LYS V 18
REMARK 465 GLN V 19
REMARK 465 LEU V 20
REMARK 465 ALA V 21
REMARK 465 THR V 22
REMARK 465 LYS V 23
REMARK 465 ALA V 24
REMARK 465 ALA V 25
REMARK 465 ARG V 26
REMARK 465 LYS V 27
REMARK 465 SER V 28
REMARK 465 ALA V 29
REMARK 465 PRO V 30
REMARK 465 ALA V 31
REMARK 465 THR V 32
REMARK 465 GLY V 33
REMARK 465 GLY V 34
REMARK 465 VAL V 35
REMARK 465 LYS V 36
REMARK 465 LYS V 37
REMARK 465 PRO V 38
REMARK 465 HIS V 39
REMARK 465 ARG V 40
REMARK 465 TYR V 41
REMARK 465 ARG V 42
REMARK 465 PRO V 43
REMARK 465 GLY V 44
REMARK 465 THR V 45
REMARK 465 VAL V 46
REMARK 465 ALA V 47
REMARK 465 LEU V 48
REMARK 465 ARG V 49
REMARK 465 GLU V 50
REMARK 465 ILE V 51
REMARK 465 ARG V 52
REMARK 465 ARG V 53
REMARK 465 TYR V 54
REMARK 465 GLN V 55
REMARK 465 LYS V 56
REMARK 465 SER V 57
REMARK 465 THR V 58
REMARK 465 ALA V 135
REMARK 465 MET W 0
REMARK 465 SER W 1
REMARK 465 GLY W 2
REMARK 465 ARG W 3
REMARK 465 GLY W 4
REMARK 465 LYS W 5
REMARK 465 GLY W 6
REMARK 465 GLY W 7
REMARK 465 LYS W 8
REMARK 465 GLY W 9
REMARK 465 LEU W 10
REMARK 465 GLY W 11
REMARK 465 LYS W 12
REMARK 465 GLY W 13
REMARK 465 GLY W 14
REMARK 465 ALA W 15
REMARK 465 LYS W 16
REMARK 465 ARG W 17
REMARK 465 HIS W 18
REMARK 465 ARG W 19
REMARK 465 LYS W 20
REMARK 465 VAL W 21
REMARK 465 LEU W 22
REMARK 465 ARG W 23
REMARK 465 GLY W 101
REMARK 465 GLY W 102
REMARK 465 SER X 62
REMARK 465 LEU X 63
REMARK 465 GLU X 64
REMARK 465 GLU X 65
REMARK 465 GLU X 66
REMARK 465 GLU X 67
REMARK 465 ALA X 124
REMARK 465 UNK X 125
REMARK 465 UNK X 126
REMARK 465 UNK X 127
REMARK 465 UNK X 128
REMARK 465 UNK X 129
REMARK 465 UNK X 130
REMARK 465 UNK X 131
REMARK 465 UNK X 132
REMARK 465 UNK X 133
REMARK 465 UNK X 134
REMARK 465 UNK X 135
REMARK 465 UNK X 136
REMARK 465 UNK X 137
REMARK 465 UNK X 138
REMARK 465 UNK X 139
REMARK 465 UNK X 140
REMARK 465 UNK X 141
REMARK 465 UNK X 142
REMARK 465 UNK X 143
REMARK 465 UNK X 144
REMARK 465 UNK X 145
REMARK 465 UNK X 146
REMARK 465 UNK X 147
REMARK 465 UNK X 148
REMARK 465 UNK X 149
REMARK 465 UNK X 150
REMARK 465 UNK X 151
REMARK 465 UNK X 152
REMARK 465 UNK X 153
REMARK 465 UNK X 154
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 J 55 CG CD OE1 NE2
REMARK 470 GLU N 59 CG CD OE1 OE2
REMARK 470 ARG P 115 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OD2 ASP Q 13 ND2 ASN Q 20 2.18
REMARK 500 O TYR U 117 NH1 ARG U 123 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PRO A 17 150.49 -49.08
REMARK 500 ASN A 125 79.27 -113.92
REMARK 500 LEU B 61 -73.32 -123.57
REMARK 500 ASP D 98 -158.98 -153.23
REMARK 500 LEU F 61 -71.02 -116.57
REMARK 500 LEU J 61 -82.61 -100.98
REMARK 500 ALA J 114 4.29 -69.49
REMARK 500 ASP L 121 -33.77 -34.91
REMARK 500 ASN M 8 148.74 -179.66
REMARK 500 LEU M 12 -66.22 -101.01
REMARK 500 ASP M 33 140.67 -39.73
REMARK 500 GLU M 36 -169.03 -112.74
REMARK 500 LEU N 61 -85.04 -117.22
REMARK 500 ASP N 81 63.72 64.90
REMARK 500 GLN O 27 -18.64 -47.23
REMARK 500 LEU Q 12 -66.42 -91.67
REMARK 500 LEU R 61 -86.37 -121.86
REMARK 500 ASP R 81 68.16 35.84
REMARK 500 TYR S 98 33.58 -99.59
REMARK 500 GLU U 36 -168.59 -108.62
REMARK 500 ASN U 143 68.15 -118.57
REMARK 500 LEU V 61 -68.66 -102.16
REMARK 500 ASP X 99 50.91 -103.10
REMARK 500 ASP X 101 79.33 -69.68
REMARK 500 ASP X 121 -70.25 -64.54
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 SEQUENCE FOR THE UNK RESIDUES OF ENTITY 4 (MCM2) SHOULD BE
REMARK 999 GRGLGRMRRGLLYDSDEEDEERPARKRRQV. ONLY FEW DENSITY OF THE REGION IS
REMARK 999 OBSERVED, WHICH HAS BEEN ASSINGNED UNK D134-140, AND IS SUPPOSED TO
REMARK 999 BE C-TERMINUS FROM CHAIN D.
DBREF 5C3I A 1 175 UNP Q9Y294 ASF1A_HUMAN 1 175
DBREF 5C3I B 0 135 UNP P68431 H31_HUMAN 1 136
DBREF 5C3I C 0 102 UNP P62805 H4_HUMAN 1 103
DBREF 5C3I D 63 126 UNP P49736 MCM2_HUMAN 63 124
DBREF 5C3I D 127 156 PDB 5C3I 5C3I 127 156
DBREF 5C3I E 1 175 UNP Q9Y294 ASF1A_HUMAN 1 175
DBREF 5C3I F 0 135 UNP P68431 H31_HUMAN 1 136
DBREF 5C3I G 0 102 UNP P62805 H4_HUMAN 1 103
DBREF 5C3I H 63 124 UNP P49736 MCM2_HUMAN 63 124
DBREF 5C3I H 125 154 PDB 5C3I 5C3I 125 154
DBREF 5C3I I 1 175 UNP Q9Y294 ASF1A_HUMAN 1 175
DBREF 5C3I J 0 135 UNP P68431 H31_HUMAN 1 136
DBREF 5C3I K 0 102 UNP P62805 H4_HUMAN 1 103
DBREF 5C3I L 63 124 UNP P49736 MCM2_HUMAN 63 124
DBREF 5C3I L 125 154 PDB 5C3I 5C3I 125 154
DBREF 5C3I M 1 175 UNP Q9Y294 ASF1A_HUMAN 1 175
DBREF 5C3I N 0 135 UNP P68431 H31_HUMAN 1 136
DBREF 5C3I O 0 102 UNP P62805 H4_HUMAN 1 103
DBREF 5C3I P 63 124 UNP P49736 MCM2_HUMAN 63 124
DBREF 5C3I P 125 154 PDB 5C3I 5C3I 125 154
DBREF 5C3I Q 1 175 UNP Q9Y294 ASF1A_HUMAN 1 175
DBREF 5C3I R 0 135 UNP P68431 H31_HUMAN 1 136
DBREF 5C3I S 0 102 UNP P62805 H4_HUMAN 1 103
DBREF 5C3I T 63 124 UNP P49736 MCM2_HUMAN 63 124
DBREF 5C3I T 125 154 PDB 5C3I 5C3I 125 154
DBREF 5C3I U 1 175 UNP Q9Y294 ASF1A_HUMAN 1 175
DBREF 5C3I V 0 135 UNP P68431 H31_HUMAN 1 136
DBREF 5C3I W 0 102 UNP P62805 H4_HUMAN 1 103
DBREF 5C3I X 63 124 UNP P49736 MCM2_HUMAN 63 124
DBREF 5C3I X 125 154 PDB 5C3I 5C3I 125 154
SEQADV 5C3I MET A -12 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I GLY A -11 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I SER A -10 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I HIS A -9 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I HIS A -8 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I HIS A -7 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I HIS A -6 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I HIS A -5 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I HIS A -4 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I SER A -3 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I ASN A -2 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I ASP A -1 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I PRO A 0 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I SER D 62 UNP P49736 EXPRESSION TAG
SEQADV 5C3I MET E -12 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I GLY E -11 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I SER E -10 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I HIS E -9 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I HIS E -8 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I HIS E -7 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I HIS E -6 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I HIS E -5 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I HIS E -4 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I SER E -3 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I ASN E -2 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I ASP E -1 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I PRO E 0 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I SER H 62 UNP P49736 EXPRESSION TAG
SEQADV 5C3I MET I -12 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I GLY I -11 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I SER I -10 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I HIS I -9 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I HIS I -8 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I HIS I -7 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I HIS I -6 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I HIS I -5 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I HIS I -4 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I SER I -3 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I ASN I -2 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I ASP I -1 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I PRO I 0 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I SER L 62 UNP P49736 EXPRESSION TAG
SEQADV 5C3I MET M -12 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I GLY M -11 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I SER M -10 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I HIS M -9 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I HIS M -8 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I HIS M -7 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I HIS M -6 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I HIS M -5 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I HIS M -4 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I SER M -3 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I ASN M -2 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I ASP M -1 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I PRO M 0 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I SER P 62 UNP P49736 EXPRESSION TAG
SEQADV 5C3I MET Q -12 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I GLY Q -11 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I SER Q -10 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I HIS Q -9 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I HIS Q -8 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I HIS Q -7 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I HIS Q -6 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I HIS Q -5 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I HIS Q -4 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I SER Q -3 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I ASN Q -2 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I ASP Q -1 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I PRO Q 0 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I SER T 62 UNP P49736 EXPRESSION TAG
SEQADV 5C3I MET U -12 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I GLY U -11 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I SER U -10 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I HIS U -9 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I HIS U -8 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I HIS U -7 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I HIS U -6 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I HIS U -5 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I HIS U -4 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I SER U -3 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I ASN U -2 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I ASP U -1 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I PRO U 0 UNP Q9Y294 EXPRESSION TAG
SEQADV 5C3I SER X 62 UNP P49736 EXPRESSION TAG
SEQRES 1 A 188 MET GLY SER HIS HIS HIS HIS HIS HIS SER ASN ASP PRO
SEQRES 2 A 188 MET ALA LYS VAL GLN VAL ASN ASN VAL VAL VAL LEU ASP
SEQRES 3 A 188 ASN PRO SER PRO PHE TYR ASN PRO PHE GLN PHE GLU ILE
SEQRES 4 A 188 THR PHE GLU CYS ILE GLU ASP LEU SER GLU ASP LEU GLU
SEQRES 5 A 188 TRP LYS ILE ILE TYR VAL GLY SER ALA GLU SER GLU GLU
SEQRES 6 A 188 TYR ASP GLN VAL LEU ASP SER VAL LEU VAL GLY PRO VAL
SEQRES 7 A 188 PRO ALA GLY ARG HIS MET PHE VAL PHE GLN ALA ASP ALA
SEQRES 8 A 188 PRO ASN PRO GLY LEU ILE PRO ASP ALA ASP ALA VAL GLY
SEQRES 9 A 188 VAL THR VAL VAL LEU ILE THR CYS THR TYR ARG GLY GLN
SEQRES 10 A 188 GLU PHE ILE ARG VAL GLY TYR TYR VAL ASN ASN GLU TYR
SEQRES 11 A 188 THR GLU THR GLU LEU ARG GLU ASN PRO PRO VAL LYS PRO
SEQRES 12 A 188 ASP PHE SER LYS LEU GLN ARG ASN ILE LEU ALA SER ASN
SEQRES 13 A 188 PRO ARG VAL THR ARG PHE HIS ILE ASN TRP GLU ASP ASN
SEQRES 14 A 188 THR GLU LYS LEU GLU ASP ALA GLU SER SER ASN PRO ASN
SEQRES 15 A 188 LEU GLN SER LEU LEU SER
SEQRES 1 B 136 MET ALA ARG THR LYS GLN THR ALA ARG LYS SER THR GLY
SEQRES 2 B 136 GLY LYS ALA PRO ARG LYS GLN LEU ALA THR LYS ALA ALA
SEQRES 3 B 136 ARG LYS SER ALA PRO ALA THR GLY GLY VAL LYS LYS PRO
SEQRES 4 B 136 HIS ARG TYR ARG PRO GLY THR VAL ALA LEU ARG GLU ILE
SEQRES 5 B 136 ARG ARG TYR GLN LYS SER THR GLU LEU LEU ILE ARG LYS
SEQRES 6 B 136 LEU PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA GLN ASP
SEQRES 7 B 136 PHE LYS THR ASP LEU ARG PHE GLN SER SER ALA VAL MET
SEQRES 8 B 136 ALA LEU GLN GLU ALA CYS GLU ALA TYR LEU VAL GLY LEU
SEQRES 9 B 136 PHE GLU ASP THR ASN LEU CYS ALA ILE HIS ALA LYS ARG
SEQRES 10 B 136 VAL THR ILE MET PRO LYS ASP ILE GLN LEU ALA ARG ARG
SEQRES 11 B 136 ILE ARG GLY GLU ARG ALA
SEQRES 1 C 103 MET SER GLY ARG GLY LYS GLY GLY LYS GLY LEU GLY LYS
SEQRES 2 C 103 GLY GLY ALA LYS ARG HIS ARG LYS VAL LEU ARG ASP ASN
SEQRES 3 C 103 ILE GLN GLY ILE THR LYS PRO ALA ILE ARG ARG LEU ALA
SEQRES 4 C 103 ARG ARG GLY GLY VAL LYS ARG ILE SER GLY LEU ILE TYR
SEQRES 5 C 103 GLU GLU THR ARG GLY VAL LEU LYS VAL PHE LEU GLU ASN
SEQRES 6 C 103 VAL ILE ARG ASP ALA VAL THR TYR THR GLU HIS ALA LYS
SEQRES 7 C 103 ARG LYS THR VAL THR ALA MET ASP VAL VAL TYR ALA LEU
SEQRES 8 C 103 LYS ARG GLN GLY ARG THR LEU TYR GLY PHE GLY GLY
SEQRES 1 D 93 SER LEU GLU GLU GLU GLU ASP GLY GLU GLU LEU ILE GLY
SEQRES 2 D 93 ASP GLY MET GLU ARG ASP TYR ARG ALA ILE PRO GLU LEU
SEQRES 3 D 93 ASP ALA TYR GLU ALA GLU GLY LEU ALA LEU ASP ASP GLU
SEQRES 4 D 93 ASP VAL GLU GLU LEU THR ALA SER GLN ARG GLU ALA ALA
SEQRES 5 D 93 GLU ARG ALA MET ARG GLN ARG ASP ARG GLU ALA UNK UNK
SEQRES 6 D 93 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 7 D 93 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 8 D 93 UNK UNK
SEQRES 1 E 188 MET GLY SER HIS HIS HIS HIS HIS HIS SER ASN ASP PRO
SEQRES 2 E 188 MET ALA LYS VAL GLN VAL ASN ASN VAL VAL VAL LEU ASP
SEQRES 3 E 188 ASN PRO SER PRO PHE TYR ASN PRO PHE GLN PHE GLU ILE
SEQRES 4 E 188 THR PHE GLU CYS ILE GLU ASP LEU SER GLU ASP LEU GLU
SEQRES 5 E 188 TRP LYS ILE ILE TYR VAL GLY SER ALA GLU SER GLU GLU
SEQRES 6 E 188 TYR ASP GLN VAL LEU ASP SER VAL LEU VAL GLY PRO VAL
SEQRES 7 E 188 PRO ALA GLY ARG HIS MET PHE VAL PHE GLN ALA ASP ALA
SEQRES 8 E 188 PRO ASN PRO GLY LEU ILE PRO ASP ALA ASP ALA VAL GLY
SEQRES 9 E 188 VAL THR VAL VAL LEU ILE THR CYS THR TYR ARG GLY GLN
SEQRES 10 E 188 GLU PHE ILE ARG VAL GLY TYR TYR VAL ASN ASN GLU TYR
SEQRES 11 E 188 THR GLU THR GLU LEU ARG GLU ASN PRO PRO VAL LYS PRO
SEQRES 12 E 188 ASP PHE SER LYS LEU GLN ARG ASN ILE LEU ALA SER ASN
SEQRES 13 E 188 PRO ARG VAL THR ARG PHE HIS ILE ASN TRP GLU ASP ASN
SEQRES 14 E 188 THR GLU LYS LEU GLU ASP ALA GLU SER SER ASN PRO ASN
SEQRES 15 E 188 LEU GLN SER LEU LEU SER
SEQRES 1 F 136 MET ALA ARG THR LYS GLN THR ALA ARG LYS SER THR GLY
SEQRES 2 F 136 GLY LYS ALA PRO ARG LYS GLN LEU ALA THR LYS ALA ALA
SEQRES 3 F 136 ARG LYS SER ALA PRO ALA THR GLY GLY VAL LYS LYS PRO
SEQRES 4 F 136 HIS ARG TYR ARG PRO GLY THR VAL ALA LEU ARG GLU ILE
SEQRES 5 F 136 ARG ARG TYR GLN LYS SER THR GLU LEU LEU ILE ARG LYS
SEQRES 6 F 136 LEU PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA GLN ASP
SEQRES 7 F 136 PHE LYS THR ASP LEU ARG PHE GLN SER SER ALA VAL MET
SEQRES 8 F 136 ALA LEU GLN GLU ALA CYS GLU ALA TYR LEU VAL GLY LEU
SEQRES 9 F 136 PHE GLU ASP THR ASN LEU CYS ALA ILE HIS ALA LYS ARG
SEQRES 10 F 136 VAL THR ILE MET PRO LYS ASP ILE GLN LEU ALA ARG ARG
SEQRES 11 F 136 ILE ARG GLY GLU ARG ALA
SEQRES 1 G 103 MET SER GLY ARG GLY LYS GLY GLY LYS GLY LEU GLY LYS
SEQRES 2 G 103 GLY GLY ALA LYS ARG HIS ARG LYS VAL LEU ARG ASP ASN
SEQRES 3 G 103 ILE GLN GLY ILE THR LYS PRO ALA ILE ARG ARG LEU ALA
SEQRES 4 G 103 ARG ARG GLY GLY VAL LYS ARG ILE SER GLY LEU ILE TYR
SEQRES 5 G 103 GLU GLU THR ARG GLY VAL LEU LYS VAL PHE LEU GLU ASN
SEQRES 6 G 103 VAL ILE ARG ASP ALA VAL THR TYR THR GLU HIS ALA LYS
SEQRES 7 G 103 ARG LYS THR VAL THR ALA MET ASP VAL VAL TYR ALA LEU
SEQRES 8 G 103 LYS ARG GLN GLY ARG THR LEU TYR GLY PHE GLY GLY
SEQRES 1 H 93 SER LEU GLU GLU GLU GLU ASP GLY GLU GLU LEU ILE GLY
SEQRES 2 H 93 ASP GLY MET GLU ARG ASP TYR ARG ALA ILE PRO GLU LEU
SEQRES 3 H 93 ASP ALA TYR GLU ALA GLU GLY LEU ALA LEU ASP ASP GLU
SEQRES 4 H 93 ASP VAL GLU GLU LEU THR ALA SER GLN ARG GLU ALA ALA
SEQRES 5 H 93 GLU ARG ALA MET ARG GLN ARG ASP ARG GLU ALA UNK UNK
SEQRES 6 H 93 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 7 H 93 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 8 H 93 UNK UNK
SEQRES 1 I 188 MET GLY SER HIS HIS HIS HIS HIS HIS SER ASN ASP PRO
SEQRES 2 I 188 MET ALA LYS VAL GLN VAL ASN ASN VAL VAL VAL LEU ASP
SEQRES 3 I 188 ASN PRO SER PRO PHE TYR ASN PRO PHE GLN PHE GLU ILE
SEQRES 4 I 188 THR PHE GLU CYS ILE GLU ASP LEU SER GLU ASP LEU GLU
SEQRES 5 I 188 TRP LYS ILE ILE TYR VAL GLY SER ALA GLU SER GLU GLU
SEQRES 6 I 188 TYR ASP GLN VAL LEU ASP SER VAL LEU VAL GLY PRO VAL
SEQRES 7 I 188 PRO ALA GLY ARG HIS MET PHE VAL PHE GLN ALA ASP ALA
SEQRES 8 I 188 PRO ASN PRO GLY LEU ILE PRO ASP ALA ASP ALA VAL GLY
SEQRES 9 I 188 VAL THR VAL VAL LEU ILE THR CYS THR TYR ARG GLY GLN
SEQRES 10 I 188 GLU PHE ILE ARG VAL GLY TYR TYR VAL ASN ASN GLU TYR
SEQRES 11 I 188 THR GLU THR GLU LEU ARG GLU ASN PRO PRO VAL LYS PRO
SEQRES 12 I 188 ASP PHE SER LYS LEU GLN ARG ASN ILE LEU ALA SER ASN
SEQRES 13 I 188 PRO ARG VAL THR ARG PHE HIS ILE ASN TRP GLU ASP ASN
SEQRES 14 I 188 THR GLU LYS LEU GLU ASP ALA GLU SER SER ASN PRO ASN
SEQRES 15 I 188 LEU GLN SER LEU LEU SER
SEQRES 1 J 136 MET ALA ARG THR LYS GLN THR ALA ARG LYS SER THR GLY
SEQRES 2 J 136 GLY LYS ALA PRO ARG LYS GLN LEU ALA THR LYS ALA ALA
SEQRES 3 J 136 ARG LYS SER ALA PRO ALA THR GLY GLY VAL LYS LYS PRO
SEQRES 4 J 136 HIS ARG TYR ARG PRO GLY THR VAL ALA LEU ARG GLU ILE
SEQRES 5 J 136 ARG ARG TYR GLN LYS SER THR GLU LEU LEU ILE ARG LYS
SEQRES 6 J 136 LEU PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA GLN ASP
SEQRES 7 J 136 PHE LYS THR ASP LEU ARG PHE GLN SER SER ALA VAL MET
SEQRES 8 J 136 ALA LEU GLN GLU ALA CYS GLU ALA TYR LEU VAL GLY LEU
SEQRES 9 J 136 PHE GLU ASP THR ASN LEU CYS ALA ILE HIS ALA LYS ARG
SEQRES 10 J 136 VAL THR ILE MET PRO LYS ASP ILE GLN LEU ALA ARG ARG
SEQRES 11 J 136 ILE ARG GLY GLU ARG ALA
SEQRES 1 K 103 MET SER GLY ARG GLY LYS GLY GLY LYS GLY LEU GLY LYS
SEQRES 2 K 103 GLY GLY ALA LYS ARG HIS ARG LYS VAL LEU ARG ASP ASN
SEQRES 3 K 103 ILE GLN GLY ILE THR LYS PRO ALA ILE ARG ARG LEU ALA
SEQRES 4 K 103 ARG ARG GLY GLY VAL LYS ARG ILE SER GLY LEU ILE TYR
SEQRES 5 K 103 GLU GLU THR ARG GLY VAL LEU LYS VAL PHE LEU GLU ASN
SEQRES 6 K 103 VAL ILE ARG ASP ALA VAL THR TYR THR GLU HIS ALA LYS
SEQRES 7 K 103 ARG LYS THR VAL THR ALA MET ASP VAL VAL TYR ALA LEU
SEQRES 8 K 103 LYS ARG GLN GLY ARG THR LEU TYR GLY PHE GLY GLY
SEQRES 1 L 93 SER LEU GLU GLU GLU GLU ASP GLY GLU GLU LEU ILE GLY
SEQRES 2 L 93 ASP GLY MET GLU ARG ASP TYR ARG ALA ILE PRO GLU LEU
SEQRES 3 L 93 ASP ALA TYR GLU ALA GLU GLY LEU ALA LEU ASP ASP GLU
SEQRES 4 L 93 ASP VAL GLU GLU LEU THR ALA SER GLN ARG GLU ALA ALA
SEQRES 5 L 93 GLU ARG ALA MET ARG GLN ARG ASP ARG GLU ALA UNK UNK
SEQRES 6 L 93 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 7 L 93 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 8 L 93 UNK UNK
SEQRES 1 M 188 MET GLY SER HIS HIS HIS HIS HIS HIS SER ASN ASP PRO
SEQRES 2 M 188 MET ALA LYS VAL GLN VAL ASN ASN VAL VAL VAL LEU ASP
SEQRES 3 M 188 ASN PRO SER PRO PHE TYR ASN PRO PHE GLN PHE GLU ILE
SEQRES 4 M 188 THR PHE GLU CYS ILE GLU ASP LEU SER GLU ASP LEU GLU
SEQRES 5 M 188 TRP LYS ILE ILE TYR VAL GLY SER ALA GLU SER GLU GLU
SEQRES 6 M 188 TYR ASP GLN VAL LEU ASP SER VAL LEU VAL GLY PRO VAL
SEQRES 7 M 188 PRO ALA GLY ARG HIS MET PHE VAL PHE GLN ALA ASP ALA
SEQRES 8 M 188 PRO ASN PRO GLY LEU ILE PRO ASP ALA ASP ALA VAL GLY
SEQRES 9 M 188 VAL THR VAL VAL LEU ILE THR CYS THR TYR ARG GLY GLN
SEQRES 10 M 188 GLU PHE ILE ARG VAL GLY TYR TYR VAL ASN ASN GLU TYR
SEQRES 11 M 188 THR GLU THR GLU LEU ARG GLU ASN PRO PRO VAL LYS PRO
SEQRES 12 M 188 ASP PHE SER LYS LEU GLN ARG ASN ILE LEU ALA SER ASN
SEQRES 13 M 188 PRO ARG VAL THR ARG PHE HIS ILE ASN TRP GLU ASP ASN
SEQRES 14 M 188 THR GLU LYS LEU GLU ASP ALA GLU SER SER ASN PRO ASN
SEQRES 15 M 188 LEU GLN SER LEU LEU SER
SEQRES 1 N 136 MET ALA ARG THR LYS GLN THR ALA ARG LYS SER THR GLY
SEQRES 2 N 136 GLY LYS ALA PRO ARG LYS GLN LEU ALA THR LYS ALA ALA
SEQRES 3 N 136 ARG LYS SER ALA PRO ALA THR GLY GLY VAL LYS LYS PRO
SEQRES 4 N 136 HIS ARG TYR ARG PRO GLY THR VAL ALA LEU ARG GLU ILE
SEQRES 5 N 136 ARG ARG TYR GLN LYS SER THR GLU LEU LEU ILE ARG LYS
SEQRES 6 N 136 LEU PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA GLN ASP
SEQRES 7 N 136 PHE LYS THR ASP LEU ARG PHE GLN SER SER ALA VAL MET
SEQRES 8 N 136 ALA LEU GLN GLU ALA CYS GLU ALA TYR LEU VAL GLY LEU
SEQRES 9 N 136 PHE GLU ASP THR ASN LEU CYS ALA ILE HIS ALA LYS ARG
SEQRES 10 N 136 VAL THR ILE MET PRO LYS ASP ILE GLN LEU ALA ARG ARG
SEQRES 11 N 136 ILE ARG GLY GLU ARG ALA
SEQRES 1 O 103 MET SER GLY ARG GLY LYS GLY GLY LYS GLY LEU GLY LYS
SEQRES 2 O 103 GLY GLY ALA LYS ARG HIS ARG LYS VAL LEU ARG ASP ASN
SEQRES 3 O 103 ILE GLN GLY ILE THR LYS PRO ALA ILE ARG ARG LEU ALA
SEQRES 4 O 103 ARG ARG GLY GLY VAL LYS ARG ILE SER GLY LEU ILE TYR
SEQRES 5 O 103 GLU GLU THR ARG GLY VAL LEU LYS VAL PHE LEU GLU ASN
SEQRES 6 O 103 VAL ILE ARG ASP ALA VAL THR TYR THR GLU HIS ALA LYS
SEQRES 7 O 103 ARG LYS THR VAL THR ALA MET ASP VAL VAL TYR ALA LEU
SEQRES 8 O 103 LYS ARG GLN GLY ARG THR LEU TYR GLY PHE GLY GLY
SEQRES 1 P 93 SER LEU GLU GLU GLU GLU ASP GLY GLU GLU LEU ILE GLY
SEQRES 2 P 93 ASP GLY MET GLU ARG ASP TYR ARG ALA ILE PRO GLU LEU
SEQRES 3 P 93 ASP ALA TYR GLU ALA GLU GLY LEU ALA LEU ASP ASP GLU
SEQRES 4 P 93 ASP VAL GLU GLU LEU THR ALA SER GLN ARG GLU ALA ALA
SEQRES 5 P 93 GLU ARG ALA MET ARG GLN ARG ASP ARG GLU ALA UNK UNK
SEQRES 6 P 93 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 7 P 93 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 8 P 93 UNK UNK
SEQRES 1 Q 188 MET GLY SER HIS HIS HIS HIS HIS HIS SER ASN ASP PRO
SEQRES 2 Q 188 MET ALA LYS VAL GLN VAL ASN ASN VAL VAL VAL LEU ASP
SEQRES 3 Q 188 ASN PRO SER PRO PHE TYR ASN PRO PHE GLN PHE GLU ILE
SEQRES 4 Q 188 THR PHE GLU CYS ILE GLU ASP LEU SER GLU ASP LEU GLU
SEQRES 5 Q 188 TRP LYS ILE ILE TYR VAL GLY SER ALA GLU SER GLU GLU
SEQRES 6 Q 188 TYR ASP GLN VAL LEU ASP SER VAL LEU VAL GLY PRO VAL
SEQRES 7 Q 188 PRO ALA GLY ARG HIS MET PHE VAL PHE GLN ALA ASP ALA
SEQRES 8 Q 188 PRO ASN PRO GLY LEU ILE PRO ASP ALA ASP ALA VAL GLY
SEQRES 9 Q 188 VAL THR VAL VAL LEU ILE THR CYS THR TYR ARG GLY GLN
SEQRES 10 Q 188 GLU PHE ILE ARG VAL GLY TYR TYR VAL ASN ASN GLU TYR
SEQRES 11 Q 188 THR GLU THR GLU LEU ARG GLU ASN PRO PRO VAL LYS PRO
SEQRES 12 Q 188 ASP PHE SER LYS LEU GLN ARG ASN ILE LEU ALA SER ASN
SEQRES 13 Q 188 PRO ARG VAL THR ARG PHE HIS ILE ASN TRP GLU ASP ASN
SEQRES 14 Q 188 THR GLU LYS LEU GLU ASP ALA GLU SER SER ASN PRO ASN
SEQRES 15 Q 188 LEU GLN SER LEU LEU SER
SEQRES 1 R 136 MET ALA ARG THR LYS GLN THR ALA ARG LYS SER THR GLY
SEQRES 2 R 136 GLY LYS ALA PRO ARG LYS GLN LEU ALA THR LYS ALA ALA
SEQRES 3 R 136 ARG LYS SER ALA PRO ALA THR GLY GLY VAL LYS LYS PRO
SEQRES 4 R 136 HIS ARG TYR ARG PRO GLY THR VAL ALA LEU ARG GLU ILE
SEQRES 5 R 136 ARG ARG TYR GLN LYS SER THR GLU LEU LEU ILE ARG LYS
SEQRES 6 R 136 LEU PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA GLN ASP
SEQRES 7 R 136 PHE LYS THR ASP LEU ARG PHE GLN SER SER ALA VAL MET
SEQRES 8 R 136 ALA LEU GLN GLU ALA CYS GLU ALA TYR LEU VAL GLY LEU
SEQRES 9 R 136 PHE GLU ASP THR ASN LEU CYS ALA ILE HIS ALA LYS ARG
SEQRES 10 R 136 VAL THR ILE MET PRO LYS ASP ILE GLN LEU ALA ARG ARG
SEQRES 11 R 136 ILE ARG GLY GLU ARG ALA
SEQRES 1 S 103 MET SER GLY ARG GLY LYS GLY GLY LYS GLY LEU GLY LYS
SEQRES 2 S 103 GLY GLY ALA LYS ARG HIS ARG LYS VAL LEU ARG ASP ASN
SEQRES 3 S 103 ILE GLN GLY ILE THR LYS PRO ALA ILE ARG ARG LEU ALA
SEQRES 4 S 103 ARG ARG GLY GLY VAL LYS ARG ILE SER GLY LEU ILE TYR
SEQRES 5 S 103 GLU GLU THR ARG GLY VAL LEU LYS VAL PHE LEU GLU ASN
SEQRES 6 S 103 VAL ILE ARG ASP ALA VAL THR TYR THR GLU HIS ALA LYS
SEQRES 7 S 103 ARG LYS THR VAL THR ALA MET ASP VAL VAL TYR ALA LEU
SEQRES 8 S 103 LYS ARG GLN GLY ARG THR LEU TYR GLY PHE GLY GLY
SEQRES 1 T 93 SER LEU GLU GLU GLU GLU ASP GLY GLU GLU LEU ILE GLY
SEQRES 2 T 93 ASP GLY MET GLU ARG ASP TYR ARG ALA ILE PRO GLU LEU
SEQRES 3 T 93 ASP ALA TYR GLU ALA GLU GLY LEU ALA LEU ASP ASP GLU
SEQRES 4 T 93 ASP VAL GLU GLU LEU THR ALA SER GLN ARG GLU ALA ALA
SEQRES 5 T 93 GLU ARG ALA MET ARG GLN ARG ASP ARG GLU ALA UNK UNK
SEQRES 6 T 93 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 7 T 93 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 8 T 93 UNK UNK
SEQRES 1 U 188 MET GLY SER HIS HIS HIS HIS HIS HIS SER ASN ASP PRO
SEQRES 2 U 188 MET ALA LYS VAL GLN VAL ASN ASN VAL VAL VAL LEU ASP
SEQRES 3 U 188 ASN PRO SER PRO PHE TYR ASN PRO PHE GLN PHE GLU ILE
SEQRES 4 U 188 THR PHE GLU CYS ILE GLU ASP LEU SER GLU ASP LEU GLU
SEQRES 5 U 188 TRP LYS ILE ILE TYR VAL GLY SER ALA GLU SER GLU GLU
SEQRES 6 U 188 TYR ASP GLN VAL LEU ASP SER VAL LEU VAL GLY PRO VAL
SEQRES 7 U 188 PRO ALA GLY ARG HIS MET PHE VAL PHE GLN ALA ASP ALA
SEQRES 8 U 188 PRO ASN PRO GLY LEU ILE PRO ASP ALA ASP ALA VAL GLY
SEQRES 9 U 188 VAL THR VAL VAL LEU ILE THR CYS THR TYR ARG GLY GLN
SEQRES 10 U 188 GLU PHE ILE ARG VAL GLY TYR TYR VAL ASN ASN GLU TYR
SEQRES 11 U 188 THR GLU THR GLU LEU ARG GLU ASN PRO PRO VAL LYS PRO
SEQRES 12 U 188 ASP PHE SER LYS LEU GLN ARG ASN ILE LEU ALA SER ASN
SEQRES 13 U 188 PRO ARG VAL THR ARG PHE HIS ILE ASN TRP GLU ASP ASN
SEQRES 14 U 188 THR GLU LYS LEU GLU ASP ALA GLU SER SER ASN PRO ASN
SEQRES 15 U 188 LEU GLN SER LEU LEU SER
SEQRES 1 V 136 MET ALA ARG THR LYS GLN THR ALA ARG LYS SER THR GLY
SEQRES 2 V 136 GLY LYS ALA PRO ARG LYS GLN LEU ALA THR LYS ALA ALA
SEQRES 3 V 136 ARG LYS SER ALA PRO ALA THR GLY GLY VAL LYS LYS PRO
SEQRES 4 V 136 HIS ARG TYR ARG PRO GLY THR VAL ALA LEU ARG GLU ILE
SEQRES 5 V 136 ARG ARG TYR GLN LYS SER THR GLU LEU LEU ILE ARG LYS
SEQRES 6 V 136 LEU PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA GLN ASP
SEQRES 7 V 136 PHE LYS THR ASP LEU ARG PHE GLN SER SER ALA VAL MET
SEQRES 8 V 136 ALA LEU GLN GLU ALA CYS GLU ALA TYR LEU VAL GLY LEU
SEQRES 9 V 136 PHE GLU ASP THR ASN LEU CYS ALA ILE HIS ALA LYS ARG
SEQRES 10 V 136 VAL THR ILE MET PRO LYS ASP ILE GLN LEU ALA ARG ARG
SEQRES 11 V 136 ILE ARG GLY GLU ARG ALA
SEQRES 1 W 103 MET SER GLY ARG GLY LYS GLY GLY LYS GLY LEU GLY LYS
SEQRES 2 W 103 GLY GLY ALA LYS ARG HIS ARG LYS VAL LEU ARG ASP ASN
SEQRES 3 W 103 ILE GLN GLY ILE THR LYS PRO ALA ILE ARG ARG LEU ALA
SEQRES 4 W 103 ARG ARG GLY GLY VAL LYS ARG ILE SER GLY LEU ILE TYR
SEQRES 5 W 103 GLU GLU THR ARG GLY VAL LEU LYS VAL PHE LEU GLU ASN
SEQRES 6 W 103 VAL ILE ARG ASP ALA VAL THR TYR THR GLU HIS ALA LYS
SEQRES 7 W 103 ARG LYS THR VAL THR ALA MET ASP VAL VAL TYR ALA LEU
SEQRES 8 W 103 LYS ARG GLN GLY ARG THR LEU TYR GLY PHE GLY GLY
SEQRES 1 X 93 SER LEU GLU GLU GLU GLU ASP GLY GLU GLU LEU ILE GLY
SEQRES 2 X 93 ASP GLY MET GLU ARG ASP TYR ARG ALA ILE PRO GLU LEU
SEQRES 3 X 93 ASP ALA TYR GLU ALA GLU GLY LEU ALA LEU ASP ASP GLU
SEQRES 4 X 93 ASP VAL GLU GLU LEU THR ALA SER GLN ARG GLU ALA ALA
SEQRES 5 X 93 GLU ARG ALA MET ARG GLN ARG ASP ARG GLU ALA UNK UNK
SEQRES 6 X 93 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 7 X 93 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 8 X 93 UNK UNK
HELIX 1 AA1 SER A 50 GLU A 52 5 3
HELIX 2 AA2 ASN A 80 ILE A 84 5 5
HELIX 3 AA3 PRO A 85 VAL A 90 1 6
HELIX 4 AA4 GLU A 119 ASN A 125 1 7
HELIX 5 AA5 ASP A 131 SER A 133 5 3
HELIX 6 AA6 ARG B 49 THR B 58 1 10
HELIX 7 AA7 ARG B 63 LYS B 79 1 17
HELIX 8 AA8 GLN B 85 ALA B 114 1 30
HELIX 9 AA9 MET B 120 ARG B 131 1 12
HELIX 10 AB1 ASP C 24 ILE C 29 5 6
HELIX 11 AB2 THR C 30 GLY C 42 1 13
HELIX 12 AB3 LEU C 49 ALA C 76 1 28
HELIX 13 AB4 THR C 82 ARG C 92 1 11
HELIX 14 AB5 THR D 106 ASP D 121 1 16
HELIX 15 AB6 SER E 50 GLU E 52 5 3
HELIX 16 AB7 PRO E 85 VAL E 90 1 6
HELIX 17 AB8 GLU E 119 ASN E 125 1 7
HELIX 18 AB9 ASP E 131 SER E 133 5 3
HELIX 19 AC1 ARG F 63 ASP F 77 1 15
HELIX 20 AC2 GLN F 85 ALA F 114 1 30
HELIX 21 AC3 MET F 120 ARG F 131 1 12
HELIX 22 AC4 ASN G 25 ILE G 29 5 5
HELIX 23 AC5 THR G 30 GLY G 42 1 13
HELIX 24 AC6 LEU G 49 ALA G 76 1 28
HELIX 25 AC7 THR G 82 ARG G 92 1 11
HELIX 26 AC8 GLY H 76 TYR H 81 1 6
HELIX 27 AC9 THR H 106 ARG H 122 1 17
HELIX 28 AD1 SER I 50 GLU I 52 5 3
HELIX 29 AD2 ASN I 80 ILE I 84 5 5
HELIX 30 AD3 PRO I 85 VAL I 90 1 6
HELIX 31 AD4 GLU I 119 ASN I 125 1 7
HELIX 32 AD5 ASP I 131 SER I 133 5 3
HELIX 33 AD6 ARG J 63 LYS J 79 1 17
HELIX 34 AD7 GLN J 85 ALA J 114 1 30
HELIX 35 AD8 MET J 120 ILE J 130 1 11
HELIX 36 AD9 THR K 30 GLY K 42 1 13
HELIX 37 AE1 LEU K 49 ALA K 76 1 28
HELIX 38 AE2 THR K 82 GLY K 94 1 13
HELIX 39 AE3 MET L 77 ARG L 82 5 6
HELIX 40 AE4 THR L 106 GLU L 123 1 18
HELIX 41 AE5 SER M 50 GLU M 52 5 3
HELIX 42 AE6 ASN M 80 ILE M 84 5 5
HELIX 43 AE7 PRO M 85 VAL M 90 1 6
HELIX 44 AE8 GLU M 119 ASN M 125 1 7
HELIX 45 AE9 ASP M 131 SER M 133 5 3
HELIX 46 AF1 ARG N 63 ASP N 77 1 15
HELIX 47 AF2 GLN N 85 ALA N 114 1 30
HELIX 48 AF3 MET N 120 ARG N 131 1 12
HELIX 49 AF4 ASN O 25 ILE O 29 5 5
HELIX 50 AF5 THR O 30 GLY O 42 1 13
HELIX 51 AF6 LEU O 49 ALA O 76 1 28
HELIX 52 AF7 THR O 82 ARG O 92 1 11
HELIX 53 AF8 GLY P 76 TYR P 81 1 6
HELIX 54 AF9 THR P 106 ALA P 116 1 11
HELIX 55 AG1 SER Q 50 GLU Q 52 5 3
HELIX 56 AG2 ASN Q 80 ILE Q 84 5 5
HELIX 57 AG3 PRO Q 85 VAL Q 90 1 6
HELIX 58 AG4 GLU Q 119 ASN Q 125 1 7
HELIX 59 AG5 ASP Q 131 SER Q 133 5 3
HELIX 60 AG6 ARG R 63 LYS R 79 1 17
HELIX 61 AG7 GLN R 85 ALA R 114 1 30
HELIX 62 AG8 MET R 120 ILE R 130 1 11
HELIX 63 AG9 ASP S 24 ILE S 29 5 6
HELIX 64 AH1 THR S 30 GLY S 42 1 13
HELIX 65 AH2 LEU S 49 ALA S 76 1 28
HELIX 66 AH3 THR S 82 GLY S 94 1 13
HELIX 67 AH4 MET T 77 ARG T 82 5 6
HELIX 68 AH5 THR T 106 ALA T 124 1 19
HELIX 69 AH6 SER U 50 GLU U 52 5 3
HELIX 70 AH7 ASN U 80 ILE U 84 5 5
HELIX 71 AH8 PRO U 85 VAL U 90 1 6
HELIX 72 AH9 GLU U 119 ASN U 125 1 7
HELIX 73 AI1 ASP U 131 SER U 133 5 3
HELIX 74 AI2 ARG V 63 LYS V 79 1 17
HELIX 75 AI3 GLN V 85 ALA V 114 1 30
HELIX 76 AI4 MET V 120 ARG V 131 1 12
HELIX 77 AI5 ASP W 24 ILE W 29 5 6
HELIX 78 AI6 THR W 30 GLY W 41 1 12
HELIX 79 AI7 LEU W 49 ALA W 76 1 28
HELIX 80 AI8 THR W 82 ARG W 92 1 11
HELIX 81 AI9 THR X 106 GLU X 123 1 18
SHEET 1 AA1 3 VAL A 4 VAL A 11 0
SHEET 2 AA1 3 PHE A 22 CYS A 30 -1 O GLU A 29 N GLN A 5
SHEET 3 AA1 3 GLY A 68 ALA A 76 -1 O GLY A 68 N CYS A 30
SHEET 1 AA2 5 SER A 16 PRO A 17 0
SHEET 2 AA2 5 LEU A 135 ILE A 139 -1 O ARG A 137 N SER A 16
SHEET 3 AA2 5 GLN A 104 TYR A 117 -1 N GLU A 116 O GLN A 136
SHEET 4 AA2 5 ARG A 145 ARG A 148 -1 O THR A 147 N ARG A 108
SHEET 5 AA2 5 ARG C 95 TYR C 98 -1 O ARG C 95 N ARG A 148
SHEET 1 AA3 7 SER A 16 PRO A 17 0
SHEET 2 AA3 7 LEU A 135 ILE A 139 -1 O ARG A 137 N SER A 16
SHEET 3 AA3 7 GLN A 104 TYR A 117 -1 N GLU A 116 O GLN A 136
SHEET 4 AA3 7 VAL A 92 TYR A 101 -1 N THR A 93 O VAL A 113
SHEET 5 AA3 7 LEU A 38 VAL A 45 -1 N ILE A 43 O LEU A 96
SHEET 6 AA3 7 ASP A 54 VAL A 62 -1 O VAL A 62 N LEU A 38
SHEET 7 AA3 7 UNK D 138 UNK D 139 1 O UNK D 139 N LEU A 61
SHEET 1 AA4 2 ARG B 83 PHE B 84 0
SHEET 2 AA4 2 THR C 80 VAL C 81 1 O VAL C 81 N ARG B 83
SHEET 1 AA5 3 THR B 118 ILE B 119 0
SHEET 2 AA5 3 ARG C 45 ILE C 46 1 O ARG C 45 N ILE B 119
SHEET 3 AA5 3 GLU D 70 GLU D 71 -1 O GLU D 70 N ILE C 46
SHEET 1 AA6 3 VAL E 4 VAL E 11 0
SHEET 2 AA6 3 PHE E 22 CYS E 30 -1 O THR E 27 N ASN E 7
SHEET 3 AA6 3 GLY E 68 ALA E 76 -1 O GLY E 68 N CYS E 30
SHEET 1 AA7 6 SER E 16 PRO E 17 0
SHEET 2 AA7 6 LEU E 135 ARG E 148 -1 O ARG E 137 N SER E 16
SHEET 3 AA7 6 GLU E 105 TYR E 117 -1 N TYR E 112 O LEU E 140
SHEET 4 AA7 6 VAL E 92 TYR E 101 -1 N THR E 93 O VAL E 113
SHEET 5 AA7 6 LEU E 38 VAL E 45 -1 N ILE E 43 O LEU E 96
SHEET 6 AA7 6 ASP E 54 VAL E 62 -1 O VAL E 62 N LEU E 38
SHEET 1 AA8 3 SER E 16 PRO E 17 0
SHEET 2 AA8 3 LEU E 135 ARG E 148 -1 O ARG E 137 N SER E 16
SHEET 3 AA8 3 ARG G 95 TYR G 98 -1 O LEU G 97 N VAL E 146
SHEET 1 AA9 5 LYS J 56 THR J 58 0
SHEET 2 AA9 5 LEU F 48 ARG F 53 1 N LEU F 48 O SER J 57
SHEET 3 AA9 5 GLY M 68 ALA M 76 -1 O ARG M 69 N ILE F 51
SHEET 4 AA9 5 PHE M 22 CYS M 30 -1 N PHE M 28 O HIS M 70
SHEET 5 AA9 5 VAL M 4 VAL M 11 -1 N VAL M 10 O GLU M 25
SHEET 1 AB1 2 ARG F 83 PHE F 84 0
SHEET 2 AB1 2 THR G 80 VAL G 81 1 O VAL G 81 N ARG F 83
SHEET 1 AB2 2 ARG G 45 SER G 47 0
SHEET 2 AB2 2 GLY H 69 GLU H 71 -1 O GLU H 70 N ILE G 46
SHEET 1 AB3 3 VAL I 4 VAL I 11 0
SHEET 2 AB3 3 PHE I 22 CYS I 30 -1 O THR I 27 N ASN I 8
SHEET 3 AB3 3 GLY I 68 ALA I 76 -1 O HIS I 70 N PHE I 28
SHEET 1 AB4 6 SER I 16 PRO I 17 0
SHEET 2 AB4 6 LEU I 135 ARG I 148 -1 O ARG I 137 N SER I 16
SHEET 3 AB4 6 GLN I 104 TYR I 117 -1 N TYR I 112 O LEU I 140
SHEET 4 AB4 6 GLY I 91 TYR I 101 -1 N THR I 93 O VAL I 113
SHEET 5 AB4 6 LEU I 38 VAL I 45 -1 N ILE I 43 O LEU I 96
SHEET 6 AB4 6 ASP I 54 VAL I 62 -1 O VAL I 62 N LEU I 38
SHEET 1 AB5 3 SER I 16 PRO I 17 0
SHEET 2 AB5 3 LEU I 135 ARG I 148 -1 O ARG I 137 N SER I 16
SHEET 3 AB5 3 ARG K 95 LEU K 97 -1 O ARG K 95 N ARG I 148
SHEET 1 AB6 7 ARG J 52 ARG J 53 0
SHEET 2 AB6 7 ASP M 54 VAL M 62 1 O LEU M 61 N ARG J 52
SHEET 3 AB6 7 LEU M 38 VAL M 45 -1 N LEU M 38 O VAL M 62
SHEET 4 AB6 7 GLY M 91 TYR M 101 -1 O LEU M 96 N ILE M 43
SHEET 5 AB6 7 GLN M 104 TYR M 117 -1 O VAL M 109 N ILE M 97
SHEET 6 AB6 7 LEU M 135 ILE M 139 -1 O GLN M 136 N GLU M 116
SHEET 7 AB6 7 SER M 16 PRO M 17 -1 N SER M 16 O ARG M 137
SHEET 1 AB7 7 ARG J 52 ARG J 53 0
SHEET 2 AB7 7 ASP M 54 VAL M 62 1 O LEU M 61 N ARG J 52
SHEET 3 AB7 7 LEU M 38 VAL M 45 -1 N LEU M 38 O VAL M 62
SHEET 4 AB7 7 GLY M 91 TYR M 101 -1 O LEU M 96 N ILE M 43
SHEET 5 AB7 7 GLN M 104 TYR M 117 -1 O VAL M 109 N ILE M 97
SHEET 6 AB7 7 ARG M 145 ARG M 148 -1 O THR M 147 N ARG M 108
SHEET 7 AB7 7 THR O 96 TYR O 98 -1 O LEU O 97 N VAL M 146
SHEET 1 AB8 2 ARG J 83 PHE J 84 0
SHEET 2 AB8 2 THR K 80 VAL K 81 1 O VAL K 81 N ARG J 83
SHEET 1 AB9 3 THR J 118 ILE J 119 0
SHEET 2 AB9 3 ARG K 45 ILE K 46 1 O ARG K 45 N ILE J 119
SHEET 3 AB9 3 GLU L 70 GLU L 71 -1 O GLU L 70 N ILE K 46
SHEET 1 AC1 2 ARG N 83 PHE N 84 0
SHEET 2 AC1 2 THR O 80 VAL O 81 1 O VAL O 81 N ARG N 83
SHEET 1 AC2 3 THR N 118 ILE N 119 0
SHEET 2 AC2 3 ARG O 45 ILE O 46 1 O ARG O 45 N ILE N 119
SHEET 3 AC2 3 GLU P 70 GLU P 71 -1 O GLU P 70 N ILE O 46
SHEET 1 AC3 3 VAL Q 4 VAL Q 11 0
SHEET 2 AC3 3 PHE Q 22 CYS Q 30 -1 O GLU Q 29 N GLN Q 5
SHEET 3 AC3 3 GLY Q 68 ALA Q 76 -1 O ALA Q 76 N PHE Q 22
SHEET 1 AC4 6 SER Q 16 PRO Q 17 0
SHEET 2 AC4 6 LEU Q 135 ILE Q 139 -1 O ARG Q 137 N SER Q 16
SHEET 3 AC4 6 GLN Q 104 TYR Q 117 -1 N ASN Q 114 O ASN Q 138
SHEET 4 AC4 6 GLY Q 91 TYR Q 101 -1 N THR Q 93 O VAL Q 113
SHEET 5 AC4 6 LEU Q 38 VAL Q 45 -1 N ILE Q 43 O LEU Q 96
SHEET 6 AC4 6 ASP Q 54 VAL Q 62 -1 O GLN Q 55 N TYR Q 44
SHEET 1 AC5 5 SER Q 16 PRO Q 17 0
SHEET 2 AC5 5 LEU Q 135 ILE Q 139 -1 O ARG Q 137 N SER Q 16
SHEET 3 AC5 5 GLN Q 104 TYR Q 117 -1 N ASN Q 114 O ASN Q 138
SHEET 4 AC5 5 ARG Q 145 ARG Q 148 -1 O THR Q 147 N ARG Q 108
SHEET 5 AC5 5 ARG S 95 LEU S 97 -1 O ARG S 95 N ARG Q 148
SHEET 1 AC6 2 ARG R 83 PHE R 84 0
SHEET 2 AC6 2 THR S 80 VAL S 81 1 O VAL S 81 N ARG R 83
SHEET 1 AC7 2 ARG S 45 ILE S 46 0
SHEET 2 AC7 2 GLU T 70 GLU T 71 -1 O GLU T 70 N ILE S 46
SHEET 1 AC8 3 VAL U 4 VAL U 11 0
SHEET 2 AC8 3 PHE U 22 CYS U 30 -1 O THR U 27 N ASN U 8
SHEET 3 AC8 3 GLY U 68 ALA U 76 -1 O PHE U 72 N ILE U 26
SHEET 1 AC9 6 SER U 16 PRO U 17 0
SHEET 2 AC9 6 LEU U 135 ARG U 148 -1 O ARG U 137 N SER U 16
SHEET 3 AC9 6 GLN U 104 TYR U 117 -1 N TYR U 112 O LEU U 140
SHEET 4 AC9 6 VAL U 92 TYR U 101 -1 N THR U 93 O VAL U 113
SHEET 5 AC9 6 LEU U 38 VAL U 45 -1 N ILE U 43 O LEU U 96
SHEET 6 AC9 6 ASP U 54 VAL U 62 -1 O VAL U 62 N LEU U 38
SHEET 1 AD1 3 SER U 16 PRO U 17 0
SHEET 2 AD1 3 LEU U 135 ARG U 148 -1 O ARG U 137 N SER U 16
SHEET 3 AD1 3 ARG W 95 TYR W 98 -1 O LEU W 97 N VAL U 146
SHEET 1 AD2 2 ARG V 83 PHE V 84 0
SHEET 2 AD2 2 THR W 80 VAL W 81 1 O VAL W 81 N ARG V 83
SHEET 1 AD3 3 THR V 118 ILE V 119 0
SHEET 2 AD3 3 ARG W 45 ILE W 46 1 O ARG W 45 N ILE V 119
SHEET 3 AD3 3 GLU X 70 GLU X 71 -1 O GLU X 70 N ILE W 46
LINK C UNK D 134 N UNK D 135 1555 1555 1.33
LINK C UNK D 135 N UNK D 136 1555 1555 1.33
LINK C UNK D 136 N UNK D 137 1555 1555 1.34
LINK C UNK D 137 N UNK D 138 1555 1555 1.33
LINK C UNK D 138 N UNK D 139 1555 1555 1.33
LINK C UNK D 139 N UNK D 140 1555 1555 1.33
CISPEP 1 ASN A 14 PRO A 15 0 -3.34
CISPEP 2 GLY A 63 PRO A 64 0 -1.87
CISPEP 3 ASN E 14 PRO E 15 0 -2.72
CISPEP 4 GLY E 63 PRO E 64 0 -4.01
CISPEP 5 ASN I 14 PRO I 15 0 -5.01
CISPEP 6 GLY I 63 PRO I 64 0 -6.66
CISPEP 7 ASN M 14 PRO M 15 0 -1.74
CISPEP 8 GLY M 63 PRO M 64 0 -1.13
CISPEP 9 ASN Q 14 PRO Q 15 0 5.06
CISPEP 10 GLY Q 63 PRO Q 64 0 -8.44
CISPEP 11 ASN U 14 PRO U 15 0 -4.07
CISPEP 12 GLY U 63 PRO U 64 0 -2.99
CRYST1 147.704 147.704 261.796 90.00 90.00 120.00 P 31 2 1 36
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 0.006770 0.003909 0.000000 0.00000
SCALE2 0.000000 0.007818 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003820 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
