HEADER CELL CYCLE 19-JUN-19 6S1R
TITLE STRUCTURE OF FISSION YEAST MIS16 BOUND TO HISTONE H4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE ACETYLTRANSFERASE TYPE B SUBUNIT 2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: KINETOCHORE PROTEIN MIS16;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: HISTONE H4;
COMPND 8 CHAIN: B;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SCHIZOSACCHAROMYCES POMBE;
SOURCE 3 ORGANISM_COMMON: FISSION YEAST;
SOURCE 4 ORGANISM_TAXID: 4896;
SOURCE 5 GENE: MIS16, HAT2, SPCC1672.10;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 ORGANISM_SCIENTIFIC: SCHIZOSACCHAROMYCES POMBE;
SOURCE 12 ORGANISM_COMMON: FISSION YEAST;
SOURCE 13 ORGANISM_TAXID: 4896
KEYWDS CENTROMERE MITOSIS WD40 HISTONE CHAPERONE, CELL CYCLE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.LEFEVRE,M.KORNTNER-VETTER,M.R.SINGLETON
REVDAT 3 24-JAN-24 6S1R 1 REMARK
REVDAT 2 14-AUG-19 6S1R 1 JRNL
REVDAT 1 07-AUG-19 6S1R 0
JRNL AUTH M.KORNTNER-VETTER,S.LEFEVRE,X.W.HU,R.GEORGE,M.R.SINGLETON
JRNL TITL SUBUNIT INTERACTIONS AND ARRANGEMENTS IN THE FISSION YEAST
JRNL TITL 2 MIS16-MIS18-MIS19 COMPLEX.
JRNL REF LIFE SCI ALLIANCE V. 2 2019
JRNL REFN ESSN 2575-1077
JRNL PMID 31371524
JRNL DOI 10.26508/LSA.201900408
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.15_3459: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.22
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 3 NUMBER OF REFLECTIONS : 39872
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.820
REMARK 3 FREE R VALUE TEST SET COUNT : 1921
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 46.2369 - 4.3372 1.00 2992 147 0.1692 0.1982
REMARK 3 2 4.3372 - 3.4429 0.99 2847 145 0.1633 0.2044
REMARK 3 3 3.4429 - 3.0078 1.00 2812 152 0.1796 0.2135
REMARK 3 4 3.0078 - 2.7329 1.00 2804 151 0.1986 0.2419
REMARK 3 5 2.7329 - 2.5370 1.00 2786 162 0.1999 0.2507
REMARK 3 6 2.5370 - 2.3874 1.00 2775 139 0.2073 0.2348
REMARK 3 7 2.3874 - 2.2679 0.97 2695 143 0.2250 0.3023
REMARK 3 8 2.2679 - 2.1691 0.98 2739 120 0.2743 0.3030
REMARK 3 9 2.1691 - 2.0856 1.00 2801 123 0.2343 0.2628
REMARK 3 10 2.0856 - 2.0137 1.00 2760 145 0.2400 0.2685
REMARK 3 11 2.0137 - 1.9507 1.00 2719 151 0.2748 0.3113
REMARK 3 12 1.9507 - 1.8949 0.77 2132 103 0.4078 0.4988
REMARK 3 13 1.8949 - 1.8451 0.91 2505 118 0.4068 0.4188
REMARK 3 14 1.8451 - 1.8000 0.94 2584 122 0.3558 0.3909
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.290
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.500
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 3304
REMARK 3 ANGLE : 0.909 4508
REMARK 3 CHIRALITY : 0.061 498
REMARK 3 PLANARITY : 0.005 591
REMARK 3 DIHEDRAL : 3.571 1963
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6S1R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-JUN-19.
REMARK 100 THE DEPOSITION ID IS D_1292103004.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-FEB-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8726
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DIALS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39885
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 46.220
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.3600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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
REMARK 200 STARTING MODEL: 6S1L
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05 M LISO4, 0.8 M NAH2PO4, 1.2 M
REMARK 280 K2HPO4, 0.1 M CAPS PH 9.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
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 28.69500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 48.75500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.99000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 48.75500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.69500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.99000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 1
REMARK 465 SER A 2
REMARK 465 GLU A 3
REMARK 465 GLU A 4
REMARK 465 VAL A 5
REMARK 465 VAL A 6
REMARK 465 GLN A 7
REMARK 465 ASP A 8
REMARK 465 ALA A 9
REMARK 465 PRO A 10
REMARK 465 LEU A 11
REMARK 465 THR A 103
REMARK 465 THR A 104
REMARK 465 GLU A 105
REMARK 465 PHE A 106
REMARK 465 THR A 107
REMARK 465 PRO A 108
REMARK 465 SER A 109
REMARK 465 THR A 110
REMARK 465 ILE A 111
REMARK 465 ARG A 112
REMARK 465 ARG A 113
REMARK 465 ALA A 114
REMARK 465 GLN A 115
REMARK 465 ALA A 116
REMARK 465 THR A 117
REMARK 465 GLU A 270
REMARK 465 GLU A 271
REMARK 465 ASP A 420
REMARK 465 HIS A 421
REMARK 465 VAL A 422
REMARK 465 GLN A 423
REMARK 465 VAL A 424
REMARK 465 SER A 425
REMARK 465 PRO A 426
REMARK 465 ARG A 427
REMARK 465 ASP A 428
REMARK 465 LEU A 429
REMARK 465 GLU A 430
REMARK 465 GLY B 14
REMARK 465 GLY B 15
REMARK 465 ALA B 16
REMARK 465 LYS B 17
REMARK 465 ARG B 18
REMARK 465 HIS B 19
REMARK 465 ARG B 20
REMARK 465 LYS B 21
REMARK 465 ILE B 22
REMARK 465 LEU B 23
REMARK 465 ARG B 24
REMARK 465 ASP B 25
REMARK 465 ASN B 26
REMARK 465 ILE B 27
REMARK 465 GLN B 28
REMARK 465 GLY B 29
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 ND2 ASN A 393 O HOH A 501 1.84
REMARK 500 O HOH A 725 O HOH A 740 1.85
REMARK 500 O HOH A 641 O HOH A 735 2.00
REMARK 500 O HOH A 576 O HOH A 727 2.00
REMARK 500 ND1 HIS A 80 O HOH A 502 2.00
REMARK 500 O HOH A 667 O HOH A 675 2.01
REMARK 500 OE1 GLU A 248 O HOH A 503 2.02
REMARK 500 O HOH A 628 O HOH A 681 2.02
REMARK 500 O HOH A 513 O HOH A 727 2.03
REMARK 500 OE2 GLU A 29 O HOH A 504 2.17
REMARK 500 OE1 GLU A 171 O HOH A 505 2.17
REMARK 500 O HOH A 739 O HOH A 750 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 511 O HOH A 649 4555 1.60
REMARK 500 NZ LYS A 223 OD1 ASN A 393 4545 2.07
REMARK 500 O HOH A 711 O HOH A 733 2555 2.13
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 ASN A 84 -74.99 74.11
REMARK 500 GLN A 215 -56.76 -9.77
REMARK 500 LYS A 304 9.31 81.87
REMARK 500 ASP A 404 33.51 -95.73
REMARK 500 THR B 31 -159.14 -85.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 THR A 214 GLN A 215 145.04
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 A 751 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH A 752 DISTANCE = 6.25 ANGSTROMS
REMARK 525 HOH A 753 DISTANCE = 6.84 ANGSTROMS
DBREF 6S1R A 2 430 UNP O94244 HAT2_SCHPO 2 430
DBREF 6S1R B 14 44 UNP P09322 H4_SCHPO 14 44
SEQADV 6S1R GLY A 1 UNP O94244 EXPRESSION TAG
SEQRES 1 A 430 GLY SER GLU GLU VAL VAL GLN ASP ALA PRO LEU GLU ASN
SEQRES 2 A 430 ASN GLU LEU ASN ALA GLU ILE ASP LEU GLN LYS THR ILE
SEQRES 3 A 430 GLN GLU GLU TYR LYS LEU TRP LYS GLN ASN VAL PRO PHE
SEQRES 4 A 430 LEU TYR ASP LEU VAL ILE THR HIS ALA LEU GLU TRP PRO
SEQRES 5 A 430 SER LEU THR ILE GLN TRP LEU PRO ASP LYS LYS THR ILE
SEQRES 6 A 430 PRO GLY THR ASP TYR SER ILE GLN ARG LEU ILE LEU GLY
SEQRES 7 A 430 THR HIS THR SER GLY ASN ASP GLN ASN TYR LEU GLN ILE
SEQRES 8 A 430 ALA SER VAL GLN LEU PRO ASN PHE ASP GLU ASP THR THR
SEQRES 9 A 430 GLU PHE THR PRO SER THR ILE ARG ARG ALA GLN ALA THR
SEQRES 10 A 430 GLY SER TYR THR ILE GLU ILE SER GLN LYS ILE PRO HIS
SEQRES 11 A 430 ASP GLY ASP VAL ASN ARG ALA ARG TYR MET PRO GLN LYS
SEQRES 12 A 430 PRO GLU ILE ILE ALA THR MET GLY GLU GLY GLY ASN ALA
SEQRES 13 A 430 TYR ILE PHE ASP THR THR CYS HIS ASP ALA LEU THR THR
SEQRES 14 A 430 GLY GLU ALA LEU PRO GLN ALA VAL LEU LYS GLY HIS THR
SEQRES 15 A 430 ALA GLU GLY PHE GLY LEU CYS TRP ASN PRO ASN LEU PRO
SEQRES 16 A 430 GLY ASN LEU ALA THR GLY ALA GLU ASP GLN VAL ILE CYS
SEQRES 17 A 430 LEU TRP ASP VAL GLN THR GLN SER PHE THR SER SER GLU
SEQRES 18 A 430 THR LYS VAL ILE SER PRO ILE ALA LYS TYR HIS ARG HIS
SEQRES 19 A 430 THR ASP ILE VAL ASN ASP VAL GLN PHE HIS PRO GLN HIS
SEQRES 20 A 430 GLU ALA LEU LEU ALA SER VAL SER ASP ASP CYS THR LEU
SEQRES 21 A 430 GLN ILE HIS ASP THR ARG LEU ASN PRO GLU GLU GLU ALA
SEQRES 22 A 430 PRO LYS VAL ILE GLN ALA HIS SER LYS ALA ILE ASN ALA
SEQRES 23 A 430 VAL ALA ILE ASN PRO PHE ASN ASP TYR LEU LEU ALA THR
SEQRES 24 A 430 ALA SER ALA ASP LYS THR VAL ALA LEU TRP ASP LEU ARG
SEQRES 25 A 430 ASN PRO TYR GLN ARG LEU HIS THR LEU GLU GLY HIS GLU
SEQRES 26 A 430 ASP GLU VAL TYR GLY LEU GLU TRP SER PRO HIS ASP GLU
SEQRES 27 A 430 PRO ILE LEU ALA SER SER SER THR ASP ARG ARG VAL CYS
SEQRES 28 A 430 ILE TRP ASP LEU GLU LYS ILE GLY GLU GLU GLN THR PRO
SEQRES 29 A 430 GLU ASP ALA GLU ASP GLY SER PRO GLU LEU LEU PHE MET
SEQRES 30 A 430 HIS GLY GLY HIS THR ASN ARG ILE SER GLU PHE SER TRP
SEQRES 31 A 430 CYS PRO ASN GLU ARG TRP VAL VAL GLY SER LEU ALA ASP
SEQRES 32 A 430 ASP ASN ILE LEU GLN ILE TRP SER PRO SER ARG VAL ILE
SEQRES 33 A 430 TRP GLY ARG ASP HIS VAL GLN VAL SER PRO ARG ASP LEU
SEQRES 34 A 430 GLU
SEQRES 1 B 31 GLY GLY ALA LYS ARG HIS ARG LYS ILE LEU ARG ASP ASN
SEQRES 2 B 31 ILE GLN GLY ILE THR LYS PRO ALA ILE ARG ARG LEU ALA
SEQRES 3 B 31 ARG ARG GLY GLY VAL
FORMUL 3 HOH *256(H2 O)
HELIX 1 AA1 GLU A 12 LEU A 40 1 29
HELIX 2 AA2 GLU A 152 GLY A 154 5 3
HELIX 3 AA3 GLN A 213 PHE A 217 5 5
HELIX 4 AA4 GLU A 356 ILE A 358 5 3
HELIX 5 AA5 THR A 363 GLY A 370 1 8
HELIX 6 AA6 SER A 413 GLY A 418 1 6
HELIX 7 AA7 THR B 31 ARG B 41 1 11
SHEET 1 AA1 4 TYR A 41 ALA A 48 0
SHEET 2 AA1 4 ILE A 406 PRO A 412 -1 O ILE A 409 N ILE A 45
SHEET 3 AA1 4 VAL A 398 ALA A 402 -1 N SER A 400 O GLN A 408
SHEET 4 AA1 4 ILE A 385 TRP A 390 -1 N SER A 389 O GLY A 399
SHEET 1 AA2 4 ILE A 56 THR A 64 0
SHEET 2 AA2 4 TYR A 70 LEU A 77 -1 O ILE A 76 N GLN A 57
SHEET 3 AA2 4 ASN A 87 PRO A 97 -1 O GLN A 90 N LEU A 77
SHEET 4 AA2 4 ILE A 122 HIS A 130 -1 O GLU A 123 N SER A 93
SHEET 1 AA3 5 ARG A 136 MET A 140 0
SHEET 2 AA3 5 LYS A 143 MET A 150 -1 O ILE A 146 N MET A 140
SHEET 3 AA3 5 ALA A 156 ASP A 160 -1 O PHE A 159 N ILE A 147
SHEET 4 AA3 5 ALA A 176 LEU A 178 -1 O LEU A 178 N ALA A 156
SHEET 5 AA3 5 LYS A 223 ILE A 225 1 O ILE A 225 N VAL A 177
SHEET 1 AA4 4 GLY A 185 TRP A 190 0
SHEET 2 AA4 4 ASN A 197 ALA A 202 -1 O ALA A 199 N CYS A 189
SHEET 3 AA4 4 ILE A 207 ASP A 211 -1 O TRP A 210 N LEU A 198
SHEET 4 AA4 4 ALA A 229 TYR A 231 -1 O ALA A 229 N LEU A 209
SHEET 1 AA5 4 VAL A 238 PHE A 243 0
SHEET 2 AA5 4 LEU A 250 SER A 255 -1 O ALA A 252 N GLN A 242
SHEET 3 AA5 4 LEU A 260 ASP A 264 -1 O HIS A 263 N LEU A 251
SHEET 4 AA5 4 LYS A 275 ILE A 277 -1 O ILE A 277 N LEU A 260
SHEET 1 AA6 4 ILE A 284 ILE A 289 0
SHEET 2 AA6 4 LEU A 296 SER A 301 -1 O ALA A 298 N ALA A 288
SHEET 3 AA6 4 VAL A 306 ASP A 310 -1 O TRP A 309 N LEU A 297
SHEET 4 AA6 4 ARG A 317 LEU A 321 -1 O LEU A 321 N VAL A 306
SHEET 1 AA7 4 VAL A 328 TRP A 333 0
SHEET 2 AA7 4 ILE A 340 SER A 345 -1 O SER A 344 N TYR A 329
SHEET 3 AA7 4 VAL A 350 ASP A 354 -1 O TRP A 353 N LEU A 341
SHEET 4 AA7 4 LEU A 374 HIS A 378 -1 O HIS A 378 N VAL A 350
CRYST1 57.390 77.980 97.510 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 0.017425 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012824 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010255 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
