HEADER NUCLEAR PROTEIN 18-JUN-01 1H6K
TITLE NUCLEAR CAP BINDING COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CBP80;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: MIF4G DOMAIN;
COMPND 5 SYNONYM: NCBP 80 KDA SUBUNIT, CBP80;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: 20 KDA NUCLEAR CAP BINDING PROTEIN;
COMPND 10 CHAIN: X, Y, Z;
COMPND 11 FRAGMENT: RNP DOMAIN;
COMPND 12 SYNONYM: CBP20, NCBP 20 KDA SUBUNIT;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 9 OTHER_DETAILS: EXPRESSION IN INSECT CELLS;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PRSETA
KEYWDS M7G CAP, CAP-BINDING-COMPLEX, RNP DOMAIN, MIF4G DOMAIN, RNA
KEYWDS 2 MATURATION, RNA EXPORT, NUCLEAR PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR C.MAZZA,M.OHNO,A.SEGREF,I.W.MATTAJ,S.CUSACK
REVDAT 5 03-APR-19 1H6K 1 SOURCE
REVDAT 4 23-AUG-17 1H6K 1 REMARK
REVDAT 3 24-FEB-09 1H6K 1 VERSN
REVDAT 2 15-MAR-02 1H6K 1 REMARK DBREF SEQRES
REVDAT 1 13-SEP-01 1H6K 0
JRNL AUTH C.MAZZA,M.OHNO,A.SEGREF,I.W.MATTAJ,S.CUSACK
JRNL TITL CRYSTAL STRUCTURE OF THE HUMAN NUCLEAR CAP BINDING COMPLEX
JRNL REF MOL.CELL V. 8 383 2001
JRNL REFN ISSN 1097-2765
JRNL PMID 11545740
JRNL DOI 10.1016/S1097-2765(01)00299-4
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.0
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 83.0
REMARK 3 NUMBER OF REFLECTIONS : 205458
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) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.203
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2157
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7488
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2650
REMARK 3 BIN FREE R VALUE SET COUNT : 90
REMARK 3 BIN FREE R VALUE : 0.3310
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 19805
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 1710
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.184
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.161
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.130
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.815
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.934
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 20304 ; 0.008 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): 27512 ; 1.045 ; 1.948
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3053 ; 0.077 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 15305 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 11296 ; 0.238 ; 0.200
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): 1844 ; 0.184 ; 0.500
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): 83 ; 0.191 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 26 ; 0.245 ; 0.500
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): 12161 ; 0.580 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 19785 ; 1.124 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 8143 ; 1.633 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 7727 ; 2.774 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1H6K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-JUN-01.
REMARK 100 THE DEPOSITION ID IS D_1290008058.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-FEB-00
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.933
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 208094
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 83.1
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.05800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 40.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.36300
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: MAD
REMARK 200 SOFTWARE USED: SHELXD
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SEE REFERENCES, PH 7.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 37.76350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 151.64550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 80.74000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 151.64550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.76350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 80.74000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 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: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, Y
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, Z
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 400
REMARK 400 COMPOUND
REMARK 400 CHAIN A, B, C ENGINEERED MUTATION ALA479SER
REMARK 400 BINDS TO 5'CAPPED MRNA. AND INVOLVED IN MEDIATING U SNRNA
REMARK 400 EXPORT FROM THE NUCLEUS.
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 LYS A 20
REMARK 465 THR A 21
REMARK 465 SER A 22
REMARK 465 ASP A 23
REMARK 465 ALA A 24
REMARK 465 ASN A 25
REMARK 465 GLU A 26
REMARK 465 PRO A 527
REMARK 465 ASN A 528
REMARK 465 GLN A 529
REMARK 465 ASP A 530
REMARK 465 ASP A 531
REMARK 465 ASP A 532
REMARK 465 ASP A 533
REMARK 465 ASP A 534
REMARK 465 GLU A 535
REMARK 465 GLY A 536
REMARK 465 PHE A 537
REMARK 465 SER A 538
REMARK 465 LEU A 666
REMARK 465 ALA A 667
REMARK 465 ARG A 668
REMARK 465 GLN A 669
REMARK 465 HIS A 670
REMARK 465 ASP A 685
REMARK 465 GLY A 686
REMARK 465 VAL A 687
REMARK 465 LEU A 688
REMARK 465 GLU A 689
REMARK 465 LYS B 20
REMARK 465 THR B 21
REMARK 465 SER B 22
REMARK 465 ASP B 23
REMARK 465 ALA B 24
REMARK 465 ASN B 25
REMARK 465 PRO B 527
REMARK 465 ASN B 528
REMARK 465 GLN B 529
REMARK 465 ASP B 530
REMARK 465 ASP B 531
REMARK 465 ASP B 532
REMARK 465 ASP B 533
REMARK 465 ASP B 534
REMARK 465 GLU B 535
REMARK 465 GLY B 536
REMARK 465 PHE B 537
REMARK 465 SER B 538
REMARK 465 LYS B 665
REMARK 465 LEU B 666
REMARK 465 ALA B 667
REMARK 465 ARG B 668
REMARK 465 GLN B 669
REMARK 465 HIS B 670
REMARK 465 ASP B 685
REMARK 465 GLY B 686
REMARK 465 VAL B 687
REMARK 465 LEU B 688
REMARK 465 LYS C 20
REMARK 465 THR C 21
REMARK 465 SER C 22
REMARK 465 ASP C 23
REMARK 465 ALA C 24
REMARK 465 ASN C 25
REMARK 465 ASN C 528
REMARK 465 GLN C 529
REMARK 465 ASP C 530
REMARK 465 ASP C 531
REMARK 465 ASP C 532
REMARK 465 ASP C 533
REMARK 465 ASP C 534
REMARK 465 GLU C 535
REMARK 465 GLY C 536
REMARK 465 PHE C 537
REMARK 465 LEU C 666
REMARK 465 ALA C 667
REMARK 465 ARG C 668
REMARK 465 GLN C 669
REMARK 465 HIS C 670
REMARK 465 ASP C 685
REMARK 465 GLY C 686
REMARK 465 VAL C 687
REMARK 465 ASP X 22
REMARK 465 GLN X 23
REMARK 465 HIS X 24
REMARK 465 PHE X 25
REMARK 465 ARG X 26
REMARK 465 GLY X 27
REMARK 465 ASP X 28
REMARK 465 ASN X 29
REMARK 465 GLU X 30
REMARK 465 GLU X 31
REMARK 465 GLN X 32
REMARK 465 GLU X 33
REMARK 465 LYS X 34
REMARK 465 LEU X 35
REMARK 465 LEU X 36
REMARK 465 LYS X 37
REMARK 465 LYS X 77
REMARK 465 THR X 79
REMARK 465 ALA X 80
REMARK 465 PHE X 119
REMARK 465 LYS X 120
REMARK 465 ASP Y 22
REMARK 465 GLN Y 23
REMARK 465 HIS Y 24
REMARK 465 PHE Y 25
REMARK 465 ARG Y 26
REMARK 465 GLY Y 27
REMARK 465 ASP Y 28
REMARK 465 ASN Y 29
REMARK 465 GLU Y 30
REMARK 465 GLU Y 31
REMARK 465 GLN Y 32
REMARK 465 GLU Y 33
REMARK 465 LYS Y 34
REMARK 465 LEU Y 35
REMARK 465 LEU Y 36
REMARK 465 LYS Y 37
REMARK 465 LYS Y 77
REMARK 465 THR Y 79
REMARK 465 ALA Y 80
REMARK 465 GLY Y 118
REMARK 465 PHE Y 119
REMARK 465 LYS Y 120
REMARK 465 ASP Z 22
REMARK 465 GLN Z 23
REMARK 465 HIS Z 24
REMARK 465 PHE Z 25
REMARK 465 ARG Z 26
REMARK 465 GLY Z 27
REMARK 465 ASP Z 28
REMARK 465 ASN Z 29
REMARK 465 GLU Z 30
REMARK 465 GLU Z 31
REMARK 465 GLN Z 32
REMARK 465 GLU Z 33
REMARK 465 LYS Z 34
REMARK 465 LEU Z 35
REMARK 465 LEU Z 36
REMARK 465 LYS Z 37
REMARK 465 THR Z 79
REMARK 465 ALA Z 80
REMARK 465 PHE Z 119
REMARK 465 LYS Z 120
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 N ASN A 63 O HOH A 2014 2.15
REMARK 500 O HOH B 2013 O HOH B 2014 2.15
REMARK 500 O HOH Y 2029 O HOH Y 2051 2.16
REMARK 500 O HOH A 2035 O HOH A 2520 2.16
REMARK 500 CD GLN A 207 O HOH A 2128 2.17
REMARK 500 O HOH A 2243 O HOH A 2245 2.17
REMARK 500 O HOH X 2013 O HOH X 2014 2.17
REMARK 500 O HOH C 2147 O HOH C 2370 2.17
REMARK 500 OE1 GLN B 383 O HOH B 2327 2.18
REMARK 500 O HOH C 2096 O HOH C 2260 2.18
REMARK 500 O ASP Y 74 O HOH Y 2034 2.18
REMARK 500 O ALA Y 117 O HOH Y 2063 2.18
REMARK 500 O HOH A 2466 O HOH A 2502 2.18
REMARK 500 OE2 GLU A 592 O HOH A 2428 2.19
REMARK 500 O HOH C 2088 O HOH C 2091 2.19
REMARK 500 CE LYS A 511 O HOH A 2400 2.19
REMARK 500 OE1 GLU A 103 O HOH A 2034 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 293 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP B 293 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP B 403 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP Y 108 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP Z 114 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 THR A 277 -161.91 -112.77
REMARK 500 SER A 386 -35.98 -139.22
REMARK 500 SER A 460 -142.17 -154.68
REMARK 500 ASP A 489 75.57 -64.93
REMARK 500 GLU A 490 -16.28 167.19
REMARK 500 ASN A 493 6.13 -65.87
REMARK 500 PRO A 525 -155.18 -65.36
REMARK 500 GLN A 691 -67.58 -109.66
REMARK 500 LEU A 769 -53.28 -122.43
REMARK 500 LYS B 188 58.63 -141.09
REMARK 500 SER B 386 -37.31 -142.23
REMARK 500 SER B 460 -141.98 -151.34
REMARK 500 PRO B 481 66.23 -69.87
REMARK 500 GLU B 490 -17.74 172.24
REMARK 500 ASN B 493 2.69 -66.63
REMARK 500 SER B 510 25.79 -78.27
REMARK 500 LYS B 511 160.43 61.99
REMARK 500 ALA B 512 132.10 174.96
REMARK 500 PRO B 525 -122.16 -60.26
REMARK 500 PHE B 569 36.32 -95.31
REMARK 500 LEU B 769 -63.62 -120.87
REMARK 500 LYS C 41 117.44 -37.37
REMARK 500 LYS C 188 48.04 -140.62
REMARK 500 SER C 386 -40.81 -131.08
REMARK 500 SER C 460 -142.27 -152.01
REMARK 500 GLU C 490 -25.80 179.54
REMARK 500 ASN C 493 2.47 -69.87
REMARK 500 SER C 510 28.99 -75.99
REMARK 500 LYS C 511 177.78 62.30
REMARK 500 ALA C 512 128.43 166.36
REMARK 500 GLU C 689 -14.62 -162.03
REMARK 500 GLU C 690 -5.99 -48.99
REMARK 500 GLN C 691 -60.44 -108.33
REMARK 500 LEU C 769 -60.99 -125.10
REMARK 500 ALA X 117 -151.79 -126.78
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2027 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH B2007 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH B2027 DISTANCE = 7.39 ANGSTROMS
REMARK 525 HOH C2028 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH Z2007 DISTANCE = 5.82 ANGSTROMS
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUES 1-19 AND 671-684 FROM CBP80
REMARK 999 (CHAINS A,B,C) HAVE BEEN REMOVED BY TRYPSIN
REMARK 999 RESIDUES 1-21, 78 AND 121-156 FROM CBP20
REMARK 999 (CHAINS X,Y,Z) HAVE BEEN REMOVED BY TRYPSIN
DBREF 1H6K A 20 670 UNP Q09161 CB80_HUMAN 20 670
DBREF 1H6K A 685 790 UNP Q09161 CB80_HUMAN 685 790
DBREF 1H6K X 22 77 UNP P52298 CB20_HUMAN 22 77
DBREF 1H6K X 79 120 UNP P52298 CB20_HUMAN 79 120
DBREF 1H6K B 20 670 UNP Q09161 CB80_HUMAN 20 670
DBREF 1H6K B 685 790 UNP Q09161 CB80_HUMAN 685 790
DBREF 1H6K Y 22 77 UNP P52298 CB20_HUMAN 22 77
DBREF 1H6K Y 79 120 UNP P52298 CB20_HUMAN 79 120
DBREF 1H6K C 20 670 UNP Q09161 CB80_HUMAN 20 670
DBREF 1H6K C 685 790 UNP Q09161 CB80_HUMAN 685 790
DBREF 1H6K Z 22 77 UNP P52298 CB20_HUMAN 22 77
DBREF 1H6K Z 79 120 UNP P52298 CB20_HUMAN 79 120
SEQADV 1H6K SER A 479 UNP Q09161 ALA 479 ENGINEERED MUTATION
SEQADV 1H6K SER B 479 UNP Q09161 ALA 479 ENGINEERED MUTATION
SEQADV 1H6K SER C 479 UNP Q09161 ALA 479 ENGINEERED MUTATION
SEQRES 1 A 757 LYS THR SER ASP ALA ASN GLU THR GLU ASP HIS LEU GLU
SEQRES 2 A 757 SER LEU ILE CYS LYS VAL GLY GLU LYS SER ALA CYS SER
SEQRES 3 A 757 LEU GLU SER ASN LEU GLU GLY LEU ALA GLY VAL LEU GLU
SEQRES 4 A 757 ALA ASP LEU PRO ASN TYR LYS SER LYS ILE LEU ARG LEU
SEQRES 5 A 757 LEU CYS THR VAL ALA ARG LEU LEU PRO GLU LYS LEU THR
SEQRES 6 A 757 ILE TYR THR THR LEU VAL GLY LEU LEU ASN ALA ARG ASN
SEQRES 7 A 757 TYR ASN PHE GLY GLY GLU PHE VAL GLU ALA MET ILE ARG
SEQRES 8 A 757 GLN LEU LYS GLU SER LEU LYS ALA ASN ASN TYR ASN GLU
SEQRES 9 A 757 ALA VAL TYR LEU VAL ARG PHE LEU SER ASP LEU VAL ASN
SEQRES 10 A 757 CYS HIS VAL ILE ALA ALA PRO SER MET VAL ALA MET PHE
SEQRES 11 A 757 GLU ASN PHE VAL SER VAL THR GLN GLU GLU ASP VAL PRO
SEQRES 12 A 757 GLN VAL ARG ARG ASP TRP TYR VAL TYR ALA PHE LEU SER
SEQRES 13 A 757 SER LEU PRO TRP VAL GLY LYS GLU LEU TYR GLU LYS LYS
SEQRES 14 A 757 ASP ALA GLU MET ASP ARG ILE PHE ALA ASN THR GLU SER
SEQRES 15 A 757 TYR LEU LYS ARG ARG GLN LYS THR HIS VAL PRO MET LEU
SEQRES 16 A 757 GLN VAL TRP THR ALA ASP LYS PRO HIS PRO GLN GLU GLU
SEQRES 17 A 757 TYR LEU ASP CYS LEU TRP ALA GLN ILE GLN LYS LEU LYS
SEQRES 18 A 757 LYS ASP ARG TRP GLN GLU ARG HIS ILE LEU ARG PRO TYR
SEQRES 19 A 757 LEU ALA PHE ASP SER ILE LEU CYS GLU ALA LEU GLN HIS
SEQRES 20 A 757 ASN LEU PRO PRO PHE THR PRO PRO PRO HIS THR GLU ASP
SEQRES 21 A 757 SER VAL TYR PRO MET PRO ARG VAL ILE PHE ARG MET PHE
SEQRES 22 A 757 ASP TYR THR ASP ASP PRO GLU GLY PRO VAL MET PRO GLY
SEQRES 23 A 757 SER HIS SER VAL GLU ARG PHE VAL ILE GLU GLU ASN LEU
SEQRES 24 A 757 HIS CYS ILE ILE LYS SER HIS TRP LYS GLU ARG LYS THR
SEQRES 25 A 757 CYS ALA ALA GLN LEU VAL SER TYR PRO GLY LYS ASN LYS
SEQRES 26 A 757 ILE PRO LEU ASN TYR HIS ILE VAL GLU VAL ILE PHE ALA
SEQRES 27 A 757 GLU LEU PHE GLN LEU PRO ALA PRO PRO HIS ILE ASP VAL
SEQRES 28 A 757 MET TYR THR THR LEU LEU ILE GLU LEU CYS LYS LEU GLN
SEQRES 29 A 757 PRO GLY SER LEU PRO GLN VAL LEU ALA GLN ALA THR GLU
SEQRES 30 A 757 MET LEU TYR MET ARG LEU ASP THR MET ASN THR THR CYS
SEQRES 31 A 757 VAL ASP ARG PHE ILE ASN TRP PHE SER HIS HIS LEU SER
SEQRES 32 A 757 ASN PHE GLN PHE ARG TRP SER TRP GLU ASP TRP SER ASP
SEQRES 33 A 757 CYS LEU SER GLN ASP PRO GLU SER PRO LYS PRO LYS PHE
SEQRES 34 A 757 VAL ARG GLU VAL LEU GLU LYS CYS MET ARG LEU SER TYR
SEQRES 35 A 757 HIS GLN ARG ILE LEU ASP ILE VAL PRO PRO THR PHE SER
SEQRES 36 A 757 ALA LEU CYS PRO SER ASN PRO THR CYS ILE TYR LYS TYR
SEQRES 37 A 757 GLY ASP GLU SER SER ASN SER LEU PRO GLY HIS SER VAL
SEQRES 38 A 757 ALA LEU CYS LEU ALA VAL ALA PHE LYS SER LYS ALA THR
SEQRES 39 A 757 ASN ASP GLU ILE PHE SER ILE LEU LYS ASP VAL PRO ASN
SEQRES 40 A 757 PRO ASN GLN ASP ASP ASP ASP ASP GLU GLY PHE SER PHE
SEQRES 41 A 757 ASN PRO LEU LYS ILE GLU VAL PHE VAL GLN THR LEU LEU
SEQRES 42 A 757 HIS LEU ALA ALA LYS SER PHE SER HIS SER PHE SER ALA
SEQRES 43 A 757 LEU ALA LYS PHE HIS GLU VAL PHE LYS THR LEU ALA GLU
SEQRES 44 A 757 SER ASP GLU GLY LYS LEU HIS VAL LEU ARG VAL MET PHE
SEQRES 45 A 757 GLU VAL TRP ARG ASN HIS PRO GLN MET ILE ALA VAL LEU
SEQRES 46 A 757 VAL ASP LYS MET ILE ARG THR GLN ILE VAL ASP CYS ALA
SEQRES 47 A 757 ALA VAL ALA ASN TRP ILE PHE SER SER GLU LEU SER ARG
SEQRES 48 A 757 ASP PHE THR ARG LEU PHE VAL TRP GLU ILE LEU HIS SER
SEQRES 49 A 757 THR ILE ARG LYS MET ASN LYS HIS VAL LEU LYS ILE GLN
SEQRES 50 A 757 LYS GLU LEU GLU GLU ALA LYS GLU LYS LEU ALA ARG GLN
SEQRES 51 A 757 HIS ASP GLY VAL LEU GLU GLU GLN ILE GLU ARG LEU GLN
SEQRES 52 A 757 GLU LYS VAL GLU SER ALA GLN SER GLU GLN LYS ASN LEU
SEQRES 53 A 757 PHE LEU VAL ILE PHE GLN ARG PHE ILE MET ILE LEU THR
SEQRES 54 A 757 GLU HIS LEU VAL ARG CYS GLU THR ASP GLY THR SER VAL
SEQRES 55 A 757 LEU THR PRO TRP TYR LYS ASN CYS ILE GLU ARG LEU GLN
SEQRES 56 A 757 GLN ILE PHE LEU GLN HIS HIS GLN ILE ILE GLN GLN TYR
SEQRES 57 A 757 MET VAL THR LEU GLU ASN LEU LEU PHE THR ALA GLU LEU
SEQRES 58 A 757 ASP PRO HIS ILE LEU ALA VAL PHE GLN GLN PHE CYS ALA
SEQRES 59 A 757 LEU GLN ALA
SEQRES 1 B 757 LYS THR SER ASP ALA ASN GLU THR GLU ASP HIS LEU GLU
SEQRES 2 B 757 SER LEU ILE CYS LYS VAL GLY GLU LYS SER ALA CYS SER
SEQRES 3 B 757 LEU GLU SER ASN LEU GLU GLY LEU ALA GLY VAL LEU GLU
SEQRES 4 B 757 ALA ASP LEU PRO ASN TYR LYS SER LYS ILE LEU ARG LEU
SEQRES 5 B 757 LEU CYS THR VAL ALA ARG LEU LEU PRO GLU LYS LEU THR
SEQRES 6 B 757 ILE TYR THR THR LEU VAL GLY LEU LEU ASN ALA ARG ASN
SEQRES 7 B 757 TYR ASN PHE GLY GLY GLU PHE VAL GLU ALA MET ILE ARG
SEQRES 8 B 757 GLN LEU LYS GLU SER LEU LYS ALA ASN ASN TYR ASN GLU
SEQRES 9 B 757 ALA VAL TYR LEU VAL ARG PHE LEU SER ASP LEU VAL ASN
SEQRES 10 B 757 CYS HIS VAL ILE ALA ALA PRO SER MET VAL ALA MET PHE
SEQRES 11 B 757 GLU ASN PHE VAL SER VAL THR GLN GLU GLU ASP VAL PRO
SEQRES 12 B 757 GLN VAL ARG ARG ASP TRP TYR VAL TYR ALA PHE LEU SER
SEQRES 13 B 757 SER LEU PRO TRP VAL GLY LYS GLU LEU TYR GLU LYS LYS
SEQRES 14 B 757 ASP ALA GLU MET ASP ARG ILE PHE ALA ASN THR GLU SER
SEQRES 15 B 757 TYR LEU LYS ARG ARG GLN LYS THR HIS VAL PRO MET LEU
SEQRES 16 B 757 GLN VAL TRP THR ALA ASP LYS PRO HIS PRO GLN GLU GLU
SEQRES 17 B 757 TYR LEU ASP CYS LEU TRP ALA GLN ILE GLN LYS LEU LYS
SEQRES 18 B 757 LYS ASP ARG TRP GLN GLU ARG HIS ILE LEU ARG PRO TYR
SEQRES 19 B 757 LEU ALA PHE ASP SER ILE LEU CYS GLU ALA LEU GLN HIS
SEQRES 20 B 757 ASN LEU PRO PRO PHE THR PRO PRO PRO HIS THR GLU ASP
SEQRES 21 B 757 SER VAL TYR PRO MET PRO ARG VAL ILE PHE ARG MET PHE
SEQRES 22 B 757 ASP TYR THR ASP ASP PRO GLU GLY PRO VAL MET PRO GLY
SEQRES 23 B 757 SER HIS SER VAL GLU ARG PHE VAL ILE GLU GLU ASN LEU
SEQRES 24 B 757 HIS CYS ILE ILE LYS SER HIS TRP LYS GLU ARG LYS THR
SEQRES 25 B 757 CYS ALA ALA GLN LEU VAL SER TYR PRO GLY LYS ASN LYS
SEQRES 26 B 757 ILE PRO LEU ASN TYR HIS ILE VAL GLU VAL ILE PHE ALA
SEQRES 27 B 757 GLU LEU PHE GLN LEU PRO ALA PRO PRO HIS ILE ASP VAL
SEQRES 28 B 757 MET TYR THR THR LEU LEU ILE GLU LEU CYS LYS LEU GLN
SEQRES 29 B 757 PRO GLY SER LEU PRO GLN VAL LEU ALA GLN ALA THR GLU
SEQRES 30 B 757 MET LEU TYR MET ARG LEU ASP THR MET ASN THR THR CYS
SEQRES 31 B 757 VAL ASP ARG PHE ILE ASN TRP PHE SER HIS HIS LEU SER
SEQRES 32 B 757 ASN PHE GLN PHE ARG TRP SER TRP GLU ASP TRP SER ASP
SEQRES 33 B 757 CYS LEU SER GLN ASP PRO GLU SER PRO LYS PRO LYS PHE
SEQRES 34 B 757 VAL ARG GLU VAL LEU GLU LYS CYS MET ARG LEU SER TYR
SEQRES 35 B 757 HIS GLN ARG ILE LEU ASP ILE VAL PRO PRO THR PHE SER
SEQRES 36 B 757 ALA LEU CYS PRO SER ASN PRO THR CYS ILE TYR LYS TYR
SEQRES 37 B 757 GLY ASP GLU SER SER ASN SER LEU PRO GLY HIS SER VAL
SEQRES 38 B 757 ALA LEU CYS LEU ALA VAL ALA PHE LYS SER LYS ALA THR
SEQRES 39 B 757 ASN ASP GLU ILE PHE SER ILE LEU LYS ASP VAL PRO ASN
SEQRES 40 B 757 PRO ASN GLN ASP ASP ASP ASP ASP GLU GLY PHE SER PHE
SEQRES 41 B 757 ASN PRO LEU LYS ILE GLU VAL PHE VAL GLN THR LEU LEU
SEQRES 42 B 757 HIS LEU ALA ALA LYS SER PHE SER HIS SER PHE SER ALA
SEQRES 43 B 757 LEU ALA LYS PHE HIS GLU VAL PHE LYS THR LEU ALA GLU
SEQRES 44 B 757 SER ASP GLU GLY LYS LEU HIS VAL LEU ARG VAL MET PHE
SEQRES 45 B 757 GLU VAL TRP ARG ASN HIS PRO GLN MET ILE ALA VAL LEU
SEQRES 46 B 757 VAL ASP LYS MET ILE ARG THR GLN ILE VAL ASP CYS ALA
SEQRES 47 B 757 ALA VAL ALA ASN TRP ILE PHE SER SER GLU LEU SER ARG
SEQRES 48 B 757 ASP PHE THR ARG LEU PHE VAL TRP GLU ILE LEU HIS SER
SEQRES 49 B 757 THR ILE ARG LYS MET ASN LYS HIS VAL LEU LYS ILE GLN
SEQRES 50 B 757 LYS GLU LEU GLU GLU ALA LYS GLU LYS LEU ALA ARG GLN
SEQRES 51 B 757 HIS ASP GLY VAL LEU GLU GLU GLN ILE GLU ARG LEU GLN
SEQRES 52 B 757 GLU LYS VAL GLU SER ALA GLN SER GLU GLN LYS ASN LEU
SEQRES 53 B 757 PHE LEU VAL ILE PHE GLN ARG PHE ILE MET ILE LEU THR
SEQRES 54 B 757 GLU HIS LEU VAL ARG CYS GLU THR ASP GLY THR SER VAL
SEQRES 55 B 757 LEU THR PRO TRP TYR LYS ASN CYS ILE GLU ARG LEU GLN
SEQRES 56 B 757 GLN ILE PHE LEU GLN HIS HIS GLN ILE ILE GLN GLN TYR
SEQRES 57 B 757 MET VAL THR LEU GLU ASN LEU LEU PHE THR ALA GLU LEU
SEQRES 58 B 757 ASP PRO HIS ILE LEU ALA VAL PHE GLN GLN PHE CYS ALA
SEQRES 59 B 757 LEU GLN ALA
SEQRES 1 C 757 LYS THR SER ASP ALA ASN GLU THR GLU ASP HIS LEU GLU
SEQRES 2 C 757 SER LEU ILE CYS LYS VAL GLY GLU LYS SER ALA CYS SER
SEQRES 3 C 757 LEU GLU SER ASN LEU GLU GLY LEU ALA GLY VAL LEU GLU
SEQRES 4 C 757 ALA ASP LEU PRO ASN TYR LYS SER LYS ILE LEU ARG LEU
SEQRES 5 C 757 LEU CYS THR VAL ALA ARG LEU LEU PRO GLU LYS LEU THR
SEQRES 6 C 757 ILE TYR THR THR LEU VAL GLY LEU LEU ASN ALA ARG ASN
SEQRES 7 C 757 TYR ASN PHE GLY GLY GLU PHE VAL GLU ALA MET ILE ARG
SEQRES 8 C 757 GLN LEU LYS GLU SER LEU LYS ALA ASN ASN TYR ASN GLU
SEQRES 9 C 757 ALA VAL TYR LEU VAL ARG PHE LEU SER ASP LEU VAL ASN
SEQRES 10 C 757 CYS HIS VAL ILE ALA ALA PRO SER MET VAL ALA MET PHE
SEQRES 11 C 757 GLU ASN PHE VAL SER VAL THR GLN GLU GLU ASP VAL PRO
SEQRES 12 C 757 GLN VAL ARG ARG ASP TRP TYR VAL TYR ALA PHE LEU SER
SEQRES 13 C 757 SER LEU PRO TRP VAL GLY LYS GLU LEU TYR GLU LYS LYS
SEQRES 14 C 757 ASP ALA GLU MET ASP ARG ILE PHE ALA ASN THR GLU SER
SEQRES 15 C 757 TYR LEU LYS ARG ARG GLN LYS THR HIS VAL PRO MET LEU
SEQRES 16 C 757 GLN VAL TRP THR ALA ASP LYS PRO HIS PRO GLN GLU GLU
SEQRES 17 C 757 TYR LEU ASP CYS LEU TRP ALA GLN ILE GLN LYS LEU LYS
SEQRES 18 C 757 LYS ASP ARG TRP GLN GLU ARG HIS ILE LEU ARG PRO TYR
SEQRES 19 C 757 LEU ALA PHE ASP SER ILE LEU CYS GLU ALA LEU GLN HIS
SEQRES 20 C 757 ASN LEU PRO PRO PHE THR PRO PRO PRO HIS THR GLU ASP
SEQRES 21 C 757 SER VAL TYR PRO MET PRO ARG VAL ILE PHE ARG MET PHE
SEQRES 22 C 757 ASP TYR THR ASP ASP PRO GLU GLY PRO VAL MET PRO GLY
SEQRES 23 C 757 SER HIS SER VAL GLU ARG PHE VAL ILE GLU GLU ASN LEU
SEQRES 24 C 757 HIS CYS ILE ILE LYS SER HIS TRP LYS GLU ARG LYS THR
SEQRES 25 C 757 CYS ALA ALA GLN LEU VAL SER TYR PRO GLY LYS ASN LYS
SEQRES 26 C 757 ILE PRO LEU ASN TYR HIS ILE VAL GLU VAL ILE PHE ALA
SEQRES 27 C 757 GLU LEU PHE GLN LEU PRO ALA PRO PRO HIS ILE ASP VAL
SEQRES 28 C 757 MET TYR THR THR LEU LEU ILE GLU LEU CYS LYS LEU GLN
SEQRES 29 C 757 PRO GLY SER LEU PRO GLN VAL LEU ALA GLN ALA THR GLU
SEQRES 30 C 757 MET LEU TYR MET ARG LEU ASP THR MET ASN THR THR CYS
SEQRES 31 C 757 VAL ASP ARG PHE ILE ASN TRP PHE SER HIS HIS LEU SER
SEQRES 32 C 757 ASN PHE GLN PHE ARG TRP SER TRP GLU ASP TRP SER ASP
SEQRES 33 C 757 CYS LEU SER GLN ASP PRO GLU SER PRO LYS PRO LYS PHE
SEQRES 34 C 757 VAL ARG GLU VAL LEU GLU LYS CYS MET ARG LEU SER TYR
SEQRES 35 C 757 HIS GLN ARG ILE LEU ASP ILE VAL PRO PRO THR PHE SER
SEQRES 36 C 757 ALA LEU CYS PRO SER ASN PRO THR CYS ILE TYR LYS TYR
SEQRES 37 C 757 GLY ASP GLU SER SER ASN SER LEU PRO GLY HIS SER VAL
SEQRES 38 C 757 ALA LEU CYS LEU ALA VAL ALA PHE LYS SER LYS ALA THR
SEQRES 39 C 757 ASN ASP GLU ILE PHE SER ILE LEU LYS ASP VAL PRO ASN
SEQRES 40 C 757 PRO ASN GLN ASP ASP ASP ASP ASP GLU GLY PHE SER PHE
SEQRES 41 C 757 ASN PRO LEU LYS ILE GLU VAL PHE VAL GLN THR LEU LEU
SEQRES 42 C 757 HIS LEU ALA ALA LYS SER PHE SER HIS SER PHE SER ALA
SEQRES 43 C 757 LEU ALA LYS PHE HIS GLU VAL PHE LYS THR LEU ALA GLU
SEQRES 44 C 757 SER ASP GLU GLY LYS LEU HIS VAL LEU ARG VAL MET PHE
SEQRES 45 C 757 GLU VAL TRP ARG ASN HIS PRO GLN MET ILE ALA VAL LEU
SEQRES 46 C 757 VAL ASP LYS MET ILE ARG THR GLN ILE VAL ASP CYS ALA
SEQRES 47 C 757 ALA VAL ALA ASN TRP ILE PHE SER SER GLU LEU SER ARG
SEQRES 48 C 757 ASP PHE THR ARG LEU PHE VAL TRP GLU ILE LEU HIS SER
SEQRES 49 C 757 THR ILE ARG LYS MET ASN LYS HIS VAL LEU LYS ILE GLN
SEQRES 50 C 757 LYS GLU LEU GLU GLU ALA LYS GLU LYS LEU ALA ARG GLN
SEQRES 51 C 757 HIS ASP GLY VAL LEU GLU GLU GLN ILE GLU ARG LEU GLN
SEQRES 52 C 757 GLU LYS VAL GLU SER ALA GLN SER GLU GLN LYS ASN LEU
SEQRES 53 C 757 PHE LEU VAL ILE PHE GLN ARG PHE ILE MET ILE LEU THR
SEQRES 54 C 757 GLU HIS LEU VAL ARG CYS GLU THR ASP GLY THR SER VAL
SEQRES 55 C 757 LEU THR PRO TRP TYR LYS ASN CYS ILE GLU ARG LEU GLN
SEQRES 56 C 757 GLN ILE PHE LEU GLN HIS HIS GLN ILE ILE GLN GLN TYR
SEQRES 57 C 757 MET VAL THR LEU GLU ASN LEU LEU PHE THR ALA GLU LEU
SEQRES 58 C 757 ASP PRO HIS ILE LEU ALA VAL PHE GLN GLN PHE CYS ALA
SEQRES 59 C 757 LEU GLN ALA
SEQRES 1 X 98 ASP GLN HIS PHE ARG GLY ASP ASN GLU GLU GLN GLU LYS
SEQRES 2 X 98 LEU LEU LYS LYS SER CYS THR LEU TYR VAL GLY ASN LEU
SEQRES 3 X 98 SER PHE TYR THR THR GLU GLU GLN ILE TYR GLU LEU PHE
SEQRES 4 X 98 SER LYS SER GLY ASP ILE LYS LYS ILE ILE MET GLY LEU
SEQRES 5 X 98 ASP LYS MET LYS THR ALA CYS GLY PHE CYS PHE VAL GLU
SEQRES 6 X 98 TYR TYR SER ARG ALA ASP ALA GLU ASN ALA MET ARG TYR
SEQRES 7 X 98 ILE ASN GLY THR ARG LEU ASP ASP ARG ILE ILE ARG THR
SEQRES 8 X 98 ASP TRP ASP ALA GLY PHE LYS
SEQRES 1 Y 98 ASP GLN HIS PHE ARG GLY ASP ASN GLU GLU GLN GLU LYS
SEQRES 2 Y 98 LEU LEU LYS LYS SER CYS THR LEU TYR VAL GLY ASN LEU
SEQRES 3 Y 98 SER PHE TYR THR THR GLU GLU GLN ILE TYR GLU LEU PHE
SEQRES 4 Y 98 SER LYS SER GLY ASP ILE LYS LYS ILE ILE MET GLY LEU
SEQRES 5 Y 98 ASP LYS MET LYS THR ALA CYS GLY PHE CYS PHE VAL GLU
SEQRES 6 Y 98 TYR TYR SER ARG ALA ASP ALA GLU ASN ALA MET ARG TYR
SEQRES 7 Y 98 ILE ASN GLY THR ARG LEU ASP ASP ARG ILE ILE ARG THR
SEQRES 8 Y 98 ASP TRP ASP ALA GLY PHE LYS
SEQRES 1 Z 98 ASP GLN HIS PHE ARG GLY ASP ASN GLU GLU GLN GLU LYS
SEQRES 2 Z 98 LEU LEU LYS LYS SER CYS THR LEU TYR VAL GLY ASN LEU
SEQRES 3 Z 98 SER PHE TYR THR THR GLU GLU GLN ILE TYR GLU LEU PHE
SEQRES 4 Z 98 SER LYS SER GLY ASP ILE LYS LYS ILE ILE MET GLY LEU
SEQRES 5 Z 98 ASP LYS MET LYS THR ALA CYS GLY PHE CYS PHE VAL GLU
SEQRES 6 Z 98 TYR TYR SER ARG ALA ASP ALA GLU ASN ALA MET ARG TYR
SEQRES 7 Z 98 ILE ASN GLY THR ARG LEU ASP ASP ARG ILE ILE ARG THR
SEQRES 8 Z 98 ASP TRP ASP ALA GLY PHE LYS
FORMUL 7 HOH *1710(H2 O)
HELIX 1 1 THR A 27 VAL A 38 1 12
HELIX 2 2 SER A 45 ASP A 60 1 16
HELIX 3 3 ASP A 60 LYS A 65 1 6
HELIX 4 4 TYR A 64 LEU A 79 1 16
HELIX 5 5 LYS A 82 ASN A 97 1 16
HELIX 6 6 ASN A 97 ALA A 118 1 22
HELIX 7 7 ASN A 120 CYS A 137 1 18
HELIX 8 8 ALA A 141 VAL A 155 1 15
HELIX 9 9 THR A 156 GLU A 158 5 3
HELIX 10 10 PRO A 162 SER A 175 1 14
HELIX 11 11 SER A 176 GLY A 181 1 6
HELIX 12 12 VAL A 180 LYS A 188 1 9
HELIX 13 13 LYS A 188 ARG A 206 1 19
HELIX 14 14 HIS A 210 GLN A 215 1 6
HELIX 15 15 TYR A 228 ASP A 242 1 15
HELIX 16 16 ARG A 251 ASP A 257 5 7
HELIX 17 17 CYS A 261 GLN A 265 5 5
HELIX 18 18 ASP A 293 ASP A 297 5 5
HELIX 19 19 SER A 308 TRP A 326 1 19
HELIX 20 20 GLU A 328 SER A 338 1 11
HELIX 21 21 PRO A 346 PHE A 360 1 15
HELIX 22 22 ILE A 368 GLN A 383 1 16
HELIX 23 23 SER A 386 ARG A 401 1 16
HELIX 24 24 LEU A 402 THR A 404 5 3
HELIX 25 25 ASN A 406 ASN A 423 1 18
HELIX 26 26 SER A 429 LEU A 437 5 9
HELIX 27 27 SER A 443 LEU A 459 1 17
HELIX 28 28 TYR A 461 VAL A 469 1 9
HELIX 29 29 PRO A 470 CYS A 477 5 8
HELIX 30 30 GLY A 497 SER A 510 1 14
HELIX 31 31 THR A 513 LYS A 522 1 10
HELIX 32 32 ASN A 540 ALA A 555 1 16
HELIX 33 33 SER A 558 PHE A 569 1 12
HELIX 34 34 PHE A 569 ALA A 577 1 9
HELIX 35 35 SER A 579 ARG A 595 1 17
HELIX 36 36 HIS A 597 THR A 611 1 15
HELIX 37 37 ASP A 615 PHE A 624 1 10
HELIX 38 38 SER A 625 SER A 629 5 5
HELIX 39 39 ARG A 634 LYS A 665 1 32
HELIX 40 40 GLN A 691 GLY A 732 1 42
HELIX 41 41 THR A 737 HIS A 754 1 18
HELIX 42 42 HIS A 754 GLN A 759 1 6
HELIX 43 43 TYR A 761 LEU A 769 1 9
HELIX 44 44 ASP A 775 ALA A 787 1 13
HELIX 45 45 GLU B 26 VAL B 38 1 13
HELIX 46 46 SER B 45 ALA B 59 1 15
HELIX 47 47 ASP B 60 LYS B 65 1 6
HELIX 48 48 TYR B 64 LEU B 79 1 16
HELIX 49 49 LYS B 82 ASN B 97 1 16
HELIX 50 50 ASN B 97 ALA B 118 1 22
HELIX 51 51 ASN B 120 CYS B 137 1 18
HELIX 52 52 ALA B 141 VAL B 155 1 15
HELIX 53 53 THR B 156 GLU B 158 5 3
HELIX 54 54 PRO B 162 SER B 175 1 14
HELIX 55 55 SER B 176 GLY B 181 1 6
HELIX 56 56 VAL B 180 ASP B 189 1 10
HELIX 57 57 LYS B 188 ARG B 205 1 18
HELIX 58 58 HIS B 210 GLN B 215 1 6
HELIX 59 59 GLU B 227 ASP B 242 1 16
HELIX 60 60 ARG B 251 ASP B 257 5 7
HELIX 61 61 CYS B 261 GLN B 265 5 5
HELIX 62 62 ASP B 293 ASP B 297 5 5
HELIX 63 63 SER B 308 TRP B 326 1 19
HELIX 64 64 GLU B 328 SER B 338 1 11
HELIX 65 65 PRO B 346 PHE B 360 1 15
HELIX 66 66 ILE B 368 GLN B 383 1 16
HELIX 67 67 SER B 386 ARG B 401 1 16
HELIX 68 68 LEU B 402 THR B 404 5 3
HELIX 69 69 ASN B 406 ASN B 423 1 18
HELIX 70 70 SER B 429 GLN B 439 5 11
HELIX 71 71 SER B 443 LEU B 459 1 17
HELIX 72 72 TYR B 461 ASP B 467 1 7
HELIX 73 73 PRO B 470 CYS B 477 5 8
HELIX 74 74 GLY B 497 SER B 510 1 14
HELIX 75 75 THR B 513 LYS B 522 1 10
HELIX 76 76 ASN B 540 ALA B 555 1 16
HELIX 77 77 SER B 558 PHE B 569 1 12
HELIX 78 78 PHE B 569 ALA B 577 1 9
HELIX 79 79 SER B 579 ARG B 595 1 17
HELIX 80 80 HIS B 597 THR B 611 1 15
HELIX 81 81 ASP B 615 PHE B 624 1 10
HELIX 82 82 SER B 625 PHE B 632 5 8
HELIX 83 83 ARG B 634 GLU B 664 1 31
HELIX 84 84 GLU B 689 GLY B 732 1 44
HELIX 85 85 THR B 737 HIS B 755 1 19
HELIX 86 86 HIS B 754 GLN B 759 1 6
HELIX 87 87 TYR B 761 LEU B 769 1 9
HELIX 88 88 ASP B 775 LEU B 788 1 14
HELIX 89 89 GLU C 26 VAL C 38 1 13
HELIX 90 90 SER C 45 ALA C 59 1 15
HELIX 91 91 ASP C 60 LYS C 65 1 6
HELIX 92 92 TYR C 64 LEU C 79 1 16
HELIX 93 93 LYS C 82 ASN C 97 1 16
HELIX 94 94 ASN C 97 ALA C 118 1 22
HELIX 95 95 ASN C 120 CYS C 137 1 18
HELIX 96 96 ALA C 141 SER C 154 1 14
HELIX 97 97 VAL C 155 GLU C 158 5 4
HELIX 98 98 PRO C 162 SER C 175 1 14
HELIX 99 99 SER C 176 GLY C 181 1 6
HELIX 100 100 VAL C 180 ASP C 189 1 10
HELIX 101 101 LYS C 188 ARG C 206 1 19
HELIX 102 102 HIS C 210 GLN C 215 1 6
HELIX 103 103 GLU C 227 ASP C 242 1 16
HELIX 104 104 ARG C 251 ASP C 257 5 7
HELIX 105 105 CYS C 261 GLN C 265 5 5
HELIX 106 106 ASP C 293 ASP C 297 5 5
HELIX 107 107 SER C 308 TRP C 326 1 19
HELIX 108 108 GLU C 328 SER C 338 1 11
HELIX 109 109 PRO C 346 GLN C 361 1 16
HELIX 110 110 ILE C 368 GLN C 383 1 16
HELIX 111 111 SER C 386 ARG C 401 1 16
HELIX 112 112 LEU C 402 THR C 404 5 3
HELIX 113 113 ASN C 406 ASN C 423 1 18
HELIX 114 114 SER C 429 LEU C 437 5 9
HELIX 115 115 SER C 443 LEU C 459 1 17
HELIX 116 116 TYR C 461 VAL C 469 1 9
HELIX 117 117 PRO C 470 CYS C 477 5 8
HELIX 118 118 GLY C 497 SER C 510 1 14
HELIX 119 119 THR C 513 ASP C 523 1 11
HELIX 120 120 ASN C 540 ALA C 555 1 16
HELIX 121 121 SER C 558 PHE C 569 1 12
HELIX 122 122 PHE C 569 ALA C 577 1 9
HELIX 123 123 SER C 579 ARG C 595 1 17
HELIX 124 124 HIS C 597 THR C 611 1 15
HELIX 125 125 ASP C 615 PHE C 624 1 10
HELIX 126 126 SER C 625 SER C 629 5 5
HELIX 127 127 ARG C 634 GLU C 664 1 31
HELIX 128 128 GLN C 691 ASP C 731 1 41
HELIX 129 129 THR C 737 HIS C 754 1 18
HELIX 130 130 HIS C 754 GLN C 759 1 6
HELIX 131 131 TYR C 761 LEU C 769 1 9
HELIX 132 132 ASP C 775 ALA C 787 1 13
HELIX 133 133 THR X 52 SER X 61 1 10
HELIX 134 134 LYS X 62 GLY X 64 5 3
HELIX 135 135 SER X 90 ILE X 101 1 12
HELIX 136 136 THR Y 52 SER Y 61 1 10
HELIX 137 137 LYS Y 62 GLY Y 64 5 3
HELIX 138 138 SER Y 90 ILE Y 101 1 12
HELIX 139 139 THR Z 52 SER Z 61 1 10
HELIX 140 140 LYS Z 62 GLY Z 64 5 3
HELIX 141 141 SER Z 90 ILE Z 101 1 12
SHEET 1 AA 2 GLU A 226 GLU A 227 0
SHEET 2 AA 2 VAL A 287 ILE A 288 -1 O ILE A 288 N GLU A 226
SHEET 1 XA 4 ILE X 66 MET X 71 0
SHEET 2 XA 4 CYS X 84 TYR X 88 -1 O PHE X 85 N ILE X 70
SHEET 3 XA 4 THR X 41 GLY X 45 -1 O LEU X 42 N VAL X 86
SHEET 4 XA 4 ARG X 112 TRP X 115 -1 O ARG X 112 N GLY X 45
SHEET 1 XB 2 ARG X 105 LEU X 106 0
SHEET 2 XB 2 ARG X 109 ILE X 110 -1 O ARG X 109 N LEU X 106
SHEET 1 YA 4 ILE Y 66 MET Y 71 0
SHEET 2 YA 4 CYS Y 84 TYR Y 88 -1 O PHE Y 85 N ILE Y 70
SHEET 3 YA 4 THR Y 41 GLY Y 45 -1 O LEU Y 42 N VAL Y 86
SHEET 4 YA 4 ARG Y 112 TRP Y 115 -1 O ARG Y 112 N GLY Y 45
SHEET 1 YB 2 ARG Y 105 LEU Y 106 0
SHEET 2 YB 2 ARG Y 109 ILE Y 110 -1 O ARG Y 109 N LEU Y 106
SHEET 1 ZA 4 ILE Z 66 MET Z 71 0
SHEET 2 ZA 4 CYS Z 84 TYR Z 88 -1 O PHE Z 85 N ILE Z 70
SHEET 3 ZA 4 THR Z 41 GLY Z 45 -1 O LEU Z 42 N VAL Z 86
SHEET 4 ZA 4 ARG Z 112 TRP Z 115 -1 O ARG Z 112 N GLY Z 45
SHEET 1 ZB 2 ARG Z 105 LEU Z 106 0
SHEET 2 ZB 2 ARG Z 109 ILE Z 110 -1 O ARG Z 109 N LEU Z 106
CISPEP 1 LYS A 221 PRO A 222 0 -1.18
CISPEP 2 LEU A 362 PRO A 363 0 -0.13
CISPEP 3 LYS B 221 PRO B 222 0 -1.68
CISPEP 4 LEU B 362 PRO B 363 0 -2.27
CISPEP 5 LYS C 221 PRO C 222 0 -1.31
CISPEP 6 LEU C 362 PRO C 363 0 1.99
CRYST1 75.527 161.480 303.291 90.00 90.00 90.00 P 21 21 21 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 0.013240 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006193 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003297 0.00000
MTRIX1 1 0.999969 -0.004966 0.006010 25.14500 1
MTRIX2 1 -0.007794 -0.654022 0.756435 73.82900 1
MTRIX3 1 0.000174 -0.756459 -0.654041 39.57200 1
MTRIX1 2 0.999969 -0.004966 0.006010 25.14500 1
MTRIX2 2 -0.007794 -0.654022 0.756435 73.82900 1
MTRIX3 2 0.000174 -0.756459 -0.654041 39.57200 1
MTRIX1 3 0.999927 -0.006696 0.010008 12.82400 1
MTRIX2 3 -0.006708 0.380447 0.924778 25.16800 1
MTRIX3 3 -0.010000 -0.924778 0.380374 46.25900 1
MTRIX1 4 0.999927 -0.006696 0.010008 12.82400 1
MTRIX2 4 -0.006708 0.380447 0.924778 25.16800 1
MTRIX3 4 -0.010000 -0.924778 0.380374 46.25900 1
(ATOM LINES ARE NOT SHOWN.)
END
