HEADER ANTITUMOR PROTEIN 06-FEB-15 4Y18
TITLE STRUCTURE OF BRCA1 BRCT DOMAINS IN COMPLEX WITH ABRAXAS DOUBLE
TITLE 2 PHOSPHORYLATED PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BREAST CANCER TYPE 1 SUSCEPTIBILITY PROTEIN;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 FRAGMENT: BRCT DOMAINS, UNP RESIDUES 1646-1859;
COMPND 5 SYNONYM: RING FINGER PROTEIN 53;
COMPND 6 EC: 6.3.2.-;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: BRCA1-A COMPLEX SUBUNIT ABRAXAS;
COMPND 10 CHAIN: I, J, K, L, M, N, O, P;
COMPND 11 FRAGMENT: UNP RESIDUES 399-409;
COMPND 12 SYNONYM: COILED-COIL DOMAIN-CONTAINING PROTEIN 98,PROTEIN FAM175A;
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 GENE: BRCA1, RNF53;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606
KEYWDS DNA DAMAGE RESPONSE, BRCT, PHOSPHOPEPTIDE, LIGASE-PEPTIDE COMPLEX,
KEYWDS 2 ANTITUMOR PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Q.WU,T.L.BLUNDELL
REVDAT 5 10-JAN-24 4Y18 1 REMARK
REVDAT 4 10-JUL-19 4Y18 1 REMARK
REVDAT 3 20-FEB-19 4Y18 1 REMARK LINK
REVDAT 2 17-FEB-16 4Y18 1 JRNL
REVDAT 1 27-JAN-16 4Y18 0
JRNL AUTH Q.WU,A.PAUL,D.SU,S.MEHMOOD,T.K.FOO,T.OCHI,E.L.BUNTING,B.XIA,
JRNL AUTH 2 C.V.ROBINSON,B.WANG,T.L.BLUNDELL
JRNL TITL STRUCTURE OF BRCA1-BRCT/ABRAXAS COMPLEX REVEALS
JRNL TITL 2 PHOSPHORYLATION-DEPENDENT BRCT DIMERIZATION AT DNA DAMAGE
JRNL TITL 3 SITES.
JRNL REF MOL.CELL V. 61 434 2016
JRNL REFN ISSN 1097-2765
JRNL PMID 26778126
JRNL DOI 10.1016/J.MOLCEL.2015.12.017
REMARK 2
REMARK 2 RESOLUTION. 3.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.4_1496)
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) : 3.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 95.26
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 39160
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.236
REMARK 3 R VALUE (WORKING SET) : 0.233
REMARK 3 FREE R VALUE : 0.298
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1961
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 95.2902 - 8.4337 1.00 2838 155 0.1969 0.2969
REMARK 3 2 8.4337 - 6.6946 1.00 2721 147 0.2130 0.2838
REMARK 3 3 6.6946 - 5.8485 1.00 2694 132 0.2408 0.3126
REMARK 3 4 5.8485 - 5.3138 1.00 2665 146 0.2184 0.2663
REMARK 3 5 5.3138 - 4.9330 1.00 2676 139 0.2124 0.2551
REMARK 3 6 4.9330 - 4.6421 1.00 2627 141 0.2283 0.2649
REMARK 3 7 4.6421 - 4.4097 1.00 2635 137 0.2384 0.3239
REMARK 3 8 4.4097 - 4.2177 1.00 2648 140 0.2426 0.3057
REMARK 3 9 4.2177 - 4.0553 1.00 2638 140 0.2422 0.2933
REMARK 3 10 4.0553 - 3.9154 1.00 2607 140 0.2661 0.3544
REMARK 3 11 3.9154 - 3.7930 1.00 2640 136 0.2820 0.2909
REMARK 3 12 3.7930 - 3.6845 1.00 2620 136 0.2899 0.3440
REMARK 3 13 3.6845 - 3.5875 1.00 2627 142 0.2937 0.3554
REMARK 3 14 3.5875 - 3.5000 0.98 2563 130 0.3194 0.3409
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 : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.470
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.080
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 14312
REMARK 3 ANGLE : 0.900 19493
REMARK 3 CHIRALITY : 0.031 2184
REMARK 3 PLANARITY : 0.003 2478
REMARK 3 DIHEDRAL : 13.510 5111
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 4Y18 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-FEB-15.
REMARK 100 THE DEPOSITION ID IS D_1000206545.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAR-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9200
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39170
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.500
REMARK 200 RESOLUTION RANGE LOW (A) : 95.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 7.400
REMARK 200 R MERGE (I) : 0.09600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : 7.80
REMARK 200 R MERGE FOR SHELL (I) : 0.70100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
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: 1T15
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HEPES, AMMONIUM SULPHATE, PEG 4000.,
REMARK 280 PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
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 43.40950
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 95.25500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 91.86300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 95.25500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 43.40950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 91.86300
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, 4, 5, 6, 7, 8, 9, 10, 11, 12
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 APPLY THE FOLLOWING TO CHAINS: A, I
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22030 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, I, J
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: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, J
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, K
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, K
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 APPLY THE FOLLOWING TO CHAINS: E, M
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 -43.40950
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 -91.86300
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, L
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 7
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3240 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, L
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, N
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -91.86300
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -95.25500
REMARK 350
REMARK 350 BIOMOLECULE: 8
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, M
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: 9
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, N
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: 10
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, O
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: 11
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3030 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, O, P
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 12
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, P
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 1636
REMARK 465 SER A 1637
REMARK 465 HIS A 1638
REMARK 465 HIS A 1639
REMARK 465 HIS A 1640
REMARK 465 HIS A 1641
REMARK 465 HIS A 1642
REMARK 465 HIS A 1643
REMARK 465 SER A 1644
REMARK 465 MET A 1645
REMARK 465 MET B 1636
REMARK 465 SER B 1637
REMARK 465 HIS B 1638
REMARK 465 HIS B 1639
REMARK 465 HIS B 1640
REMARK 465 HIS B 1641
REMARK 465 HIS B 1642
REMARK 465 HIS B 1643
REMARK 465 SER B 1644
REMARK 465 MET B 1645
REMARK 465 MET C 1636
REMARK 465 SER C 1637
REMARK 465 HIS C 1638
REMARK 465 HIS C 1639
REMARK 465 HIS C 1640
REMARK 465 HIS C 1641
REMARK 465 HIS C 1642
REMARK 465 HIS C 1643
REMARK 465 SER C 1644
REMARK 465 MET C 1645
REMARK 465 MET D 1636
REMARK 465 SER D 1637
REMARK 465 HIS D 1638
REMARK 465 HIS D 1639
REMARK 465 HIS D 1640
REMARK 465 HIS D 1641
REMARK 465 HIS D 1642
REMARK 465 HIS D 1643
REMARK 465 SER D 1644
REMARK 465 MET D 1645
REMARK 465 PRO D 1859
REMARK 465 MET E 1636
REMARK 465 SER E 1637
REMARK 465 HIS E 1638
REMARK 465 HIS E 1639
REMARK 465 HIS E 1640
REMARK 465 HIS E 1641
REMARK 465 HIS E 1642
REMARK 465 HIS E 1643
REMARK 465 SER E 1644
REMARK 465 MET E 1645
REMARK 465 MET F 1636
REMARK 465 SER F 1637
REMARK 465 HIS F 1638
REMARK 465 HIS F 1639
REMARK 465 HIS F 1640
REMARK 465 HIS F 1641
REMARK 465 HIS F 1642
REMARK 465 HIS F 1643
REMARK 465 SER F 1644
REMARK 465 MET F 1645
REMARK 465 MET G 1636
REMARK 465 SER G 1637
REMARK 465 HIS G 1638
REMARK 465 HIS G 1639
REMARK 465 HIS G 1640
REMARK 465 HIS G 1641
REMARK 465 HIS G 1642
REMARK 465 HIS G 1643
REMARK 465 SER G 1644
REMARK 465 MET G 1645
REMARK 465 VAL G 1646
REMARK 465 ASN G 1647
REMARK 465 LYS G 1648
REMARK 465 MET H 1636
REMARK 465 SER H 1637
REMARK 465 HIS H 1638
REMARK 465 HIS H 1639
REMARK 465 HIS H 1640
REMARK 465 HIS H 1641
REMARK 465 HIS H 1642
REMARK 465 HIS H 1643
REMARK 465 SER H 1644
REMARK 465 MET H 1645
REMARK 465 VAL H 1646
REMARK 465 ASN H 1647
REMARK 465 LYS H 1648
REMARK 465 GLY I 399
REMARK 465 PHE I 400
REMARK 465 GLY J 399
REMARK 465 PHE J 400
REMARK 465 GLY K 399
REMARK 465 PHE K 400
REMARK 465 GLY L 399
REMARK 465 PHE L 400
REMARK 465 GLY L 401
REMARK 465 GLY M 399
REMARK 465 PHE M 400
REMARK 465 GLY M 401
REMARK 465 GLY N 399
REMARK 465 PHE N 400
REMARK 465 GLY N 401
REMARK 465 GLU N 402
REMARK 465 GLY O 399
REMARK 465 PHE O 400
REMARK 465 GLY O 401
REMARK 465 GLU O 402
REMARK 465 GLY P 399
REMARK 465 PHE P 400
REMARK 465 GLY P 401
REMARK 465 GLU P 402
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 LYS A1648 CG CD CE NZ
REMARK 470 ARG A1649 CG CD NE CZ NH1 NH2
REMARK 470 LYS A1667 CG CD CE NZ
REMARK 470 LEU A1800 CG CD1 CD2
REMARK 470 ASP A1851 CG OD1 OD2
REMARK 470 LYS B1648 CG CD CE NZ
REMARK 470 ARG B1649 CG CD NE CZ NH1 NH2
REMARK 470 LYS B1671 CG CD CE NZ
REMARK 470 ARG B1758 CG CD NE CZ NH1 NH2
REMARK 470 GLU B1817 CG CD OE1 OE2
REMARK 470 LYS C1648 CG CD CE NZ
REMARK 470 ARG C1649 CG CD NE CZ NH1 NH2
REMARK 470 LEU C1664 CG CD1 CD2
REMARK 470 LYS C1671 CG CD CE NZ
REMARK 470 GLU C1817 CG CD OE1 OE2
REMARK 470 ASN C1819 CG OD1 ND2
REMARK 470 ARG D1649 CG CD NE CZ NH1 NH2
REMARK 470 LYS D1667 CG CD CE NZ
REMARK 470 LYS D1671 CG CD CE NZ
REMARK 470 HIS D1732 CG ND1 CD2 CE1 NE2
REMARK 470 ARG D1762 CG CD NE CZ NH1 NH2
REMARK 470 GLU D1817 CG CD OE1 OE2
REMARK 470 ASP D1818 CG OD1 OD2
REMARK 470 ASN D1819 CG OD1 ND2
REMARK 470 LYS E1648 CG CD CE NZ
REMARK 470 ARG E1649 CG CD NE CZ NH1 NH2
REMARK 470 LYS E1671 CG CD CE NZ
REMARK 470 LEU E1679 CG CD1 CD2
REMARK 470 LYS E1724 CG CD CE NZ
REMARK 470 ARG E1758 CG CD NE CZ NH1 NH2
REMARK 470 ARG E1762 CG CD NE CZ NH1 NH2
REMARK 470 GLU E1817 CG CD OE1 OE2
REMARK 470 LYS F1648 CG CD CE NZ
REMARK 470 ARG F1649 CG CD NE CZ NH1 NH2
REMARK 470 LYS F1671 CG CD CE NZ
REMARK 470 ARG F1726 CG CD NE CZ NH1 NH2
REMARK 470 LYS F1727 CG CD CE NZ
REMARK 470 ARG F1758 CG CD NE CZ NH1 NH2
REMARK 470 GLU F1817 CG CD OE1 OE2
REMARK 470 ASP F1818 CG OD1 OD2
REMARK 470 ASN F1819 CG OD1 ND2
REMARK 470 ARG G1649 CG CD NE CZ NH1 NH2
REMARK 470 MET G1652 CG SD CE
REMARK 470 PHE G1662 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 MET G1663 CG SD CE
REMARK 470 ARG G1758 CG CD NE CZ NH1 NH2
REMARK 470 GLU G1817 CG CD OE1 OE2
REMARK 470 ASP G1818 CG OD1 OD2
REMARK 470 ARG H1649 CG CD NE CZ NH1 NH2
REMARK 470 MET H1652 CG SD CE
REMARK 470 PHE H1662 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 MET H1663 CG SD CE
REMARK 470 TYR H1666 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS H1667 CG CD CE NZ
REMARK 470 PHE H1668 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS H1671 CG CD CE NZ
REMARK 470 VAL H1688 CG1 CG2
REMARK 470 LYS H1711 CG CD CE NZ
REMARK 470 LYS H1724 CG CD CE NZ
REMARK 470 ARG H1726 CG CD NE CZ NH1 NH2
REMARK 470 ARG H1758 CG CD NE CZ NH1 NH2
REMARK 470 GLU H1817 CG CD OE1 OE2
REMARK 470 ASP H1818 CG OD1 OD2
REMARK 470 GLN H1857 CG CD OE1 NE2
REMARK 470 ARG I 405 CG CD NE CZ NH1 NH2
REMARK 470 ARG J 405 CG CD NE CZ NH1 NH2
REMARK 470 ARG K 405 CG CD NE CZ NH1 NH2
REMARK 470 ARG L 405 CG CD NE CZ NH1 NH2
REMARK 470 ARG N 405 CG CD NE CZ NH1 NH2
REMARK 470 TYR O 403 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG O 405 CG CD NE CZ NH1 NH2
REMARK 470 ARG P 405 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O ALA D 1669 O HIS D 1672 1.88
REMARK 500 OG SER B 1722 O LYS B 1727 2.16
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 SD MET C 1663 SD MET E 1663 4445 1.03
REMARK 500 SD MET C 1663 CG MET E 1663 4445 1.80
REMARK 500 SD MET C 1663 CE MET E 1663 4445 1.91
REMARK 500 CE MET C 1663 CG MET E 1663 4445 1.94
REMARK 500 NH2 ARG D 1670 O1P SEP N 406 3544 2.06
REMARK 500 NH2 ARG D 1670 O ARG N 405 3544 2.11
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 A1745 45.93 -152.84
REMARK 500 GLU A1829 76.00 -100.42
REMARK 500 ASN B1745 46.68 -153.08
REMARK 500 MET B1775 109.34 -160.31
REMARK 500 GLU B1817 14.46 59.09
REMARK 500 ASN C1745 46.33 -153.29
REMARK 500 GLU C1817 14.86 58.99
REMARK 500 GLU C1829 78.06 -102.28
REMARK 500 ASN D1745 45.81 -151.64
REMARK 500 GLU D1829 78.22 -103.11
REMARK 500 GLN D1857 -159.15 -108.23
REMARK 500 ASN E1745 47.70 -152.96
REMARK 500 GLU E1817 7.23 58.11
REMARK 500 GLU E1829 78.61 -102.65
REMARK 500 ASN F1745 47.06 -152.21
REMARK 500 GLU F1829 76.00 -102.01
REMARK 500 ASN G1745 46.73 -152.50
REMARK 500 MET G1775 109.16 -160.98
REMARK 500 GLU G1829 78.67 -102.98
REMARK 500 ASN H1745 47.22 -152.93
REMARK 500 GLU H1829 78.82 -101.29
REMARK 500 SEP N 404 -4.75 84.26
REMARK 500 ARG N 405 -134.66 53.55
REMARK 500
REMARK 500 REMARK: NULL
DBREF 4Y18 A 1646 1859 UNP P38398 BRCA1_HUMAN 1646 1859
DBREF 4Y18 B 1646 1859 UNP P38398 BRCA1_HUMAN 1646 1859
DBREF 4Y18 C 1646 1859 UNP P38398 BRCA1_HUMAN 1646 1859
DBREF 4Y18 D 1646 1859 UNP P38398 BRCA1_HUMAN 1646 1859
DBREF 4Y18 E 1646 1859 UNP P38398 BRCA1_HUMAN 1646 1859
DBREF 4Y18 F 1646 1859 UNP P38398 BRCA1_HUMAN 1646 1859
DBREF 4Y18 G 1646 1859 UNP P38398 BRCA1_HUMAN 1646 1859
DBREF 4Y18 H 1646 1859 UNP P38398 BRCA1_HUMAN 1646 1859
DBREF 4Y18 I 399 409 UNP Q6UWZ7 F175A_HUMAN 399 409
DBREF 4Y18 J 399 409 UNP Q6UWZ7 F175A_HUMAN 399 409
DBREF 4Y18 K 399 409 UNP Q6UWZ7 F175A_HUMAN 399 409
DBREF 4Y18 L 399 409 UNP Q6UWZ7 F175A_HUMAN 399 409
DBREF 4Y18 M 399 409 UNP Q6UWZ7 F175A_HUMAN 399 409
DBREF 4Y18 N 399 409 UNP Q6UWZ7 F175A_HUMAN 399 409
DBREF 4Y18 O 399 409 UNP Q6UWZ7 F175A_HUMAN 399 409
DBREF 4Y18 P 399 409 UNP Q6UWZ7 F175A_HUMAN 399 409
SEQADV 4Y18 MET A 1636 UNP P38398 INITIATING METHIONINE
SEQADV 4Y18 SER A 1637 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS A 1638 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS A 1639 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS A 1640 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS A 1641 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS A 1642 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS A 1643 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 SER A 1644 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 MET A 1645 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 MET B 1636 UNP P38398 INITIATING METHIONINE
SEQADV 4Y18 SER B 1637 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS B 1638 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS B 1639 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS B 1640 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS B 1641 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS B 1642 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS B 1643 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 SER B 1644 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 MET B 1645 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 MET C 1636 UNP P38398 INITIATING METHIONINE
SEQADV 4Y18 SER C 1637 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS C 1638 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS C 1639 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS C 1640 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS C 1641 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS C 1642 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS C 1643 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 SER C 1644 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 MET C 1645 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 MET D 1636 UNP P38398 INITIATING METHIONINE
SEQADV 4Y18 SER D 1637 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS D 1638 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS D 1639 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS D 1640 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS D 1641 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS D 1642 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS D 1643 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 SER D 1644 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 MET D 1645 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 MET E 1636 UNP P38398 INITIATING METHIONINE
SEQADV 4Y18 SER E 1637 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS E 1638 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS E 1639 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS E 1640 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS E 1641 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS E 1642 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS E 1643 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 SER E 1644 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 MET E 1645 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 MET F 1636 UNP P38398 INITIATING METHIONINE
SEQADV 4Y18 SER F 1637 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS F 1638 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS F 1639 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS F 1640 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS F 1641 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS F 1642 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS F 1643 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 SER F 1644 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 MET F 1645 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 MET G 1636 UNP P38398 INITIATING METHIONINE
SEQADV 4Y18 SER G 1637 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS G 1638 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS G 1639 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS G 1640 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS G 1641 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS G 1642 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS G 1643 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 SER G 1644 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 MET G 1645 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 MET H 1636 UNP P38398 INITIATING METHIONINE
SEQADV 4Y18 SER H 1637 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS H 1638 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS H 1639 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS H 1640 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS H 1641 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS H 1642 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 HIS H 1643 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 SER H 1644 UNP P38398 EXPRESSION TAG
SEQADV 4Y18 MET H 1645 UNP P38398 EXPRESSION TAG
SEQRES 1 A 224 MET SER HIS HIS HIS HIS HIS HIS SER MET VAL ASN LYS
SEQRES 2 A 224 ARG MET SER MET VAL VAL SER GLY LEU THR PRO GLU GLU
SEQRES 3 A 224 PHE MET LEU VAL TYR LYS PHE ALA ARG LYS HIS HIS ILE
SEQRES 4 A 224 THR LEU THR ASN LEU ILE THR GLU GLU THR THR HIS VAL
SEQRES 5 A 224 VAL MET LYS THR ASP ALA GLU PHE VAL CYS GLU ARG THR
SEQRES 6 A 224 LEU LYS TYR PHE LEU GLY ILE ALA GLY GLY LYS TRP VAL
SEQRES 7 A 224 VAL SER TYR PHE TRP VAL THR GLN SER ILE LYS GLU ARG
SEQRES 8 A 224 LYS MET LEU ASN GLU HIS ASP PHE GLU VAL ARG GLY ASP
SEQRES 9 A 224 VAL VAL ASN GLY ARG ASN HIS GLN GLY PRO LYS ARG ALA
SEQRES 10 A 224 ARG GLU SER GLN ASP ARG LYS ILE PHE ARG GLY LEU GLU
SEQRES 11 A 224 ILE CYS CYS TYR GLY PRO PHE THR ASN MET PRO THR ASP
SEQRES 12 A 224 GLN LEU GLU TRP MET VAL GLN LEU CYS GLY ALA SER VAL
SEQRES 13 A 224 VAL LYS GLU LEU SER SER PHE THR LEU GLY THR GLY VAL
SEQRES 14 A 224 HIS PRO ILE VAL VAL VAL GLN PRO ASP ALA TRP THR GLU
SEQRES 15 A 224 ASP ASN GLY PHE HIS ALA ILE GLY GLN MET CYS GLU ALA
SEQRES 16 A 224 PRO VAL VAL THR ARG GLU TRP VAL LEU ASP SER VAL ALA
SEQRES 17 A 224 LEU TYR GLN CYS GLN GLU LEU ASP THR TYR LEU ILE PRO
SEQRES 18 A 224 GLN ILE PRO
SEQRES 1 B 224 MET SER HIS HIS HIS HIS HIS HIS SER MET VAL ASN LYS
SEQRES 2 B 224 ARG MET SER MET VAL VAL SER GLY LEU THR PRO GLU GLU
SEQRES 3 B 224 PHE MET LEU VAL TYR LYS PHE ALA ARG LYS HIS HIS ILE
SEQRES 4 B 224 THR LEU THR ASN LEU ILE THR GLU GLU THR THR HIS VAL
SEQRES 5 B 224 VAL MET LYS THR ASP ALA GLU PHE VAL CYS GLU ARG THR
SEQRES 6 B 224 LEU LYS TYR PHE LEU GLY ILE ALA GLY GLY LYS TRP VAL
SEQRES 7 B 224 VAL SER TYR PHE TRP VAL THR GLN SER ILE LYS GLU ARG
SEQRES 8 B 224 LYS MET LEU ASN GLU HIS ASP PHE GLU VAL ARG GLY ASP
SEQRES 9 B 224 VAL VAL ASN GLY ARG ASN HIS GLN GLY PRO LYS ARG ALA
SEQRES 10 B 224 ARG GLU SER GLN ASP ARG LYS ILE PHE ARG GLY LEU GLU
SEQRES 11 B 224 ILE CYS CYS TYR GLY PRO PHE THR ASN MET PRO THR ASP
SEQRES 12 B 224 GLN LEU GLU TRP MET VAL GLN LEU CYS GLY ALA SER VAL
SEQRES 13 B 224 VAL LYS GLU LEU SER SER PHE THR LEU GLY THR GLY VAL
SEQRES 14 B 224 HIS PRO ILE VAL VAL VAL GLN PRO ASP ALA TRP THR GLU
SEQRES 15 B 224 ASP ASN GLY PHE HIS ALA ILE GLY GLN MET CYS GLU ALA
SEQRES 16 B 224 PRO VAL VAL THR ARG GLU TRP VAL LEU ASP SER VAL ALA
SEQRES 17 B 224 LEU TYR GLN CYS GLN GLU LEU ASP THR TYR LEU ILE PRO
SEQRES 18 B 224 GLN ILE PRO
SEQRES 1 C 224 MET SER HIS HIS HIS HIS HIS HIS SER MET VAL ASN LYS
SEQRES 2 C 224 ARG MET SER MET VAL VAL SER GLY LEU THR PRO GLU GLU
SEQRES 3 C 224 PHE MET LEU VAL TYR LYS PHE ALA ARG LYS HIS HIS ILE
SEQRES 4 C 224 THR LEU THR ASN LEU ILE THR GLU GLU THR THR HIS VAL
SEQRES 5 C 224 VAL MET LYS THR ASP ALA GLU PHE VAL CYS GLU ARG THR
SEQRES 6 C 224 LEU LYS TYR PHE LEU GLY ILE ALA GLY GLY LYS TRP VAL
SEQRES 7 C 224 VAL SER TYR PHE TRP VAL THR GLN SER ILE LYS GLU ARG
SEQRES 8 C 224 LYS MET LEU ASN GLU HIS ASP PHE GLU VAL ARG GLY ASP
SEQRES 9 C 224 VAL VAL ASN GLY ARG ASN HIS GLN GLY PRO LYS ARG ALA
SEQRES 10 C 224 ARG GLU SER GLN ASP ARG LYS ILE PHE ARG GLY LEU GLU
SEQRES 11 C 224 ILE CYS CYS TYR GLY PRO PHE THR ASN MET PRO THR ASP
SEQRES 12 C 224 GLN LEU GLU TRP MET VAL GLN LEU CYS GLY ALA SER VAL
SEQRES 13 C 224 VAL LYS GLU LEU SER SER PHE THR LEU GLY THR GLY VAL
SEQRES 14 C 224 HIS PRO ILE VAL VAL VAL GLN PRO ASP ALA TRP THR GLU
SEQRES 15 C 224 ASP ASN GLY PHE HIS ALA ILE GLY GLN MET CYS GLU ALA
SEQRES 16 C 224 PRO VAL VAL THR ARG GLU TRP VAL LEU ASP SER VAL ALA
SEQRES 17 C 224 LEU TYR GLN CYS GLN GLU LEU ASP THR TYR LEU ILE PRO
SEQRES 18 C 224 GLN ILE PRO
SEQRES 1 D 224 MET SER HIS HIS HIS HIS HIS HIS SER MET VAL ASN LYS
SEQRES 2 D 224 ARG MET SER MET VAL VAL SER GLY LEU THR PRO GLU GLU
SEQRES 3 D 224 PHE MET LEU VAL TYR LYS PHE ALA ARG LYS HIS HIS ILE
SEQRES 4 D 224 THR LEU THR ASN LEU ILE THR GLU GLU THR THR HIS VAL
SEQRES 5 D 224 VAL MET LYS THR ASP ALA GLU PHE VAL CYS GLU ARG THR
SEQRES 6 D 224 LEU LYS TYR PHE LEU GLY ILE ALA GLY GLY LYS TRP VAL
SEQRES 7 D 224 VAL SER TYR PHE TRP VAL THR GLN SER ILE LYS GLU ARG
SEQRES 8 D 224 LYS MET LEU ASN GLU HIS ASP PHE GLU VAL ARG GLY ASP
SEQRES 9 D 224 VAL VAL ASN GLY ARG ASN HIS GLN GLY PRO LYS ARG ALA
SEQRES 10 D 224 ARG GLU SER GLN ASP ARG LYS ILE PHE ARG GLY LEU GLU
SEQRES 11 D 224 ILE CYS CYS TYR GLY PRO PHE THR ASN MET PRO THR ASP
SEQRES 12 D 224 GLN LEU GLU TRP MET VAL GLN LEU CYS GLY ALA SER VAL
SEQRES 13 D 224 VAL LYS GLU LEU SER SER PHE THR LEU GLY THR GLY VAL
SEQRES 14 D 224 HIS PRO ILE VAL VAL VAL GLN PRO ASP ALA TRP THR GLU
SEQRES 15 D 224 ASP ASN GLY PHE HIS ALA ILE GLY GLN MET CYS GLU ALA
SEQRES 16 D 224 PRO VAL VAL THR ARG GLU TRP VAL LEU ASP SER VAL ALA
SEQRES 17 D 224 LEU TYR GLN CYS GLN GLU LEU ASP THR TYR LEU ILE PRO
SEQRES 18 D 224 GLN ILE PRO
SEQRES 1 E 224 MET SER HIS HIS HIS HIS HIS HIS SER MET VAL ASN LYS
SEQRES 2 E 224 ARG MET SER MET VAL VAL SER GLY LEU THR PRO GLU GLU
SEQRES 3 E 224 PHE MET LEU VAL TYR LYS PHE ALA ARG LYS HIS HIS ILE
SEQRES 4 E 224 THR LEU THR ASN LEU ILE THR GLU GLU THR THR HIS VAL
SEQRES 5 E 224 VAL MET LYS THR ASP ALA GLU PHE VAL CYS GLU ARG THR
SEQRES 6 E 224 LEU LYS TYR PHE LEU GLY ILE ALA GLY GLY LYS TRP VAL
SEQRES 7 E 224 VAL SER TYR PHE TRP VAL THR GLN SER ILE LYS GLU ARG
SEQRES 8 E 224 LYS MET LEU ASN GLU HIS ASP PHE GLU VAL ARG GLY ASP
SEQRES 9 E 224 VAL VAL ASN GLY ARG ASN HIS GLN GLY PRO LYS ARG ALA
SEQRES 10 E 224 ARG GLU SER GLN ASP ARG LYS ILE PHE ARG GLY LEU GLU
SEQRES 11 E 224 ILE CYS CYS TYR GLY PRO PHE THR ASN MET PRO THR ASP
SEQRES 12 E 224 GLN LEU GLU TRP MET VAL GLN LEU CYS GLY ALA SER VAL
SEQRES 13 E 224 VAL LYS GLU LEU SER SER PHE THR LEU GLY THR GLY VAL
SEQRES 14 E 224 HIS PRO ILE VAL VAL VAL GLN PRO ASP ALA TRP THR GLU
SEQRES 15 E 224 ASP ASN GLY PHE HIS ALA ILE GLY GLN MET CYS GLU ALA
SEQRES 16 E 224 PRO VAL VAL THR ARG GLU TRP VAL LEU ASP SER VAL ALA
SEQRES 17 E 224 LEU TYR GLN CYS GLN GLU LEU ASP THR TYR LEU ILE PRO
SEQRES 18 E 224 GLN ILE PRO
SEQRES 1 F 224 MET SER HIS HIS HIS HIS HIS HIS SER MET VAL ASN LYS
SEQRES 2 F 224 ARG MET SER MET VAL VAL SER GLY LEU THR PRO GLU GLU
SEQRES 3 F 224 PHE MET LEU VAL TYR LYS PHE ALA ARG LYS HIS HIS ILE
SEQRES 4 F 224 THR LEU THR ASN LEU ILE THR GLU GLU THR THR HIS VAL
SEQRES 5 F 224 VAL MET LYS THR ASP ALA GLU PHE VAL CYS GLU ARG THR
SEQRES 6 F 224 LEU LYS TYR PHE LEU GLY ILE ALA GLY GLY LYS TRP VAL
SEQRES 7 F 224 VAL SER TYR PHE TRP VAL THR GLN SER ILE LYS GLU ARG
SEQRES 8 F 224 LYS MET LEU ASN GLU HIS ASP PHE GLU VAL ARG GLY ASP
SEQRES 9 F 224 VAL VAL ASN GLY ARG ASN HIS GLN GLY PRO LYS ARG ALA
SEQRES 10 F 224 ARG GLU SER GLN ASP ARG LYS ILE PHE ARG GLY LEU GLU
SEQRES 11 F 224 ILE CYS CYS TYR GLY PRO PHE THR ASN MET PRO THR ASP
SEQRES 12 F 224 GLN LEU GLU TRP MET VAL GLN LEU CYS GLY ALA SER VAL
SEQRES 13 F 224 VAL LYS GLU LEU SER SER PHE THR LEU GLY THR GLY VAL
SEQRES 14 F 224 HIS PRO ILE VAL VAL VAL GLN PRO ASP ALA TRP THR GLU
SEQRES 15 F 224 ASP ASN GLY PHE HIS ALA ILE GLY GLN MET CYS GLU ALA
SEQRES 16 F 224 PRO VAL VAL THR ARG GLU TRP VAL LEU ASP SER VAL ALA
SEQRES 17 F 224 LEU TYR GLN CYS GLN GLU LEU ASP THR TYR LEU ILE PRO
SEQRES 18 F 224 GLN ILE PRO
SEQRES 1 G 224 MET SER HIS HIS HIS HIS HIS HIS SER MET VAL ASN LYS
SEQRES 2 G 224 ARG MET SER MET VAL VAL SER GLY LEU THR PRO GLU GLU
SEQRES 3 G 224 PHE MET LEU VAL TYR LYS PHE ALA ARG LYS HIS HIS ILE
SEQRES 4 G 224 THR LEU THR ASN LEU ILE THR GLU GLU THR THR HIS VAL
SEQRES 5 G 224 VAL MET LYS THR ASP ALA GLU PHE VAL CYS GLU ARG THR
SEQRES 6 G 224 LEU LYS TYR PHE LEU GLY ILE ALA GLY GLY LYS TRP VAL
SEQRES 7 G 224 VAL SER TYR PHE TRP VAL THR GLN SER ILE LYS GLU ARG
SEQRES 8 G 224 LYS MET LEU ASN GLU HIS ASP PHE GLU VAL ARG GLY ASP
SEQRES 9 G 224 VAL VAL ASN GLY ARG ASN HIS GLN GLY PRO LYS ARG ALA
SEQRES 10 G 224 ARG GLU SER GLN ASP ARG LYS ILE PHE ARG GLY LEU GLU
SEQRES 11 G 224 ILE CYS CYS TYR GLY PRO PHE THR ASN MET PRO THR ASP
SEQRES 12 G 224 GLN LEU GLU TRP MET VAL GLN LEU CYS GLY ALA SER VAL
SEQRES 13 G 224 VAL LYS GLU LEU SER SER PHE THR LEU GLY THR GLY VAL
SEQRES 14 G 224 HIS PRO ILE VAL VAL VAL GLN PRO ASP ALA TRP THR GLU
SEQRES 15 G 224 ASP ASN GLY PHE HIS ALA ILE GLY GLN MET CYS GLU ALA
SEQRES 16 G 224 PRO VAL VAL THR ARG GLU TRP VAL LEU ASP SER VAL ALA
SEQRES 17 G 224 LEU TYR GLN CYS GLN GLU LEU ASP THR TYR LEU ILE PRO
SEQRES 18 G 224 GLN ILE PRO
SEQRES 1 H 224 MET SER HIS HIS HIS HIS HIS HIS SER MET VAL ASN LYS
SEQRES 2 H 224 ARG MET SER MET VAL VAL SER GLY LEU THR PRO GLU GLU
SEQRES 3 H 224 PHE MET LEU VAL TYR LYS PHE ALA ARG LYS HIS HIS ILE
SEQRES 4 H 224 THR LEU THR ASN LEU ILE THR GLU GLU THR THR HIS VAL
SEQRES 5 H 224 VAL MET LYS THR ASP ALA GLU PHE VAL CYS GLU ARG THR
SEQRES 6 H 224 LEU LYS TYR PHE LEU GLY ILE ALA GLY GLY LYS TRP VAL
SEQRES 7 H 224 VAL SER TYR PHE TRP VAL THR GLN SER ILE LYS GLU ARG
SEQRES 8 H 224 LYS MET LEU ASN GLU HIS ASP PHE GLU VAL ARG GLY ASP
SEQRES 9 H 224 VAL VAL ASN GLY ARG ASN HIS GLN GLY PRO LYS ARG ALA
SEQRES 10 H 224 ARG GLU SER GLN ASP ARG LYS ILE PHE ARG GLY LEU GLU
SEQRES 11 H 224 ILE CYS CYS TYR GLY PRO PHE THR ASN MET PRO THR ASP
SEQRES 12 H 224 GLN LEU GLU TRP MET VAL GLN LEU CYS GLY ALA SER VAL
SEQRES 13 H 224 VAL LYS GLU LEU SER SER PHE THR LEU GLY THR GLY VAL
SEQRES 14 H 224 HIS PRO ILE VAL VAL VAL GLN PRO ASP ALA TRP THR GLU
SEQRES 15 H 224 ASP ASN GLY PHE HIS ALA ILE GLY GLN MET CYS GLU ALA
SEQRES 16 H 224 PRO VAL VAL THR ARG GLU TRP VAL LEU ASP SER VAL ALA
SEQRES 17 H 224 LEU TYR GLN CYS GLN GLU LEU ASP THR TYR LEU ILE PRO
SEQRES 18 H 224 GLN ILE PRO
SEQRES 1 I 11 GLY PHE GLY GLU TYR SEP ARG SEP PRO THR PHE
SEQRES 1 J 11 GLY PHE GLY GLU TYR SEP ARG SEP PRO THR PHE
SEQRES 1 K 11 GLY PHE GLY GLU TYR SEP ARG SEP PRO THR PHE
SEQRES 1 L 11 GLY PHE GLY GLU TYR SEP ARG SEP PRO THR PHE
SEQRES 1 M 11 GLY PHE GLY GLU TYR SEP ARG SEP PRO THR PHE
SEQRES 1 N 11 GLY PHE GLY GLU TYR SEP ARG SEP PRO THR PHE
SEQRES 1 O 11 GLY PHE GLY GLU TYR SEP ARG SEP PRO THR PHE
SEQRES 1 P 11 GLY PHE GLY GLU TYR SEP ARG SEP PRO THR PHE
MODRES 4Y18 SEP I 404 SER MODIFIED RESIDUE
MODRES 4Y18 SEP I 406 SER MODIFIED RESIDUE
MODRES 4Y18 SEP J 404 SER MODIFIED RESIDUE
MODRES 4Y18 SEP J 406 SER MODIFIED RESIDUE
MODRES 4Y18 SEP K 404 SER MODIFIED RESIDUE
MODRES 4Y18 SEP K 406 SER MODIFIED RESIDUE
MODRES 4Y18 SEP L 404 SER MODIFIED RESIDUE
MODRES 4Y18 SEP L 406 SER MODIFIED RESIDUE
MODRES 4Y18 SEP M 404 SER MODIFIED RESIDUE
MODRES 4Y18 SEP M 406 SER MODIFIED RESIDUE
MODRES 4Y18 SEP N 404 SER MODIFIED RESIDUE
MODRES 4Y18 SEP N 406 SER MODIFIED RESIDUE
MODRES 4Y18 SEP O 404 SER MODIFIED RESIDUE
MODRES 4Y18 SEP O 406 SER MODIFIED RESIDUE
MODRES 4Y18 SEP P 404 SER MODIFIED RESIDUE
MODRES 4Y18 SEP P 406 SER MODIFIED RESIDUE
HET SEP I 404 10
HET SEP I 406 10
HET SEP J 404 10
HET SEP J 406 10
HET SEP K 404 10
HET SEP K 406 10
HET SEP L 404 10
HET SEP L 406 10
HET SEP M 404 10
HET SEP M 406 10
HET SEP N 404 10
HET SEP N 406 10
HET SEP O 404 10
HET SEP O 406 10
HET SEP P 404 10
HET SEP P 406 10
HETNAM SEP PHOSPHOSERINE
HETSYN SEP PHOSPHONOSERINE
FORMUL 9 SEP 16(C3 H8 N O6 P)
FORMUL 17 HOH *(H2 O)
HELIX 1 AA1 THR A 1658 HIS A 1672 1 15
HELIX 2 AA2 THR A 1700 GLY A 1709 1 10
HELIX 3 AA3 TYR A 1716 ARG A 1726 1 11
HELIX 4 AA4 ASN A 1730 GLU A 1735 5 6
HELIX 5 AA5 GLN A 1747 GLU A 1754 1 8
HELIX 6 AA6 PRO A 1776 CYS A 1787 1 12
HELIX 7 AA7 GLU A 1794 PHE A 1798 5 5
HELIX 8 AA8 GLN A 1811 TRP A 1815 5 5
HELIX 9 AA9 ASN A 1819 MET A 1827 5 9
HELIX 10 AB1 ARG A 1835 TYR A 1845 1 11
HELIX 11 AB2 GLU A 1849 LEU A 1854 5 6
HELIX 12 AB3 THR B 1658 HIS B 1672 1 15
HELIX 13 AB4 THR B 1700 GLY B 1709 1 10
HELIX 14 AB5 TYR B 1716 GLU B 1725 1 10
HELIX 15 AB6 ASN B 1730 GLU B 1735 5 6
HELIX 16 AB7 GLN B 1747 SER B 1755 1 9
HELIX 17 AB8 PRO B 1776 CYS B 1787 1 12
HELIX 18 AB9 GLU B 1794 PHE B 1798 5 5
HELIX 19 AC1 GLN B 1811 TRP B 1815 5 5
HELIX 20 AC2 ASN B 1819 MET B 1827 5 9
HELIX 21 AC3 ARG B 1835 TYR B 1845 1 11
HELIX 22 AC4 GLU B 1849 LEU B 1854 5 6
HELIX 23 AC5 THR C 1658 HIS C 1672 1 15
HELIX 24 AC6 THR C 1700 GLY C 1709 1 10
HELIX 25 AC7 TYR C 1716 ARG C 1726 1 11
HELIX 26 AC8 ASN C 1730 GLU C 1735 5 6
HELIX 27 AC9 GLN C 1747 SER C 1755 1 9
HELIX 28 AD1 PRO C 1776 CYS C 1787 1 12
HELIX 29 AD2 GLU C 1794 PHE C 1798 5 5
HELIX 30 AD3 GLN C 1811 TRP C 1815 5 5
HELIX 31 AD4 ASN C 1819 MET C 1827 5 9
HELIX 32 AD5 ARG C 1835 TYR C 1845 1 11
HELIX 33 AD6 GLU C 1849 LEU C 1854 5 6
HELIX 34 AD7 THR D 1658 HIS D 1672 1 15
HELIX 35 AD8 THR D 1700 GLY D 1709 1 10
HELIX 36 AD9 TYR D 1716 ARG D 1726 1 11
HELIX 37 AE1 ASN D 1730 GLU D 1735 5 6
HELIX 38 AE2 GLN D 1747 SER D 1755 1 9
HELIX 39 AE3 GLN D 1756 LYS D 1759 5 4
HELIX 40 AE4 PRO D 1776 CYS D 1787 1 12
HELIX 41 AE5 GLU D 1794 PHE D 1798 5 5
HELIX 42 AE6 ASN D 1819 MET D 1827 5 9
HELIX 43 AE7 ARG D 1835 TYR D 1845 1 11
HELIX 44 AE8 GLU D 1849 LEU D 1854 5 6
HELIX 45 AE9 THR E 1658 HIS E 1673 1 16
HELIX 46 AF1 THR E 1700 GLY E 1709 1 10
HELIX 47 AF2 TYR E 1716 GLU E 1725 1 10
HELIX 48 AF3 ASN E 1730 GLU E 1735 5 6
HELIX 49 AF4 GLN E 1747 SER E 1755 1 9
HELIX 50 AF5 GLN E 1756 LYS E 1759 5 4
HELIX 51 AF6 PRO E 1776 CYS E 1787 1 12
HELIX 52 AF7 GLU E 1794 PHE E 1798 5 5
HELIX 53 AF8 GLN E 1811 TRP E 1815 5 5
HELIX 54 AF9 ASN E 1819 MET E 1827 5 9
HELIX 55 AG1 ARG E 1835 TYR E 1845 1 11
HELIX 56 AG2 GLU E 1849 LEU E 1854 5 6
HELIX 57 AG3 THR F 1658 HIS F 1672 1 15
HELIX 58 AG4 THR F 1700 GLY F 1709 1 10
HELIX 59 AG5 TYR F 1716 ARG F 1726 1 11
HELIX 60 AG6 ASN F 1730 GLU F 1735 5 6
HELIX 61 AG7 GLN F 1747 SER F 1755 1 9
HELIX 62 AG8 PRO F 1776 CYS F 1787 1 12
HELIX 63 AG9 GLU F 1794 PHE F 1798 5 5
HELIX 64 AH1 ASN F 1819 MET F 1827 5 9
HELIX 65 AH2 ARG F 1835 TYR F 1845 1 11
HELIX 66 AH3 GLU F 1849 LEU F 1854 5 6
HELIX 67 AH4 THR G 1658 HIS G 1672 1 15
HELIX 68 AH5 THR G 1700 GLY G 1709 1 10
HELIX 69 AH6 TYR G 1716 ARG G 1726 1 11
HELIX 70 AH7 ASN G 1730 GLU G 1735 5 6
HELIX 71 AH8 GLN G 1747 SER G 1755 1 9
HELIX 72 AH9 PRO G 1776 CYS G 1787 1 12
HELIX 73 AI1 GLU G 1794 PHE G 1798 5 5
HELIX 74 AI2 GLN G 1811 TRP G 1815 5 5
HELIX 75 AI3 ASN G 1819 HIS G 1822 5 4
HELIX 76 AI4 ALA G 1823 CYS G 1828 1 6
HELIX 77 AI5 ARG G 1835 TYR G 1845 1 11
HELIX 78 AI6 GLU G 1849 LEU G 1854 5 6
HELIX 79 AI7 THR H 1658 HIS H 1672 1 15
HELIX 80 AI8 THR H 1700 GLY H 1709 1 10
HELIX 81 AI9 TYR H 1716 ARG H 1726 1 11
HELIX 82 AJ1 ASN H 1730 GLU H 1735 5 6
HELIX 83 AJ2 GLN H 1747 SER H 1755 1 9
HELIX 84 AJ3 PRO H 1776 CYS H 1787 1 12
HELIX 85 AJ4 GLU H 1794 PHE H 1798 5 5
HELIX 86 AJ5 GLN H 1811 TRP H 1815 5 5
HELIX 87 AJ6 ASN H 1819 MET H 1827 5 9
HELIX 88 AJ7 ARG H 1835 TYR H 1845 1 11
HELIX 89 AJ8 GLU H 1849 LEU H 1854 5 6
SHEET 1 AA1 4 THR A1675 LEU A1676 0
SHEET 2 AA1 4 SER A1651 SER A1655 1 N MET A1652 O THR A1675
SHEET 3 AA1 4 HIS A1686 MET A1689 1 O VAL A1688 N SER A1655
SHEET 4 AA1 4 TRP A1712 SER A1715 1 O TRP A1712 N VAL A1687
SHEET 1 AA2 2 VAL A1696 CYS A1697 0
SHEET 2 AA2 2 GLY A1738 ASP A1739 1 O GLY A1738 N CYS A1697
SHEET 1 AA3 4 SER A1790 VAL A1791 0
SHEET 2 AA3 4 LEU A1764 CYS A1768 1 N LEU A1764 O SER A1790
SHEET 3 AA3 4 HIS A1805 VAL A1810 1 O ILE A1807 N CYS A1767
SHEET 4 AA3 4 VAL A1832 THR A1834 1 O VAL A1833 N VAL A1808
SHEET 1 AA4 4 THR B1675 LEU B1676 0
SHEET 2 AA4 4 SER B1651 SER B1655 1 N MET B1652 O THR B1675
SHEET 3 AA4 4 HIS B1686 MET B1689 1 O VAL B1688 N SER B1655
SHEET 4 AA4 4 TRP B1712 SER B1715 1 O VAL B1714 N MET B1689
SHEET 1 AA5 2 VAL B1696 CYS B1697 0
SHEET 2 AA5 2 GLY B1738 ASP B1739 1 O GLY B1738 N CYS B1697
SHEET 1 AA6 4 SER B1790 VAL B1791 0
SHEET 2 AA6 4 LEU B1764 CYS B1768 1 N LEU B1764 O SER B1790
SHEET 3 AA6 4 HIS B1805 VAL B1810 1 O ILE B1807 N GLU B1765
SHEET 4 AA6 4 VAL B1832 THR B1834 1 O VAL B1833 N VAL B1808
SHEET 1 AA7 4 THR C1675 LEU C1676 0
SHEET 2 AA7 4 SER C1651 SER C1655 1 N MET C1652 O THR C1675
SHEET 3 AA7 4 HIS C1686 MET C1689 1 O VAL C1688 N VAL C1653
SHEET 4 AA7 4 TRP C1712 SER C1715 1 O VAL C1714 N MET C1689
SHEET 1 AA8 2 VAL C1696 CYS C1697 0
SHEET 2 AA8 2 GLY C1738 ASP C1739 1 O GLY C1738 N CYS C1697
SHEET 1 AA9 4 SER C1790 VAL C1791 0
SHEET 2 AA9 4 LEU C1764 CYS C1768 1 N LEU C1764 O SER C1790
SHEET 3 AA9 4 HIS C1805 VAL C1810 1 O ILE C1807 N GLU C1765
SHEET 4 AA9 4 VAL C1832 THR C1834 1 O VAL C1833 N VAL C1808
SHEET 1 AB1 4 THR D1675 LEU D1676 0
SHEET 2 AB1 4 SER D1651 SER D1655 1 N MET D1652 O THR D1675
SHEET 3 AB1 4 HIS D1686 MET D1689 1 O VAL D1688 N VAL D1653
SHEET 4 AB1 4 TRP D1712 SER D1715 1 O TRP D1712 N VAL D1687
SHEET 1 AB2 2 VAL D1696 CYS D1697 0
SHEET 2 AB2 2 GLY D1738 ASP D1739 1 O GLY D1738 N CYS D1697
SHEET 1 AB3 4 SER D1790 VAL D1791 0
SHEET 2 AB3 4 LEU D1764 CYS D1768 1 N LEU D1764 O SER D1790
SHEET 3 AB3 4 HIS D1805 VAL D1810 1 O HIS D1805 N GLU D1765
SHEET 4 AB3 4 VAL D1832 THR D1834 1 O VAL D1833 N VAL D1808
SHEET 1 AB4 4 THR E1675 LEU E1676 0
SHEET 2 AB4 4 SER E1651 SER E1655 1 N MET E1652 O THR E1675
SHEET 3 AB4 4 HIS E1686 MET E1689 1 O VAL E1688 N VAL E1653
SHEET 4 AB4 4 TRP E1712 SER E1715 1 O VAL E1714 N MET E1689
SHEET 1 AB5 2 VAL E1696 CYS E1697 0
SHEET 2 AB5 2 GLY E1738 ASP E1739 1 O GLY E1738 N CYS E1697
SHEET 1 AB6 4 SER E1790 VAL E1791 0
SHEET 2 AB6 4 GLU E1765 CYS E1768 1 N ILE E1766 O SER E1790
SHEET 3 AB6 4 PRO E1806 VAL E1810 1 O ILE E1807 N CYS E1767
SHEET 4 AB6 4 VAL E1832 THR E1834 1 O VAL E1833 N VAL E1808
SHEET 1 AB7 4 THR F1675 LEU F1676 0
SHEET 2 AB7 4 SER F1651 SER F1655 1 N MET F1652 O THR F1675
SHEET 3 AB7 4 HIS F1686 MET F1689 1 O VAL F1688 N SER F1655
SHEET 4 AB7 4 TRP F1712 SER F1715 1 O VAL F1714 N MET F1689
SHEET 1 AB8 2 VAL F1696 CYS F1697 0
SHEET 2 AB8 2 GLY F1738 ASP F1739 1 O GLY F1738 N CYS F1697
SHEET 1 AB9 4 SER F1790 VAL F1792 0
SHEET 2 AB9 4 LEU F1764 TYR F1769 1 N LEU F1764 O SER F1790
SHEET 3 AB9 4 HIS F1805 VAL F1810 1 O ILE F1807 N GLU F1765
SHEET 4 AB9 4 VAL F1832 THR F1834 1 O VAL F1833 N VAL F1810
SHEET 1 AC1 4 THR G1675 THR G1677 0
SHEET 2 AC1 4 SER G1651 SER G1655 1 N MET G1652 O THR G1675
SHEET 3 AC1 4 HIS G1686 MET G1689 1 O VAL G1688 N VAL G1653
SHEET 4 AC1 4 TRP G1712 SER G1715 1 O TRP G1712 N VAL G1687
SHEET 1 AC2 2 VAL G1696 CYS G1697 0
SHEET 2 AC2 2 GLY G1738 ASP G1739 1 O GLY G1738 N CYS G1697
SHEET 1 AC3 4 SER G1790 VAL G1791 0
SHEET 2 AC3 4 LEU G1764 CYS G1768 1 N LEU G1764 O SER G1790
SHEET 3 AC3 4 HIS G1805 VAL G1810 1 O HIS G1805 N GLU G1765
SHEET 4 AC3 4 VAL G1832 THR G1834 1 O VAL G1833 N VAL G1808
SHEET 1 AC4 4 THR H1675 THR H1677 0
SHEET 2 AC4 4 SER H1651 SER H1655 1 N MET H1652 O THR H1675
SHEET 3 AC4 4 HIS H1686 MET H1689 1 O VAL H1688 N VAL H1653
SHEET 4 AC4 4 TRP H1712 SER H1715 1 O TRP H1712 N VAL H1687
SHEET 1 AC5 2 VAL H1696 CYS H1697 0
SHEET 2 AC5 2 GLY H1738 ASP H1739 1 O GLY H1738 N CYS H1697
SHEET 1 AC6 4 SER H1790 VAL H1791 0
SHEET 2 AC6 4 LEU H1764 CYS H1768 1 N LEU H1764 O SER H1790
SHEET 3 AC6 4 HIS H1805 VAL H1810 1 O HIS H1805 N GLU H1765
SHEET 4 AC6 4 VAL H1832 THR H1834 1 O VAL H1833 N VAL H1808
LINK C TYR I 403 N SEP I 404 1555 1555 1.33
LINK C SEP I 404 N ARG I 405 1555 1555 1.32
LINK C ARG I 405 N SEP I 406 1555 1555 1.33
LINK C SEP I 406 N PRO I 407 1555 1555 1.33
LINK C TYR J 403 N SEP J 404 1555 1555 1.33
LINK C SEP J 404 N ARG J 405 1555 1555 1.33
LINK C ARG J 405 N SEP J 406 1555 1555 1.33
LINK C SEP J 406 N PRO J 407 1555 1555 1.33
LINK C TYR K 403 N SEP K 404 1555 1555 1.32
LINK C SEP K 404 N ARG K 405 1555 1555 1.32
LINK C ARG K 405 N SEP K 406 1555 1555 1.33
LINK C SEP K 406 N PRO K 407 1555 1555 1.33
LINK C TYR L 403 N SEP L 404 1555 1555 1.33
LINK C SEP L 404 N ARG L 405 1555 1555 1.33
LINK C ARG L 405 N SEP L 406 1555 1555 1.33
LINK C SEP L 406 N PRO L 407 1555 1555 1.33
LINK C TYR M 403 N SEP M 404 1555 1555 1.32
LINK C SEP M 404 N ARG M 405 1555 1555 1.32
LINK C ARG M 405 N SEP M 406 1555 1555 1.32
LINK C SEP M 406 N PRO M 407 1555 1555 1.32
LINK C TYR N 403 N SEP N 404 1555 1555 1.33
LINK C SEP N 404 N ARG N 405 1555 1555 1.33
LINK C ARG N 405 N SEP N 406 1555 1555 1.33
LINK C SEP N 406 N PRO N 407 1555 1555 1.33
LINK C TYR O 403 N SEP O 404 1555 1555 1.33
LINK C SEP O 404 N ARG O 405 1555 1555 1.33
LINK C ARG O 405 N SEP O 406 1555 1555 1.33
LINK C SEP O 406 N PRO O 407 1555 1555 1.33
LINK C TYR P 403 N SEP P 404 1555 1555 1.33
LINK C SEP P 404 N ARG P 405 1555 1555 1.32
LINK C ARG P 405 N SEP P 406 1555 1555 1.33
LINK C SEP P 406 N PRO P 407 1555 1555 1.34
CISPEP 1 GLY A 1770 PRO A 1771 0 3.46
CISPEP 2 GLY B 1770 PRO B 1771 0 3.28
CISPEP 3 GLY C 1770 PRO C 1771 0 2.60
CISPEP 4 GLY D 1770 PRO D 1771 0 3.37
CISPEP 5 GLY E 1770 PRO E 1771 0 3.68
CISPEP 6 GLY F 1770 PRO F 1771 0 2.18
CISPEP 7 GLY G 1770 PRO G 1771 0 3.31
CISPEP 8 GLY H 1770 PRO H 1771 0 3.77
CRYST1 86.819 183.726 190.510 90.00 90.00 90.00 P 21 21 21 32
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 0.011518 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005443 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005249 0.00000
(ATOM LINES ARE NOT SHOWN.)
END