HEADER HYDROLASE 05-DEC-06 2O4X
TITLE CRYSTAL STRUCTURE OF HUMAN P100 TUDOR DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: STAPHYLOCOCCAL NUCLEASE DOMAIN-CONTAINING PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 654-870;
COMPND 5 SYNONYM: P100 CO-ACTIVATOR, 100 KDA COACTIVATOR, EBNA2 COACTIVATOR
COMPND 6 P100;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: STAPHYLOCOCCAL NUCLEASE DOMAIN-CONTAINING PROTEIN 1;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: RESIDUES 680-795;
COMPND 12 SYNONYM: P100 CO-ACTIVATOR, 100 KDA COACTIVATOR, EBNA2 COACTIVATOR
COMPND 13 P100;
COMPND 14 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: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX6P-1;
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_STRAIN: BL21;
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PGEX6P-1
KEYWDS OB FOLD, BETA BARREL, AROMATIC CAGE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.SHAW,M.ZHAO,C.CHENG,H.XU,J.YANG,O.SILVENNOINEN,Z.RAO,B.C.WANG,
AUTHOR 2 Z.J.LIU
REVDAT 3 27-DEC-23 2O4X 1 SEQADV
REVDAT 2 24-FEB-09 2O4X 1 VERSN
REVDAT 1 13-FEB-07 2O4X 0
JRNL AUTH N.SHAW,M.ZHAO,C.CHENG,H.XU,J.YANG,O.SILVENNOINEN,Z.RAO,
JRNL AUTH 2 B.C.WANG,Z.J.LIU
JRNL TITL CRYSTAL STRUCTURE OF HUMAN P100 TUDOR DOMAIN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 44.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 29102
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) : 0.234
REMARK 3 R VALUE (WORKING SET) : 0.233
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.500
REMARK 3 FREE R VALUE TEST SET COUNT : 1701
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) : 2060
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2950
REMARK 3 BIN FREE R VALUE SET COUNT : 126
REMARK 3 BIN FREE R VALUE : 0.3160
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2436
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 156
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.33
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.65000
REMARK 3 B22 (A**2) : 0.84000
REMARK 3 B33 (A**2) : -0.19000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.177
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.152
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.109
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.794
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.929
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.923
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2493 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3381 ; 1.080 ; 1.952
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 301 ; 5.386 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 125 ;34.123 ;23.520
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 414 ;13.110 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 21 ;10.898 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 368 ; 0.073 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1933 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1062 ; 0.219 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1708 ; 0.319 ; 0.500
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 243 ; 0.177 ; 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): 29 ; 0.167 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 12 ; 0.122 ; 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): 1572 ; 1.159 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2465 ; 1.837 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1049 ; 1.128 ; 2.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 916 ; 1.728 ; 3.000
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 : 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2O4X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-DEC-06.
REMARK 100 THE DEPOSITION ID IS D_1000040691.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-JUN-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : SI CHANNEL 220
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000, XFIT
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29102
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 44.240
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07800
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) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.40000
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: PT-SAS
REMARK 200 SOFTWARE USED: XFIT
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0 MICROLITER DROPS CONTAINING EQUAL
REMARK 280 VOLUMES OF PROTEIN CONCENTRATE (10.0MG/ML), RESERVOIR SOLUTION
REMARK 280 CONTAING 20% PEG 8000, 100.0MM PHOSPHATE, 0.1M HEPES PH 4.2 ,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K
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 24.96550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 47.63950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.70650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 47.63950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.96550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 46.70650
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 VAL B 699
REMARK 465 GLU B 700
REMARK 465 GLY B 701
REMARK 465 SER B 702
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 683 CD GLU A 683 OE2 0.089
REMARK 500 GLU B 683 CD GLU B 683 OE2 0.082
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLU A 726 -117.80 -105.92
REMARK 500 SER A 822 38.29 36.86
REMARK 500 ASN A 866 -105.05 48.43
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2O4X A 654 870 UNP Q7KZF4 SND1_HUMAN 679 895
DBREF 2O4X B 680 770 UNP Q7KZF4 SND1_HUMAN 705 795
SEQADV 2O4X PHE A 682 UNP Q7KZF4 LEU 707 CONFLICT
SEQADV 2O4X PHE B 682 UNP Q7KZF4 LEU 707 CONFLICT
SEQRES 1 A 217 SER ALA SER TYR LYS PRO VAL PHE VAL THR GLU ILE THR
SEQRES 2 A 217 ASP ASP LEU HIS PHE TYR VAL GLN ASP VAL GLU THR GLY
SEQRES 3 A 217 THR GLN PHE GLU LYS LEU MET GLU ASN MET ARG ASN ASP
SEQRES 4 A 217 ILE ALA SER HIS PRO PRO VAL GLU GLY SER TYR ALA PRO
SEQRES 5 A 217 ARG ARG GLY GLU PHE CYS ILE ALA LYS PHE VAL ASP GLY
SEQRES 6 A 217 GLU TRP TYR ARG ALA ARG VAL GLU LYS VAL GLU SER PRO
SEQRES 7 A 217 ALA LYS ILE HIS VAL PHE TYR ILE ASP TYR GLY ASN ARG
SEQRES 8 A 217 GLU VAL LEU PRO SER THR ARG LEU GLY THR LEU SER PRO
SEQRES 9 A 217 ALA PHE SER THR ARG VAL LEU PRO ALA GLN ALA THR GLU
SEQRES 10 A 217 TYR ALA PHE ALA PHE ILE GLN VAL PRO GLN ASP ASP ASP
SEQRES 11 A 217 ALA ARG THR ASP ALA VAL ASP SER VAL VAL ARG ASP ILE
SEQRES 12 A 217 GLN ASN THR GLN CYS LEU LEU ASN VAL GLU HIS LEU SER
SEQRES 13 A 217 ALA GLY CYS PRO HIS VAL THR LEU GLN PHE ALA ASP SER
SEQRES 14 A 217 LYS GLY ASP VAL GLY LEU GLY LEU VAL LYS GLU GLY LEU
SEQRES 15 A 217 VAL MET VAL GLU VAL ARG LYS GLU LYS GLN PHE GLN LYS
SEQRES 16 A 217 VAL ILE THR GLU TYR LEU ASN ALA GLN GLU SER ALA LYS
SEQRES 17 A 217 SER ALA ARG LEU ASN LEU TRP ARG TYR
SEQRES 1 B 91 THR GLN PHE GLU LYS LEU MET GLU ASN MET ARG ASN ASP
SEQRES 2 B 91 ILE ALA SER HIS PRO PRO VAL GLU GLY SER TYR ALA PRO
SEQRES 3 B 91 ARG ARG GLY GLU PHE CYS ILE ALA LYS PHE VAL ASP GLY
SEQRES 4 B 91 GLU TRP TYR ARG ALA ARG VAL GLU LYS VAL GLU SER PRO
SEQRES 5 B 91 ALA LYS ILE HIS VAL PHE TYR ILE ASP TYR GLY ASN ARG
SEQRES 6 B 91 GLU VAL LEU PRO SER THR ARG LEU GLY THR LEU SER PRO
SEQRES 7 B 91 ALA PHE SER THR ARG VAL LEU PRO ALA GLN ALA THR GLU
FORMUL 3 HOH *156(H2 O)
HELIX 1 1 THR A 678 HIS A 696 1 19
HELIX 2 2 PRO A 748 THR A 750 5 3
HELIX 3 3 SER A 756 SER A 760 5 5
HELIX 4 4 ASP A 781 GLN A 797 1 17
HELIX 5 5 ASP A 825 GLU A 833 1 9
HELIX 6 6 GLU A 843 GLN A 845 5 3
HELIX 7 7 PHE A 846 ALA A 863 1 18
HELIX 8 8 LEU A 865 ARG A 869 5 5
HELIX 9 9 THR B 680 HIS B 696 1 17
HELIX 10 10 PRO B 748 THR B 750 5 3
HELIX 11 11 SER B 756 SER B 760 5 5
SHEET 1 A 6 LYS A 658 ILE A 665 0
SHEET 2 A 6 HIS A 670 ASP A 675 -1 O GLN A 674 N PHE A 661
SHEET 3 A 6 THR A 769 PHE A 773 -1 O TYR A 771 N PHE A 671
SHEET 4 A 6 HIS A 814 GLN A 818 1 O VAL A 815 N ALA A 772
SHEET 5 A 6 THR A 799 HIS A 807 -1 N LEU A 802 O GLN A 818
SHEET 6 A 6 LYS A 658 ILE A 665 -1 N VAL A 662 O THR A 799
SHEET 1 B 5 ARG A 744 LEU A 747 0
SHEET 2 B 5 LYS A 733 TYR A 738 -1 N VAL A 736 O GLU A 745
SHEET 3 B 5 TRP A 720 SER A 730 -1 N LYS A 727 O HIS A 735
SHEET 4 B 5 PHE A 710 LYS A 714 -1 N CYS A 711 O ALA A 723
SHEET 5 B 5 LEU A 752 GLY A 753 -1 O GLY A 753 N ILE A 712
SHEET 1 C 2 ILE A 776 GLN A 777 0
SHEET 2 C 2 MET A 837 VAL A 838 -1 O MET A 837 N GLN A 777
SHEET 1 D 5 ARG B 744 LEU B 747 0
SHEET 2 D 5 LYS B 733 TYR B 738 -1 N VAL B 736 O GLU B 745
SHEET 3 D 5 TRP B 720 SER B 730 -1 N GLU B 726 O HIS B 735
SHEET 4 D 5 PHE B 710 LYS B 714 -1 N ALA B 713 O TYR B 721
SHEET 5 D 5 LEU B 752 GLY B 753 -1 O GLY B 753 N ILE B 712
CISPEP 1 GLU A 700 GLY A 701 0 -2.68
CRYST1 49.931 93.413 95.279 90.00 90.00 90.00 P 21 21 21 4
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 0.020028 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010705 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010495 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
