HEADER TRANSCRIPTION 20-SEP-12 4BB7
TITLE CRYSTAL STRUCTURE OF THE YEAST RSC2 BAH DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHROMATIN STRUCTURE-REMODELING COMPLEX SUBUNIT RSC2;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: DOMAIN, RESIDUES 401-641;
COMPND 5 SYNONYM: RSC COMPLEX SUBUNIT RSC2, REMODEL THE STRUCTURE OF CHROMATIN
COMPND 6 COMPLEX SUBUNIT 2;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: ROSETTA2;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PTWO-E
KEYWDS TRANSCRIPTION, DNA BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR A.L.CHAMBERS,L.H.PEARL,A.W.OLIVER,J.A.DOWNS
REVDAT 3 20-DEC-23 4BB7 1 REMARK
REVDAT 2 06-NOV-13 4BB7 1 JRNL
REVDAT 1 14-AUG-13 4BB7 0
JRNL AUTH A.L.CHAMBERS,L.H.PEARL,A.W.OLIVER,J.A.DOWNS
JRNL TITL THE BAH DOMAIN OF RSC2 IS A HISTONE H3 BINDING DOMAIN.
JRNL REF NUCLEIC ACIDS RES. V. 41 9168 2013
JRNL REFN ISSN 0305-1048
JRNL PMID 23907388
JRNL DOI 10.1093/NAR/GKT662
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.49
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.010
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 42819
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.220
REMARK 3 R VALUE (WORKING SET) : 0.217
REMARK 3 FREE R VALUE : 0.286
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.700
REMARK 3 FREE R VALUE TEST SET COUNT : 1998
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 44.5009 - 5.7805 0.99 3040 148 0.2879 0.3533
REMARK 3 2 5.7805 - 4.5897 0.99 2962 146 0.2122 0.2843
REMARK 3 3 4.5897 - 4.0100 0.99 2963 144 0.1898 0.2638
REMARK 3 4 4.0100 - 3.6435 0.98 2920 144 0.1987 0.2462
REMARK 3 5 3.6435 - 3.3825 0.98 2866 140 0.1972 0.2397
REMARK 3 6 3.3825 - 3.1831 0.98 2908 142 0.1968 0.2734
REMARK 3 7 3.1831 - 3.0237 0.98 2862 141 0.1965 0.2644
REMARK 3 8 3.0237 - 2.8921 0.98 2908 142 0.2162 0.2426
REMARK 3 9 2.8921 - 2.7808 0.98 2890 141 0.2037 0.3508
REMARK 3 10 2.7808 - 2.6849 0.98 2883 142 0.2348 0.2881
REMARK 3 11 2.6849 - 2.6009 0.99 2908 141 0.2309 0.3586
REMARK 3 12 2.6009 - 2.5266 0.98 2902 143 0.2569 0.3533
REMARK 3 13 2.5266 - 2.4601 0.99 2876 140 0.2415 0.2927
REMARK 3 14 2.4601 - 2.4000 0.99 2933 144 0.2543 0.3364
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.40
REMARK 3 B_SOL : 61.75
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.400
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.040
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.45
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.61650
REMARK 3 B22 (A**2) : -4.38210
REMARK 3 B33 (A**2) : 8.99860
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.21250
REMARK 3 B23 (A**2) : 0.00000
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 : 0.004 7850
REMARK 3 ANGLE : 0.772 10697
REMARK 3 CHIRALITY : 0.052 1114
REMARK 3 PLANARITY : 0.003 1404
REMARK 3 DIHEDRAL : 12.393 2943
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 4BB7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-SEP-12.
REMARK 100 THE DEPOSITION ID IS D_1290054162.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-APR-09
REMARK 200 TEMPERATURE (KELVIN) : 199
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I02
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97960
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42935
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 45.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.14000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.42000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
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: PDB ENTRY 1W4S
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES.NAOH PH 7.5, 0.2 M
REMARK 280 (NH4)2SO4, 20-30% W/V PEG 3350
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 32.03500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 1080 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.6 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 350
REMARK 350 BIOMOLECULE: 2
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: 370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29500 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.8 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 384
REMARK 465 HIS A 385
REMARK 465 HIS A 386
REMARK 465 HIS A 387
REMARK 465 HIS A 388
REMARK 465 HIS A 389
REMARK 465 HIS A 390
REMARK 465 LEU A 391
REMARK 465 GLU A 392
REMARK 465 VAL A 393
REMARK 465 LEU A 394
REMARK 465 PHE A 395
REMARK 465 GLN A 396
REMARK 465 GLY A 397
REMARK 465 PRO A 398
REMARK 465 LEU A 504
REMARK 465 ASN A 635
REMARK 465 THR A 636
REMARK 465 PRO A 637
REMARK 465 THR A 638
REMARK 465 ALA A 639
REMARK 465 ASN A 640
REMARK 465 ALA A 641
REMARK 465 MET B 384
REMARK 465 HIS B 385
REMARK 465 HIS B 386
REMARK 465 HIS B 387
REMARK 465 HIS B 388
REMARK 465 HIS B 389
REMARK 465 HIS B 390
REMARK 465 LEU B 391
REMARK 465 GLU B 392
REMARK 465 VAL B 393
REMARK 465 LEU B 394
REMARK 465 PHE B 395
REMARK 465 GLN B 396
REMARK 465 GLY B 397
REMARK 465 ASP B 538
REMARK 465 LEU B 539
REMARK 465 ASP B 540
REMARK 465 ASN B 635
REMARK 465 THR B 636
REMARK 465 PRO B 637
REMARK 465 THR B 638
REMARK 465 ALA B 639
REMARK 465 ASN B 640
REMARK 465 ALA B 641
REMARK 465 MET C 384
REMARK 465 HIS C 385
REMARK 465 HIS C 386
REMARK 465 HIS C 387
REMARK 465 HIS C 388
REMARK 465 HIS C 389
REMARK 465 HIS C 390
REMARK 465 LEU C 391
REMARK 465 GLU C 392
REMARK 465 VAL C 393
REMARK 465 LEU C 394
REMARK 465 PHE C 395
REMARK 465 GLN C 396
REMARK 465 GLY C 397
REMARK 465 PRO C 398
REMARK 465 HIS C 399
REMARK 465 THR C 634
REMARK 465 ASN C 635
REMARK 465 THR C 636
REMARK 465 PRO C 637
REMARK 465 THR C 638
REMARK 465 ALA C 639
REMARK 465 ASN C 640
REMARK 465 ALA C 641
REMARK 465 MET D 384
REMARK 465 HIS D 385
REMARK 465 HIS D 386
REMARK 465 HIS D 387
REMARK 465 HIS D 388
REMARK 465 HIS D 389
REMARK 465 HIS D 390
REMARK 465 LEU D 391
REMARK 465 GLU D 392
REMARK 465 VAL D 393
REMARK 465 LEU D 394
REMARK 465 PHE D 395
REMARK 465 GLN D 396
REMARK 465 GLY D 397
REMARK 465 PRO D 398
REMARK 465 THR D 634
REMARK 465 ASN D 635
REMARK 465 THR D 636
REMARK 465 PRO D 637
REMARK 465 THR D 638
REMARK 465 ALA D 639
REMARK 465 ASN D 640
REMARK 465 ALA D 641
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 HIS A 399 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 503 CG CD CE NZ
REMARK 470 GLU A 505 CG CD OE1 OE2
REMARK 470 GLU A 535 CG CD OE1 OE2
REMARK 470 ASP A 540 CG OD1 OD2
REMARK 470 GLU A 541 CG CD OE1 OE2
REMARK 470 ARG A 611 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 622 CG CD OE1 OE2
REMARK 470 GLU A 628 CG CD OE1 OE2
REMARK 470 THR A 634 OG1 CG2
REMARK 470 ARG B 497 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 503 CG CD CE NZ
REMARK 470 LEU B 504 CG CD1 CD2
REMARK 470 GLU B 517 CG CD OE1 OE2
REMARK 470 GLU B 541 CG CD OE1 OE2
REMARK 470 ASN B 547 CG OD1 ND2
REMARK 470 ARG B 597 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 611 CG CD NE CZ NH1 NH2
REMARK 470 SER B 619 OG
REMARK 470 GLU B 622 CG CD OE1 OE2
REMARK 470 THR B 634 OG1 CG2
REMARK 470 ASP C 401 CG OD1 OD2
REMARK 470 LYS C 503 CG CD CE NZ
REMARK 470 GLU C 534 CG CD OE1 OE2
REMARK 470 GLU C 535 CG CD OE1 OE2
REMARK 470 ASP C 538 CG OD1 OD2
REMARK 470 ASP C 540 CG OD1 OD2
REMARK 470 ARG C 611 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 622 CG CD OE1 OE2
REMARK 470 HIS D 399 CG ND1 CD2 CE1 NE2
REMARK 470 ASP D 401 CG OD1 OD2
REMARK 470 ARG D 497 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 503 CG CD CE NZ
REMARK 470 GLU D 505 CG CD OE1 OE2
REMARK 470 ASP D 540 CG OD1 OD2
REMARK 470 GLU D 622 CG CD OE1 OE2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS A 529 CD CE NZ
REMARK 480 ASP D 538 CG OD1 OD2
REMARK 480 ARG D 611 CG CD NE CZ NH1 NH2
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 527 77.17 -111.75
REMARK 500 ASP A 581 24.94 -79.77
REMARK 500 VAL A 586 143.37 -170.18
REMARK 500 ASN A 617 -8.68 71.49
REMARK 500 ASP A 618 49.83 -97.47
REMARK 500 GLU A 621 41.23 -91.71
REMARK 500 GLU A 622 143.35 -172.56
REMARK 500 ASP B 423 90.08 -167.21
REMARK 500 PRO B 424 -2.10 -59.34
REMARK 500 ASN B 467 57.89 -118.40
REMARK 500 GLU B 505 45.11 -94.72
REMARK 500 LYS B 520 72.08 52.38
REMARK 500 ILE B 536 -4.55 -141.01
REMARK 500 ASP B 581 40.30 -94.99
REMARK 500 LYS B 594 174.68 -56.23
REMARK 500 ASN B 617 -0.71 78.90
REMARK 500 SER B 619 82.58 46.19
REMARK 500 ASP C 423 97.94 -165.07
REMARK 500 PRO C 563 151.28 -49.97
REMARK 500 ASP C 598 76.78 -155.86
REMARK 500 ASP D 423 94.35 -167.60
REMARK 500 ASN D 467 57.60 -118.67
REMARK 500 ASP D 598 82.92 -155.46
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 A2070 DISTANCE = 6.43 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 900
DBREF 4BB7 A 401 641 UNP Q06488 RSC2_YEAST 401 641
DBREF 4BB7 B 401 641 UNP Q06488 RSC2_YEAST 401 641
DBREF 4BB7 C 401 641 UNP Q06488 RSC2_YEAST 401 641
DBREF 4BB7 D 401 641 UNP Q06488 RSC2_YEAST 401 641
SEQADV 4BB7 MET A 384 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 HIS A 385 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 HIS A 386 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 HIS A 387 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 HIS A 388 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 HIS A 389 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 HIS A 390 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 LEU A 391 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 GLU A 392 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 VAL A 393 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 LEU A 394 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 PHE A 395 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 GLN A 396 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 GLY A 397 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 PRO A 398 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 HIS A 399 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 MET A 400 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 MET B 384 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 HIS B 385 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 HIS B 386 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 HIS B 387 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 HIS B 388 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 HIS B 389 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 HIS B 390 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 LEU B 391 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 GLU B 392 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 VAL B 393 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 LEU B 394 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 PHE B 395 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 GLN B 396 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 GLY B 397 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 PRO B 398 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 HIS B 399 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 MET B 400 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 MET C 384 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 HIS C 385 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 HIS C 386 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 HIS C 387 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 HIS C 388 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 HIS C 389 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 HIS C 390 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 LEU C 391 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 GLU C 392 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 VAL C 393 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 LEU C 394 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 PHE C 395 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 GLN C 396 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 GLY C 397 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 PRO C 398 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 HIS C 399 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 MET C 400 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 MET D 384 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 HIS D 385 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 HIS D 386 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 HIS D 387 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 HIS D 388 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 HIS D 389 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 HIS D 390 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 LEU D 391 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 GLU D 392 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 VAL D 393 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 LEU D 394 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 PHE D 395 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 GLN D 396 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 GLY D 397 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 PRO D 398 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 HIS D 399 UNP Q06488 EXPRESSION TAG
SEQADV 4BB7 MET D 400 UNP Q06488 EXPRESSION TAG
SEQRES 1 A 258 MET HIS HIS HIS HIS HIS HIS LEU GLU VAL LEU PHE GLN
SEQRES 2 A 258 GLY PRO HIS MET ASP GLU VAL ILE VAL ASN ASN ILE SER
SEQRES 3 A 258 TYR HIS VAL GLY ASP TRP ALA LEU LEU ARG ASN GLN ASN
SEQRES 4 A 258 ASP PRO GLN LYS PRO ILE VAL GLY GLN ILE PHE ARG LEU
SEQRES 5 A 258 TRP LYS THR PRO ASP GLY LYS GLN TRP LEU ASN ALA CYS
SEQRES 6 A 258 TRP TYR TYR ARG PRO GLU GLN THR VAL HIS ARG VAL ASP
SEQRES 7 A 258 ARG LEU PHE TYR LYS ASN GLU VAL MET LYS THR GLY GLN
SEQRES 8 A 258 TYR ARG ASP HIS LEU VAL SER ASN LEU VAL GLY LYS CYS
SEQRES 9 A 258 TYR VAL ILE HIS PHE THR ARG TYR GLN ARG GLY ASN PRO
SEQRES 10 A 258 ASP MET LYS LEU GLU GLY PRO LEU PHE VAL CYS GLU PHE
SEQRES 11 A 258 ARG TYR ASN GLU SER ASP LYS ILE PHE ASN LYS ILE ARG
SEQRES 12 A 258 THR TRP LYS ALA CYS LEU PRO GLU GLU ILE ARG ASP LEU
SEQRES 13 A 258 ASP GLU ALA THR ILE PRO VAL ASN GLY ARG LYS PHE PHE
SEQRES 14 A 258 LYS TYR PRO SER PRO ILE ARG HIS LEU LEU PRO ALA ASN
SEQRES 15 A 258 ALA THR PRO HIS ASP ARG VAL PRO GLU PRO THR MET GLY
SEQRES 16 A 258 SER PRO ASP ALA PRO PRO LEU VAL GLY ALA VAL TYR MET
SEQRES 17 A 258 ARG PRO LYS MET GLN ARG ASP ASP LEU GLY GLU TYR ALA
SEQRES 18 A 258 THR SER ASP ASP CYS PRO ARG TYR ILE ILE ARG PRO ASN
SEQRES 19 A 258 ASP SER PRO GLU GLU GLY GLN VAL ASP ILE GLU THR GLY
SEQRES 20 A 258 THR ILE THR THR ASN THR PRO THR ALA ASN ALA
SEQRES 1 B 258 MET HIS HIS HIS HIS HIS HIS LEU GLU VAL LEU PHE GLN
SEQRES 2 B 258 GLY PRO HIS MET ASP GLU VAL ILE VAL ASN ASN ILE SER
SEQRES 3 B 258 TYR HIS VAL GLY ASP TRP ALA LEU LEU ARG ASN GLN ASN
SEQRES 4 B 258 ASP PRO GLN LYS PRO ILE VAL GLY GLN ILE PHE ARG LEU
SEQRES 5 B 258 TRP LYS THR PRO ASP GLY LYS GLN TRP LEU ASN ALA CYS
SEQRES 6 B 258 TRP TYR TYR ARG PRO GLU GLN THR VAL HIS ARG VAL ASP
SEQRES 7 B 258 ARG LEU PHE TYR LYS ASN GLU VAL MET LYS THR GLY GLN
SEQRES 8 B 258 TYR ARG ASP HIS LEU VAL SER ASN LEU VAL GLY LYS CYS
SEQRES 9 B 258 TYR VAL ILE HIS PHE THR ARG TYR GLN ARG GLY ASN PRO
SEQRES 10 B 258 ASP MET LYS LEU GLU GLY PRO LEU PHE VAL CYS GLU PHE
SEQRES 11 B 258 ARG TYR ASN GLU SER ASP LYS ILE PHE ASN LYS ILE ARG
SEQRES 12 B 258 THR TRP LYS ALA CYS LEU PRO GLU GLU ILE ARG ASP LEU
SEQRES 13 B 258 ASP GLU ALA THR ILE PRO VAL ASN GLY ARG LYS PHE PHE
SEQRES 14 B 258 LYS TYR PRO SER PRO ILE ARG HIS LEU LEU PRO ALA ASN
SEQRES 15 B 258 ALA THR PRO HIS ASP ARG VAL PRO GLU PRO THR MET GLY
SEQRES 16 B 258 SER PRO ASP ALA PRO PRO LEU VAL GLY ALA VAL TYR MET
SEQRES 17 B 258 ARG PRO LYS MET GLN ARG ASP ASP LEU GLY GLU TYR ALA
SEQRES 18 B 258 THR SER ASP ASP CYS PRO ARG TYR ILE ILE ARG PRO ASN
SEQRES 19 B 258 ASP SER PRO GLU GLU GLY GLN VAL ASP ILE GLU THR GLY
SEQRES 20 B 258 THR ILE THR THR ASN THR PRO THR ALA ASN ALA
SEQRES 1 C 258 MET HIS HIS HIS HIS HIS HIS LEU GLU VAL LEU PHE GLN
SEQRES 2 C 258 GLY PRO HIS MET ASP GLU VAL ILE VAL ASN ASN ILE SER
SEQRES 3 C 258 TYR HIS VAL GLY ASP TRP ALA LEU LEU ARG ASN GLN ASN
SEQRES 4 C 258 ASP PRO GLN LYS PRO ILE VAL GLY GLN ILE PHE ARG LEU
SEQRES 5 C 258 TRP LYS THR PRO ASP GLY LYS GLN TRP LEU ASN ALA CYS
SEQRES 6 C 258 TRP TYR TYR ARG PRO GLU GLN THR VAL HIS ARG VAL ASP
SEQRES 7 C 258 ARG LEU PHE TYR LYS ASN GLU VAL MET LYS THR GLY GLN
SEQRES 8 C 258 TYR ARG ASP HIS LEU VAL SER ASN LEU VAL GLY LYS CYS
SEQRES 9 C 258 TYR VAL ILE HIS PHE THR ARG TYR GLN ARG GLY ASN PRO
SEQRES 10 C 258 ASP MET LYS LEU GLU GLY PRO LEU PHE VAL CYS GLU PHE
SEQRES 11 C 258 ARG TYR ASN GLU SER ASP LYS ILE PHE ASN LYS ILE ARG
SEQRES 12 C 258 THR TRP LYS ALA CYS LEU PRO GLU GLU ILE ARG ASP LEU
SEQRES 13 C 258 ASP GLU ALA THR ILE PRO VAL ASN GLY ARG LYS PHE PHE
SEQRES 14 C 258 LYS TYR PRO SER PRO ILE ARG HIS LEU LEU PRO ALA ASN
SEQRES 15 C 258 ALA THR PRO HIS ASP ARG VAL PRO GLU PRO THR MET GLY
SEQRES 16 C 258 SER PRO ASP ALA PRO PRO LEU VAL GLY ALA VAL TYR MET
SEQRES 17 C 258 ARG PRO LYS MET GLN ARG ASP ASP LEU GLY GLU TYR ALA
SEQRES 18 C 258 THR SER ASP ASP CYS PRO ARG TYR ILE ILE ARG PRO ASN
SEQRES 19 C 258 ASP SER PRO GLU GLU GLY GLN VAL ASP ILE GLU THR GLY
SEQRES 20 C 258 THR ILE THR THR ASN THR PRO THR ALA ASN ALA
SEQRES 1 D 258 MET HIS HIS HIS HIS HIS HIS LEU GLU VAL LEU PHE GLN
SEQRES 2 D 258 GLY PRO HIS MET ASP GLU VAL ILE VAL ASN ASN ILE SER
SEQRES 3 D 258 TYR HIS VAL GLY ASP TRP ALA LEU LEU ARG ASN GLN ASN
SEQRES 4 D 258 ASP PRO GLN LYS PRO ILE VAL GLY GLN ILE PHE ARG LEU
SEQRES 5 D 258 TRP LYS THR PRO ASP GLY LYS GLN TRP LEU ASN ALA CYS
SEQRES 6 D 258 TRP TYR TYR ARG PRO GLU GLN THR VAL HIS ARG VAL ASP
SEQRES 7 D 258 ARG LEU PHE TYR LYS ASN GLU VAL MET LYS THR GLY GLN
SEQRES 8 D 258 TYR ARG ASP HIS LEU VAL SER ASN LEU VAL GLY LYS CYS
SEQRES 9 D 258 TYR VAL ILE HIS PHE THR ARG TYR GLN ARG GLY ASN PRO
SEQRES 10 D 258 ASP MET LYS LEU GLU GLY PRO LEU PHE VAL CYS GLU PHE
SEQRES 11 D 258 ARG TYR ASN GLU SER ASP LYS ILE PHE ASN LYS ILE ARG
SEQRES 12 D 258 THR TRP LYS ALA CYS LEU PRO GLU GLU ILE ARG ASP LEU
SEQRES 13 D 258 ASP GLU ALA THR ILE PRO VAL ASN GLY ARG LYS PHE PHE
SEQRES 14 D 258 LYS TYR PRO SER PRO ILE ARG HIS LEU LEU PRO ALA ASN
SEQRES 15 D 258 ALA THR PRO HIS ASP ARG VAL PRO GLU PRO THR MET GLY
SEQRES 16 D 258 SER PRO ASP ALA PRO PRO LEU VAL GLY ALA VAL TYR MET
SEQRES 17 D 258 ARG PRO LYS MET GLN ARG ASP ASP LEU GLY GLU TYR ALA
SEQRES 18 D 258 THR SER ASP ASP CYS PRO ARG TYR ILE ILE ARG PRO ASN
SEQRES 19 D 258 ASP SER PRO GLU GLU GLY GLN VAL ASP ILE GLU THR GLY
SEQRES 20 D 258 THR ILE THR THR ASN THR PRO THR ALA ASN ALA
HET SO4 A 700 5
HET CL A 800 1
HET CL A 801 1
HET SO4 B 700 5
HET CL B 701 1
HET CL B 702 1
HET CL B 703 1
HET SO4 C 700 5
HET SO4 C 701 5
HET SO4 C 702 5
HET CL C 801 1
HET SO4 D 700 5
HET SO4 D 701 5
HET SO4 D 702 5
HET CL D 703 1
HET CL D 704 1
HET GOL D 900 6
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 SO4 8(O4 S 2-)
FORMUL 6 CL 8(CL 1-)
FORMUL 21 GOL C3 H8 O3
FORMUL 22 HOH *541(H2 O)
HELIX 1 1 ARG A 452 THR A 456 5 5
HELIX 2 2 PHE A 492 ARG A 497 1 6
HELIX 3 3 THR A 527 LEU A 532 5 6
HELIX 4 4 PRO A 533 ARG A 537 5 5
HELIX 5 5 ILE A 558 LEU A 562 5 5
HELIX 6 6 ARG B 452 GLN B 455 5 4
HELIX 7 7 PHE B 492 ARG B 497 1 6
HELIX 8 8 THR B 527 LEU B 532 5 6
HELIX 9 9 PRO B 533 ARG B 537 5 5
HELIX 10 10 ILE B 558 LEU B 562 5 5
HELIX 11 11 ARG C 452 GLN C 455 5 4
HELIX 12 12 PHE C 492 ARG C 497 1 6
HELIX 13 13 THR C 527 LEU C 532 5 6
HELIX 14 14 ILE C 558 LEU C 562 5 5
HELIX 15 15 ARG D 452 GLN D 455 5 4
HELIX 16 16 PHE D 492 ARG D 497 1 6
HELIX 17 17 THR D 527 LEU D 532 5 6
HELIX 18 18 PRO D 533 ARG D 537 5 5
HELIX 19 19 ILE D 558 LEU D 562 5 5
SHEET 1 AA 2 VAL A 403 VAL A 405 0
SHEET 2 AA 2 ILE A 408 TYR A 410 -1 O ILE A 408 N VAL A 405
SHEET 1 AB 5 MET A 470 LEU A 479 0
SHEET 2 AB 5 GLN A 443 TYR A 451 -1 O LEU A 445 N HIS A 478
SHEET 3 AB 5 ILE A 428 LYS A 437 -1 O VAL A 429 N TYR A 450
SHEET 4 AB 5 TRP A 415 LEU A 418 -1 O ALA A 416 N GLY A 430
SHEET 5 AB 5 LEU A 483 LYS A 486 -1 N VAL A 484 O LEU A 417
SHEET 1 AC 2 HIS A 458 ARG A 459 0
SHEET 2 AC 2 VAL A 589 TYR A 590 1 N TYR A 590 O HIS A 458
SHEET 1 AD 2 LEU A 463 TYR A 465 0
SHEET 2 AD 2 ARG A 549 PRO A 555 -1 O TYR A 554 N PHE A 464
SHEET 1 AE 2 ILE A 613 ILE A 614 0
SHEET 2 AE 2 ARG A 549 PRO A 555 1 O PHE A 551 N ILE A 614
SHEET 1 AF 4 GLN A 624 ASP A 626 0
SHEET 2 AF 4 THR A 631 THR A 633 -1 O THR A 631 N ASP A 626
SHEET 3 AF 4 ARG A 549 PRO A 555 -1 O LYS A 550 N ILE A 632
SHEET 4 AF 4 ILE A 613 ILE A 614 1 O ILE A 614 N LYS A 553
SHEET 1 AG 4 GLN A 624 ASP A 626 0
SHEET 2 AG 4 THR A 631 THR A 633 -1 O THR A 631 N ASP A 626
SHEET 3 AG 4 ARG A 549 PRO A 555 -1 O LYS A 550 N ILE A 632
SHEET 4 AG 4 LEU A 463 TYR A 465 -1 O PHE A 464 N TYR A 554
SHEET 1 AH 2 TYR A 488 HIS A 491 0
SHEET 2 AH 2 LEU A 508 CYS A 511 1 O PHE A 509 N ILE A 490
SHEET 1 AI 2 GLY A 498 PRO A 500 0
SHEET 2 AI 2 THR A 543 PRO A 545 -1 O ILE A 544 N ASN A 499
SHEET 1 AJ 2 PHE A 513 ASN A 516 0
SHEET 2 AJ 2 ILE A 521 LYS A 524 -1 O ILE A 521 N ASN A 516
SHEET 1 BA 2 VAL B 403 ILE B 404 0
SHEET 2 BA 2 SER B 409 TYR B 410 -1 O TYR B 410 N VAL B 403
SHEET 1 BB 5 MET B 470 LEU B 479 0
SHEET 2 BB 5 GLN B 443 TYR B 451 -1 O LEU B 445 N HIS B 478
SHEET 3 BB 5 ILE B 428 LYS B 437 -1 O VAL B 429 N TYR B 450
SHEET 4 BB 5 TRP B 415 LEU B 418 -1 O ALA B 416 N GLY B 430
SHEET 5 BB 5 LEU B 483 LYS B 486 -1 N VAL B 484 O LEU B 417
SHEET 1 BC 2 VAL B 457 ARG B 459 0
SHEET 2 BC 2 ALA B 588 TYR B 590 1 O ALA B 588 N HIS B 458
SHEET 1 BD 2 PHE B 464 TYR B 465 0
SHEET 2 BD 2 ARG B 549 TYR B 554 -1 O TYR B 554 N PHE B 464
SHEET 1 BE 2 ILE B 613 ILE B 614 0
SHEET 2 BE 2 ARG B 549 TYR B 554 1 O PHE B 551 N ILE B 614
SHEET 1 BF 4 GLN B 624 ASP B 626 0
SHEET 2 BF 4 THR B 631 THR B 633 -1 O THR B 631 N ASP B 626
SHEET 3 BF 4 ARG B 549 TYR B 554 -1 O LYS B 550 N ILE B 632
SHEET 4 BF 4 ILE B 613 ILE B 614 1 O ILE B 614 N LYS B 553
SHEET 1 BG 4 GLN B 624 ASP B 626 0
SHEET 2 BG 4 THR B 631 THR B 633 -1 O THR B 631 N ASP B 626
SHEET 3 BG 4 ARG B 549 TYR B 554 -1 O LYS B 550 N ILE B 632
SHEET 4 BG 4 PHE B 464 TYR B 465 -1 O PHE B 464 N TYR B 554
SHEET 1 BH 2 TYR B 488 HIS B 491 0
SHEET 2 BH 2 LEU B 508 CYS B 511 1 O PHE B 509 N ILE B 490
SHEET 1 BI 2 GLY B 498 PRO B 500 0
SHEET 2 BI 2 THR B 543 PRO B 545 -1 O ILE B 544 N ASN B 499
SHEET 1 BJ 2 PHE B 513 ASN B 516 0
SHEET 2 BJ 2 ILE B 521 LYS B 524 -1 O ILE B 521 N ASN B 516
SHEET 1 CA 2 VAL C 403 VAL C 405 0
SHEET 2 CA 2 ILE C 408 TYR C 410 -1 O ILE C 408 N VAL C 405
SHEET 1 CB 5 MET C 470 LEU C 479 0
SHEET 2 CB 5 GLN C 443 TYR C 451 -1 O LEU C 445 N HIS C 478
SHEET 3 CB 5 ILE C 428 LYS C 437 -1 O VAL C 429 N TYR C 450
SHEET 4 CB 5 TRP C 415 LEU C 418 -1 O ALA C 416 N GLY C 430
SHEET 5 CB 5 LEU C 483 LYS C 486 -1 N VAL C 484 O LEU C 417
SHEET 1 CC 2 VAL C 457 ARG C 459 0
SHEET 2 CC 2 ALA C 588 TYR C 590 1 O ALA C 588 N HIS C 458
SHEET 1 CD 2 LEU C 463 PHE C 464 0
SHEET 2 CD 2 TYR C 554 PRO C 555 -1 O TYR C 554 N PHE C 464
SHEET 1 CE 2 TYR C 488 HIS C 491 0
SHEET 2 CE 2 LEU C 508 CYS C 511 1 O PHE C 509 N ILE C 490
SHEET 1 CF 2 GLY C 498 PRO C 500 0
SHEET 2 CF 2 THR C 543 PRO C 545 -1 O ILE C 544 N ASN C 499
SHEET 1 CG 2 PHE C 513 ASN C 516 0
SHEET 2 CG 2 ILE C 521 LYS C 524 -1 O ILE C 521 N ASN C 516
SHEET 1 CH 4 ILE C 613 ILE C 614 0
SHEET 2 CH 4 LYS C 550 PHE C 552 1 O PHE C 551 N ILE C 614
SHEET 3 CH 4 THR C 631 THR C 633 -1 O ILE C 632 N LYS C 550
SHEET 4 CH 4 GLN C 624 ASP C 626 -1 O GLN C 624 N THR C 633
SHEET 1 DA 2 VAL D 403 VAL D 405 0
SHEET 2 DA 2 ILE D 408 TYR D 410 -1 O ILE D 408 N VAL D 405
SHEET 1 DB 5 MET D 470 LEU D 479 0
SHEET 2 DB 5 GLN D 443 TYR D 451 -1 O LEU D 445 N HIS D 478
SHEET 3 DB 5 ILE D 428 LYS D 437 -1 O VAL D 429 N TYR D 450
SHEET 4 DB 5 TRP D 415 LEU D 418 -1 O ALA D 416 N GLY D 430
SHEET 5 DB 5 LEU D 483 LYS D 486 -1 N VAL D 484 O LEU D 417
SHEET 1 DC 2 VAL D 457 ARG D 459 0
SHEET 2 DC 2 ALA D 588 TYR D 590 1 O ALA D 588 N HIS D 458
SHEET 1 DD 2 TYR D 488 HIS D 491 0
SHEET 2 DD 2 LEU D 508 CYS D 511 1 O PHE D 509 N ILE D 490
SHEET 1 DE 2 GLY D 498 PRO D 500 0
SHEET 2 DE 2 THR D 543 PRO D 545 -1 O ILE D 544 N ASN D 499
SHEET 1 DF 2 PHE D 513 ASN D 516 0
SHEET 2 DF 2 ILE D 521 LYS D 524 -1 O ILE D 521 N ASN D 516
SHEET 1 DG 4 ILE D 613 ILE D 614 0
SHEET 2 DG 4 LYS D 550 PHE D 552 1 O PHE D 551 N ILE D 614
SHEET 3 DG 4 THR D 631 THR D 633 -1 O ILE D 632 N LYS D 550
SHEET 4 DG 4 GLN D 624 ASP D 626 -1 O GLN D 624 N THR D 633
SITE 1 AC1 3 ILE A 525 ARG A 526 THR A 527
SITE 1 AC2 3 ARG A 459 ARG A 462 TYR A 603
SITE 1 AC3 1 ASN A 482
SITE 1 AC4 4 ARG A 526 ARG B 514 ARG B 526 THR B 527
SITE 1 AC5 3 ARG B 459 ARG B 462 TYR B 603
SITE 1 AC6 4 ARG C 514 ARG C 526 THR C 527 HOH D2098
SITE 1 AC7 9 PHE C 522 ASN C 523 LYS C 524 ARG C 526
SITE 2 AC7 9 HOH C2101 HOH C2102 HOH C2149 SO4 D 702
SITE 3 AC7 9 HOH D2099
SITE 1 AC8 5 ASN C 516 GLU C 517 SER C 518 HOH C2058
SITE 2 AC8 5 ARG D 597
SITE 1 AC9 3 ARG C 459 ARG C 462 TYR C 603
SITE 1 BC1 3 ARG D 526 THR D 527 HOH D2165
SITE 1 BC2 7 TYR D 515 ASN D 516 GLU D 517 SER D 518
SITE 2 BC2 7 HOH D2061 HOH D2063 HOH D2166
SITE 1 BC3 6 SO4 C 701 ASN D 523 LYS D 524 ARG D 526
SITE 2 BC3 6 HOH D2099 HOH D2145
SITE 1 BC4 3 ARG D 459 ARG D 462 TYR D 603
SITE 1 BC5 4 ARG D 549 THR D 631 THR D 633 HOH D2164
SITE 1 BC6 4 VAL D 460 ASP D 461 HOH D2167 HOH D2168
CRYST1 64.090 64.070 136.840 90.00 95.47 90.00 P 1 21 1 8
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 0.015603 0.000000 0.001494 0.00000
SCALE2 0.000000 0.015608 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007341 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
