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HEADER IMMUNE SYSTEM 27-OCT-16 5TS1
TITLE CRYSTAL STRUCTURE OF MHC-I H2-KD COMPLEXED WITH PEPTIDES OF
TITLE 2 MYCOBACTERIAL TUBERCULOSIS (YYQSGLSIV)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: H-2 CLASS I HISTOCOMPATIBILITY ANTIGEN, K-D ALPHA CHAIN;
COMPND 3 CHAIN: A, C, E, G;
COMPND 4 FRAGMENT: UNP RESIDUES 23-297;
COMPND 5 SYNONYM: H-2K(D);
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: BETA-2-MICROGLOBULIN;
COMPND 9 CHAIN: B, D, F, H;
COMPND 10 FRAGMENT: RESIDUES 21-119;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: PEPTIDE (P9) OF MTB85B (MYCOBACTERIUM TUBERCULOSIS)
COMPND 14 YYQSGLSIV;
COMPND 15 CHAIN: P, Q, R, S;
COMPND 16 FRAGMENT: UNP RESIDUES 101-109;
COMPND 17 SYNONYM: DGAT,30 KDA EXTRACELLULAR PROTEIN,ACYL-COA:DIACYLGLYCEROL
COMPND 18 ACYLTRANSFERASE,ANTIGEN 85 COMPLEX B,AG85B,EXTRACELLULAR ALPHA-
COMPND 19 ANTIGEN,FIBRONECTIN-BINDING PROTEIN B,FBPS B;
COMPND 20 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: H2-K1, H2-K;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21-B;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: B2M, CDABP0092, HDCMA22P;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET3A;
SOURCE 21 MOL_ID: 3;
SOURCE 22 SYNTHETIC: YES;
SOURCE 23 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 24 ORGANISM_TAXID: 83332
KEYWDS MAJOR HISTOMPATIBILITY COMPLEX CLASS I, MHC-I, H2-KD, H-2KD,
KEYWDS 2 MYCOBACTERIAL TUBERCULOSIS, TB PEPTIDE, MTB85B, MTB85A, MKAN85B,
KEYWDS 3 IMMUNE RESPONSE, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR J.JIANG,K.NATARAJAN,D.MARGULIES
REVDAT 3 05-FEB-20 5TS1 1 REMARK ATOM
REVDAT 2 14-AUG-19 5TS1 1 JRNL
REVDAT 1 09-MAY-18 5TS1 0
JRNL AUTH S.KOMINE-AIZAWA,J.JIANG,S.MIZUNO,S.HAYAKAWA,K.MATSUO,
JRNL AUTH 2 L.F.BOYD,D.H.MARGULIES,M.HONDA
JRNL TITL MHC-RESTRICTED AG85B-SPECIFIC CD8+T CELLS ARE ENHANCED BY
JRNL TITL 2 RECOMBINANT BCG PRIME AND DNA BOOST IMMUNIZATION IN MICE.
JRNL REF EUR.J.IMMUNOL. 2019
JRNL REFN ISSN 0014-2980
JRNL PMID 31135967
JRNL DOI 10.1002/EJI.201847988
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.10.1_2155
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.20
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 78047
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.090
REMARK 3 FREE R VALUE TEST SET COUNT : 3975
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 46.7080 - 6.2386 0.94 3749 198 0.2285 0.2531
REMARK 3 2 6.2386 - 4.9535 0.94 3745 197 0.1702 0.1781
REMARK 3 3 4.9535 - 4.3279 0.94 3708 195 0.1444 0.1784
REMARK 3 4 4.3279 - 3.9324 0.94 3714 196 0.1508 0.1908
REMARK 3 5 3.9324 - 3.6507 0.94 3745 197 0.1680 0.1980
REMARK 3 6 3.6507 - 3.4355 0.94 3722 196 0.1744 0.1948
REMARK 3 7 3.4355 - 3.2635 0.94 3725 196 0.1776 0.2022
REMARK 3 8 3.2635 - 3.1215 0.93 3697 194 0.1840 0.2181
REMARK 3 9 3.1215 - 3.0013 0.93 3728 196 0.1851 0.2438
REMARK 3 10 3.0013 - 2.8978 0.93 3732 197 0.1967 0.2327
REMARK 3 11 2.8978 - 2.8072 0.93 3662 193 0.1928 0.2283
REMARK 3 12 2.8072 - 2.7269 0.93 3717 195 0.2020 0.2632
REMARK 3 13 2.7269 - 2.6552 0.93 3673 194 0.2022 0.2561
REMARK 3 14 2.6552 - 2.5904 0.93 3720 195 0.2112 0.2701
REMARK 3 15 2.5904 - 2.5315 0.93 3688 194 0.2137 0.2411
REMARK 3 16 2.5315 - 2.4776 0.93 3668 193 0.2138 0.2686
REMARK 3 17 2.4776 - 2.4281 0.93 3731 197 0.2341 0.2939
REMARK 3 18 2.4281 - 2.3822 0.92 3661 193 0.2212 0.2958
REMARK 3 19 2.3822 - 2.3397 0.93 3658 192 0.2367 0.3015
REMARK 3 20 2.3397 - 2.3000 0.92 3696 195 0.2449 0.3199
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 : 0.34
REMARK 3 B_SOL : 21.60
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.590
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.70
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 13049
REMARK 3 ANGLE : 1.201 17720
REMARK 3 CHIRALITY : 0.071 1796
REMARK 3 PLANARITY : 0.009 2298
REMARK 3 DIHEDRAL : 20.419 7651
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 5TS1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-OCT-16.
REMARK 100 THE DEPOSITION ID IS D_1000224690.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-MAR-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0333
REMARK 200 MONOCHROMATOR : SI 100
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX300HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 78047
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 47.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.23200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.4
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 1.18000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 14% PEG 4000, 0.1M MES BUFFER, 5% MPD,
REMARK 280 PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18300 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, Q
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, R
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, S
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 LYS A 275
REMARK 465 PRO A 276
REMARK 465 LYS C 275
REMARK 465 PRO C 276
REMARK 465 LYS E 275
REMARK 465 PRO E 276
REMARK 465 LYS G 275
REMARK 465 PRO G 276
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 LEU A 219 CG CD1 CD2
REMARK 470 GLU A 222 CG CD OE1 OE2
REMARK 470 ASP A 223 CG OD1 OD2
REMARK 470 LEU A 224 CG CD1 CD2
REMARK 470 MET B 99 CG SD CE
REMARK 470 GLU C 222 CG CD OE1 OE2
REMARK 470 ASP C 223 CG OD1 OD2
REMARK 470 MET D 99 CG SD CE
REMARK 470 GLU E 222 CG CD OE1 OE2
REMARK 470 THR E 225 OG1 CG2
REMARK 470 MET F 99 CG SD CE
REMARK 470 GLU G 222 CG CD OE1 OE2
REMARK 470 ASP G 223 CG OD1 OD2
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 LEU E 130 NH2 ARG E 157 1.80
REMARK 500 O HOH C 463 O HOH C 487 1.98
REMARK 500 O GLN A 255 NH1 ARG A 273 2.00
REMARK 500 OE1 GLU A 128 O HOH A 401 2.00
REMARK 500 O HOH C 401 O HOH C 427 2.02
REMARK 500 O HOH A 431 O HOH A 492 2.02
REMARK 500 OE1 GLU C 232 OG SER D 28 2.06
REMARK 500 O ASN G 220 N GLU G 222 2.07
REMARK 500 OE2 GLU E 154 O HOH E 301 2.07
REMARK 500 O ARG G 66 O HOH G 401 2.08
REMARK 500 O HOH E 308 O HOH E 342 2.09
REMARK 500 O LYS C 186 O HOH C 401 2.09
REMARK 500 O ALA C 205 O HOH C 402 2.10
REMARK 500 OD1 ASN E 42 NH1 ARG E 44 2.13
REMARK 500 O GLN G 226 O HOH G 402 2.13
REMARK 500 OD1 ASP E 122 NE1 TRP F 60 2.15
REMARK 500 O ALA C 24 O HOH C 403 2.16
REMARK 500 O HOH C 447 O HOH C 460 2.16
REMARK 500 O HOH D 221 O HOH D 230 2.16
REMARK 500 OH TYR E 159 O HOH E 302 2.16
REMARK 500 O SER C 88 O HOH C 404 2.17
REMARK 500 NH1 ARG E 273 O HOH E 303 2.17
REMARK 500 O HOH C 485 O HOH D 209 2.17
REMARK 500 O ASN G 42 O HOH G 403 2.17
REMARK 500 NH2 ARG C 21 OD1 ASP C 37 2.18
REMARK 500 O LEU G 130 NH2 ARG G 157 2.18
REMARK 500 O HOH A 429 O HOH C 464 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 409 O HOH E 328 1656 2.01
REMARK 500 O HOH C 425 O HOH G 469 1645 2.10
REMARK 500 O HOH A 453 O HOH E 324 1646 2.11
REMARK 500 NH1 ARG A 111 OE1 GLU B 47 1655 2.15
REMARK 500 OE1 GLU E 128 N LYS F 48 1455 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 ARG G 35 CD ARG G 35 NE -0.148
REMARK 500 ARG G 35 NE ARG G 35 CZ -0.161
REMARK 500 ARG G 35 CZ ARG G 35 NH1 -0.149
REMARK 500 ARG G 35 CZ ARG G 35 NH2 -0.128
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU A 174 CA - CB - CG ANGL. DEV. = 16.2 DEGREES
REMARK 500 LEU A 251 CA - CB - CG ANGL. DEV. = 13.9 DEGREES
REMARK 500 LEU H 65 CA - CB - CG ANGL. DEV. = 15.0 DEGREES
REMARK 500 CYS H 80 CA - CB - SG ANGL. DEV. = 9.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 29 -122.39 57.12
REMARK 500 ASP A 41 -95.98 -28.61
REMARK 500 LYS B 48 42.24 71.07
REMARK 500 LEU P 6 -99.68 -101.72
REMARK 500 ASP C 29 -121.63 56.84
REMARK 500 SER C 195 -99.25 39.67
REMARK 500 GLN C 196 -4.29 -177.01
REMARK 500 ASN C 220 -98.38 2.99
REMARK 500 GLU C 222 72.11 54.73
REMARK 500 LYS D 48 77.46 85.06
REMARK 500 LEU Q 6 -98.61 -103.53
REMARK 500 ASP E 29 -121.73 56.73
REMARK 500 ASP E 41 -136.57 20.48
REMARK 500 PRO E 43 119.86 -37.65
REMARK 500 SER E 195 -151.07 -138.12
REMARK 500 LEU E 219 -75.17 -118.61
REMARK 500 LEU E 224 40.29 -98.67
REMARK 500 LEU R 6 -99.60 -101.44
REMARK 500 ASP G 29 -121.52 57.57
REMARK 500 SER G 195 -139.67 29.29
REMARK 500 ASN G 220 -177.35 59.63
REMARK 500 GLU G 222 80.15 63.48
REMARK 500 ASP G 227 9.40 -48.90
REMARK 500 LYS H 48 62.34 75.31
REMARK 500 LEU S 6 -99.55 -101.55
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 GLN C 226 ASP C 227 143.43
REMARK 500 SER E 195 GLN E 196 146.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL F 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL G 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL H 101
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5TRZ RELATED DB: PDB
DBREF 5TS1 A 2 276 UNP P01902 HA1D_MOUSE 23 297
DBREF 5TS1 B 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 5TS1 P 1 9 UNP P9WQP1 A85B_MYCTU 101 109
DBREF 5TS1 C 2 276 UNP P01902 HA1D_MOUSE 23 297
DBREF 5TS1 D 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 5TS1 Q 1 9 UNP P9WQP1 A85B_MYCTU 101 109
DBREF 5TS1 E 2 276 UNP P01902 HA1D_MOUSE 23 297
DBREF 5TS1 F 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 5TS1 R 1 9 UNP P9WQP1 A85B_MYCTU 101 109
DBREF 5TS1 G 2 276 UNP P01902 HA1D_MOUSE 23 297
DBREF 5TS1 H 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 5TS1 S 1 9 UNP P9WQP1 A85B_MYCTU 101 109
SEQADV 5TS1 HIS A 114 UNP P01902 GLN 135 CONFLICT
SEQADV 5TS1 PRO A 276 UNP P01902 LEU 297 CONFLICT
SEQADV 5TS1 MET B 0 UNP P61769 INITIATING METHIONINE
SEQADV 5TS1 HIS C 114 UNP P01902 GLN 135 CONFLICT
SEQADV 5TS1 PRO C 276 UNP P01902 LEU 297 CONFLICT
SEQADV 5TS1 MET D 0 UNP P61769 INITIATING METHIONINE
SEQADV 5TS1 HIS E 114 UNP P01902 GLN 135 CONFLICT
SEQADV 5TS1 PRO E 276 UNP P01902 LEU 297 CONFLICT
SEQADV 5TS1 MET F 0 UNP P61769 INITIATING METHIONINE
SEQADV 5TS1 HIS G 114 UNP P01902 GLN 135 CONFLICT
SEQADV 5TS1 PRO G 276 UNP P01902 LEU 297 CONFLICT
SEQADV 5TS1 MET H 0 UNP P61769 INITIATING METHIONINE
SEQRES 1 A 275 PRO HIS SER LEU ARG TYR PHE VAL THR ALA VAL SER ARG
SEQRES 2 A 275 PRO GLY LEU GLY GLU PRO ARG PHE ILE ALA VAL GLY TYR
SEQRES 3 A 275 VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER ASP ALA
SEQRES 4 A 275 ASP ASN PRO ARG PHE GLU PRO ARG ALA PRO TRP MET GLU
SEQRES 5 A 275 GLN GLU GLY PRO GLU TYR TRP GLU GLU GLN THR GLN ARG
SEQRES 6 A 275 ALA LYS SER ASP GLU GLN TRP PHE ARG VAL SER LEU ARG
SEQRES 7 A 275 THR ALA GLN ARG TYR TYR ASN GLN SER LYS GLY GLY SER
SEQRES 8 A 275 HIS THR PHE GLN ARG MET PHE GLY CYS ASP VAL GLY SER
SEQRES 9 A 275 ASP TRP ARG LEU LEU ARG GLY TYR HIS GLN PHE ALA TYR
SEQRES 10 A 275 ASP GLY ARG ASP TYR ILE ALA LEU ASN GLU ASP LEU LYS
SEQRES 11 A 275 THR TRP THR ALA ALA ASP THR ALA ALA LEU ILE THR ARG
SEQRES 12 A 275 ARG LYS TRP GLU GLN ALA GLY ASP ALA GLU TYR TYR ARG
SEQRES 13 A 275 ALA TYR LEU GLU GLY GLU CYS VAL GLU TRP LEU ARG ARG
SEQRES 14 A 275 TYR LEU GLU LEU GLY ASN GLU THR LEU LEU ARG THR ASP
SEQRES 15 A 275 SER PRO LYS ALA HIS VAL THR TYR HIS PRO ARG SER GLN
SEQRES 16 A 275 VAL ASP VAL THR LEU ARG CYS TRP ALA LEU GLY PHE TYR
SEQRES 17 A 275 PRO ALA ASP ILE THR LEU THR TRP GLN LEU ASN GLY GLU
SEQRES 18 A 275 ASP LEU THR GLN ASP MET GLU LEU VAL GLU THR ARG PRO
SEQRES 19 A 275 ALA GLY ASP GLY THR PHE GLN LYS TRP ALA ALA VAL VAL
SEQRES 20 A 275 VAL PRO LEU GLY LYS GLU GLN ASN TYR THR CYS HIS VAL
SEQRES 21 A 275 HIS HIS LYS GLY LEU PRO GLU PRO LEU THR LEU ARG TRP
SEQRES 22 A 275 LYS PRO
SEQRES 1 B 100 MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG
SEQRES 2 B 100 HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS
SEQRES 3 B 100 TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP
SEQRES 4 B 100 LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS
SEQRES 5 B 100 SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU
SEQRES 6 B 100 LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU
SEQRES 7 B 100 TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO
SEQRES 8 B 100 LYS ILE VAL LYS TRP ASP ARG ASP MET
SEQRES 1 P 9 TYR TYR GLN SER GLY LEU SER ILE VAL
SEQRES 1 C 275 PRO HIS SER LEU ARG TYR PHE VAL THR ALA VAL SER ARG
SEQRES 2 C 275 PRO GLY LEU GLY GLU PRO ARG PHE ILE ALA VAL GLY TYR
SEQRES 3 C 275 VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER ASP ALA
SEQRES 4 C 275 ASP ASN PRO ARG PHE GLU PRO ARG ALA PRO TRP MET GLU
SEQRES 5 C 275 GLN GLU GLY PRO GLU TYR TRP GLU GLU GLN THR GLN ARG
SEQRES 6 C 275 ALA LYS SER ASP GLU GLN TRP PHE ARG VAL SER LEU ARG
SEQRES 7 C 275 THR ALA GLN ARG TYR TYR ASN GLN SER LYS GLY GLY SER
SEQRES 8 C 275 HIS THR PHE GLN ARG MET PHE GLY CYS ASP VAL GLY SER
SEQRES 9 C 275 ASP TRP ARG LEU LEU ARG GLY TYR HIS GLN PHE ALA TYR
SEQRES 10 C 275 ASP GLY ARG ASP TYR ILE ALA LEU ASN GLU ASP LEU LYS
SEQRES 11 C 275 THR TRP THR ALA ALA ASP THR ALA ALA LEU ILE THR ARG
SEQRES 12 C 275 ARG LYS TRP GLU GLN ALA GLY ASP ALA GLU TYR TYR ARG
SEQRES 13 C 275 ALA TYR LEU GLU GLY GLU CYS VAL GLU TRP LEU ARG ARG
SEQRES 14 C 275 TYR LEU GLU LEU GLY ASN GLU THR LEU LEU ARG THR ASP
SEQRES 15 C 275 SER PRO LYS ALA HIS VAL THR TYR HIS PRO ARG SER GLN
SEQRES 16 C 275 VAL ASP VAL THR LEU ARG CYS TRP ALA LEU GLY PHE TYR
SEQRES 17 C 275 PRO ALA ASP ILE THR LEU THR TRP GLN LEU ASN GLY GLU
SEQRES 18 C 275 ASP LEU THR GLN ASP MET GLU LEU VAL GLU THR ARG PRO
SEQRES 19 C 275 ALA GLY ASP GLY THR PHE GLN LYS TRP ALA ALA VAL VAL
SEQRES 20 C 275 VAL PRO LEU GLY LYS GLU GLN ASN TYR THR CYS HIS VAL
SEQRES 21 C 275 HIS HIS LYS GLY LEU PRO GLU PRO LEU THR LEU ARG TRP
SEQRES 22 C 275 LYS PRO
SEQRES 1 D 100 MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG
SEQRES 2 D 100 HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS
SEQRES 3 D 100 TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP
SEQRES 4 D 100 LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS
SEQRES 5 D 100 SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU
SEQRES 6 D 100 LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU
SEQRES 7 D 100 TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO
SEQRES 8 D 100 LYS ILE VAL LYS TRP ASP ARG ASP MET
SEQRES 1 Q 9 TYR TYR GLN SER GLY LEU SER ILE VAL
SEQRES 1 E 275 PRO HIS SER LEU ARG TYR PHE VAL THR ALA VAL SER ARG
SEQRES 2 E 275 PRO GLY LEU GLY GLU PRO ARG PHE ILE ALA VAL GLY TYR
SEQRES 3 E 275 VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER ASP ALA
SEQRES 4 E 275 ASP ASN PRO ARG PHE GLU PRO ARG ALA PRO TRP MET GLU
SEQRES 5 E 275 GLN GLU GLY PRO GLU TYR TRP GLU GLU GLN THR GLN ARG
SEQRES 6 E 275 ALA LYS SER ASP GLU GLN TRP PHE ARG VAL SER LEU ARG
SEQRES 7 E 275 THR ALA GLN ARG TYR TYR ASN GLN SER LYS GLY GLY SER
SEQRES 8 E 275 HIS THR PHE GLN ARG MET PHE GLY CYS ASP VAL GLY SER
SEQRES 9 E 275 ASP TRP ARG LEU LEU ARG GLY TYR HIS GLN PHE ALA TYR
SEQRES 10 E 275 ASP GLY ARG ASP TYR ILE ALA LEU ASN GLU ASP LEU LYS
SEQRES 11 E 275 THR TRP THR ALA ALA ASP THR ALA ALA LEU ILE THR ARG
SEQRES 12 E 275 ARG LYS TRP GLU GLN ALA GLY ASP ALA GLU TYR TYR ARG
SEQRES 13 E 275 ALA TYR LEU GLU GLY GLU CYS VAL GLU TRP LEU ARG ARG
SEQRES 14 E 275 TYR LEU GLU LEU GLY ASN GLU THR LEU LEU ARG THR ASP
SEQRES 15 E 275 SER PRO LYS ALA HIS VAL THR TYR HIS PRO ARG SER GLN
SEQRES 16 E 275 VAL ASP VAL THR LEU ARG CYS TRP ALA LEU GLY PHE TYR
SEQRES 17 E 275 PRO ALA ASP ILE THR LEU THR TRP GLN LEU ASN GLY GLU
SEQRES 18 E 275 ASP LEU THR GLN ASP MET GLU LEU VAL GLU THR ARG PRO
SEQRES 19 E 275 ALA GLY ASP GLY THR PHE GLN LYS TRP ALA ALA VAL VAL
SEQRES 20 E 275 VAL PRO LEU GLY LYS GLU GLN ASN TYR THR CYS HIS VAL
SEQRES 21 E 275 HIS HIS LYS GLY LEU PRO GLU PRO LEU THR LEU ARG TRP
SEQRES 22 E 275 LYS PRO
SEQRES 1 F 100 MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG
SEQRES 2 F 100 HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS
SEQRES 3 F 100 TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP
SEQRES 4 F 100 LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS
SEQRES 5 F 100 SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU
SEQRES 6 F 100 LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU
SEQRES 7 F 100 TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO
SEQRES 8 F 100 LYS ILE VAL LYS TRP ASP ARG ASP MET
SEQRES 1 R 9 TYR TYR GLN SER GLY LEU SER ILE VAL
SEQRES 1 G 275 PRO HIS SER LEU ARG TYR PHE VAL THR ALA VAL SER ARG
SEQRES 2 G 275 PRO GLY LEU GLY GLU PRO ARG PHE ILE ALA VAL GLY TYR
SEQRES 3 G 275 VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER ASP ALA
SEQRES 4 G 275 ASP ASN PRO ARG PHE GLU PRO ARG ALA PRO TRP MET GLU
SEQRES 5 G 275 GLN GLU GLY PRO GLU TYR TRP GLU GLU GLN THR GLN ARG
SEQRES 6 G 275 ALA LYS SER ASP GLU GLN TRP PHE ARG VAL SER LEU ARG
SEQRES 7 G 275 THR ALA GLN ARG TYR TYR ASN GLN SER LYS GLY GLY SER
SEQRES 8 G 275 HIS THR PHE GLN ARG MET PHE GLY CYS ASP VAL GLY SER
SEQRES 9 G 275 ASP TRP ARG LEU LEU ARG GLY TYR HIS GLN PHE ALA TYR
SEQRES 10 G 275 ASP GLY ARG ASP TYR ILE ALA LEU ASN GLU ASP LEU LYS
SEQRES 11 G 275 THR TRP THR ALA ALA ASP THR ALA ALA LEU ILE THR ARG
SEQRES 12 G 275 ARG LYS TRP GLU GLN ALA GLY ASP ALA GLU TYR TYR ARG
SEQRES 13 G 275 ALA TYR LEU GLU GLY GLU CYS VAL GLU TRP LEU ARG ARG
SEQRES 14 G 275 TYR LEU GLU LEU GLY ASN GLU THR LEU LEU ARG THR ASP
SEQRES 15 G 275 SER PRO LYS ALA HIS VAL THR TYR HIS PRO ARG SER GLN
SEQRES 16 G 275 VAL ASP VAL THR LEU ARG CYS TRP ALA LEU GLY PHE TYR
SEQRES 17 G 275 PRO ALA ASP ILE THR LEU THR TRP GLN LEU ASN GLY GLU
SEQRES 18 G 275 ASP LEU THR GLN ASP MET GLU LEU VAL GLU THR ARG PRO
SEQRES 19 G 275 ALA GLY ASP GLY THR PHE GLN LYS TRP ALA ALA VAL VAL
SEQRES 20 G 275 VAL PRO LEU GLY LYS GLU GLN ASN TYR THR CYS HIS VAL
SEQRES 21 G 275 HIS HIS LYS GLY LEU PRO GLU PRO LEU THR LEU ARG TRP
SEQRES 22 G 275 LYS PRO
SEQRES 1 H 100 MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG
SEQRES 2 H 100 HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS
SEQRES 3 H 100 TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP
SEQRES 4 H 100 LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS
SEQRES 5 H 100 SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU
SEQRES 6 H 100 LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU
SEQRES 7 H 100 TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO
SEQRES 8 H 100 LYS ILE VAL LYS TRP ASP ARG ASP MET
SEQRES 1 S 9 TYR TYR GLN SER GLY LEU SER ILE VAL
HET GOL A 301 6
HET GOL A 302 6
HET EDO A 303 4
HET EDO C 301 4
HET EDO C 302 4
HET GOL D 101 6
HET GOL F 101 6
HET GOL G 301 6
HET GOL H 101 6
HETNAM GOL GLYCEROL
HETNAM EDO 1,2-ETHANEDIOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 13 GOL 6(C3 H8 O3)
FORMUL 15 EDO 3(C2 H6 O2)
FORMUL 22 HOH *472(H2 O)
HELIX 1 AA1 ALA A 49 GLU A 53 5 5
HELIX 2 AA2 GLY A 56 TYR A 85 1 30
HELIX 3 AA3 ASP A 137 GLY A 151 1 15
HELIX 4 AA4 GLY A 151 GLY A 162 1 12
HELIX 5 AA5 GLY A 162 GLY A 175 1 14
HELIX 6 AA6 GLY A 175 LEU A 180 1 6
HELIX 7 AA7 LYS A 253 GLN A 255 5 3
HELIX 8 AA8 ALA C 49 GLU C 53 5 5
HELIX 9 AA9 GLY C 56 TYR C 85 1 30
HELIX 10 AB1 ASP C 137 ALA C 150 1 14
HELIX 11 AB2 GLY C 151 GLY C 162 1 12
HELIX 12 AB3 GLY C 162 GLY C 175 1 14
HELIX 13 AB4 GLY C 175 LEU C 180 1 6
HELIX 14 AB5 LYS C 253 TYR C 257 5 5
HELIX 15 AB6 ALA E 49 GLU E 53 5 5
HELIX 16 AB7 GLY E 56 TYR E 85 1 30
HELIX 17 AB8 ASP E 137 GLY E 151 1 15
HELIX 18 AB9 GLY E 151 GLY E 162 1 12
HELIX 19 AC1 GLY E 162 GLY E 175 1 14
HELIX 20 AC2 GLY E 175 LEU E 180 1 6
HELIX 21 AC3 LYS E 253 TYR E 257 5 5
HELIX 22 AC4 ALA G 49 GLU G 53 5 5
HELIX 23 AC5 GLY G 56 TYR G 85 1 30
HELIX 24 AC6 ASP G 137 ALA G 150 1 14
HELIX 25 AC7 GLY G 151 GLY G 162 1 12
HELIX 26 AC8 GLY G 162 GLY G 175 1 14
HELIX 27 AC9 GLY G 175 LEU G 180 1 6
HELIX 28 AD1 LYS G 253 GLN G 255 5 3
SHEET 1 AA1 8 GLU A 46 PRO A 47 0
SHEET 2 AA1 8 THR A 31 ASP A 37 -1 N ARG A 35 O GLU A 46
SHEET 3 AA1 8 ARG A 21 VAL A 28 -1 N VAL A 28 O THR A 31
SHEET 4 AA1 8 HIS A 3 VAL A 12 -1 N ARG A 6 O TYR A 27
SHEET 5 AA1 8 THR A 94 VAL A 103 -1 O CYS A 101 N LEU A 5
SHEET 6 AA1 8 LEU A 109 TYR A 118 -1 O LEU A 110 N ASP A 102
SHEET 7 AA1 8 ARG A 121 LEU A 126 -1 O LEU A 126 N HIS A 114
SHEET 8 AA1 8 TRP A 133 ALA A 135 -1 O THR A 134 N ALA A 125
SHEET 1 AA2 4 LYS A 186 PRO A 193 0
SHEET 2 AA2 4 ASP A 198 PHE A 208 -1 O TRP A 204 N HIS A 188
SHEET 3 AA2 4 PHE A 241 PRO A 250 -1 O ALA A 245 N CYS A 203
SHEET 4 AA2 4 GLU A 229 LEU A 230 -1 N GLU A 229 O ALA A 246
SHEET 1 AA3 4 LYS A 186 PRO A 193 0
SHEET 2 AA3 4 ASP A 198 PHE A 208 -1 O TRP A 204 N HIS A 188
SHEET 3 AA3 4 PHE A 241 PRO A 250 -1 O ALA A 245 N CYS A 203
SHEET 4 AA3 4 ARG A 234 PRO A 235 -1 N ARG A 234 O GLN A 242
SHEET 1 AA4 3 THR A 214 LEU A 219 0
SHEET 2 AA4 3 TYR A 257 HIS A 262 -1 O HIS A 260 N THR A 216
SHEET 3 AA4 3 LEU A 270 LEU A 272 -1 O LEU A 272 N CYS A 259
SHEET 1 AA5 4 LYS B 6 SER B 11 0
SHEET 2 AA5 4 ASN B 21 PHE B 30 -1 O ASN B 24 N TYR B 10
SHEET 3 AA5 4 PHE B 62 PHE B 70 -1 O TYR B 66 N CYS B 25
SHEET 4 AA5 4 GLU B 50 HIS B 51 -1 N GLU B 50 O TYR B 67
SHEET 1 AA6 4 LYS B 6 SER B 11 0
SHEET 2 AA6 4 ASN B 21 PHE B 30 -1 O ASN B 24 N TYR B 10
SHEET 3 AA6 4 PHE B 62 PHE B 70 -1 O TYR B 66 N CYS B 25
SHEET 4 AA6 4 SER B 55 PHE B 56 -1 N SER B 55 O TYR B 63
SHEET 1 AA7 4 GLU B 44 ARG B 45 0
SHEET 2 AA7 4 GLU B 36 LYS B 41 -1 N LYS B 41 O GLU B 44
SHEET 3 AA7 4 TYR B 78 ASN B 83 -1 O ALA B 79 N LEU B 40
SHEET 4 AA7 4 LYS B 91 LYS B 94 -1 O LYS B 91 N VAL B 82
SHEET 1 AA8 8 GLU C 46 PRO C 47 0
SHEET 2 AA8 8 THR C 31 ASP C 37 -1 N ARG C 35 O GLU C 46
SHEET 3 AA8 8 ARG C 21 VAL C 28 -1 N VAL C 28 O THR C 31
SHEET 4 AA8 8 HIS C 3 VAL C 12 -1 N VAL C 12 O ARG C 21
SHEET 5 AA8 8 THR C 94 VAL C 103 -1 O PHE C 95 N ALA C 11
SHEET 6 AA8 8 LEU C 109 TYR C 118 -1 O LEU C 110 N ASP C 102
SHEET 7 AA8 8 ARG C 121 LEU C 126 -1 O LEU C 126 N HIS C 114
SHEET 8 AA8 8 TRP C 133 ALA C 135 -1 O THR C 134 N ALA C 125
SHEET 1 AA9 4 LYS C 186 ARG C 194 0
SHEET 2 AA9 4 ASP C 198 PHE C 208 -1 O THR C 200 N HIS C 192
SHEET 3 AA9 4 PHE C 241 PRO C 250 -1 O ALA C 245 N CYS C 203
SHEET 4 AA9 4 GLU C 229 LEU C 230 -1 N GLU C 229 O ALA C 246
SHEET 1 AB1 4 LYS C 186 ARG C 194 0
SHEET 2 AB1 4 ASP C 198 PHE C 208 -1 O THR C 200 N HIS C 192
SHEET 3 AB1 4 PHE C 241 PRO C 250 -1 O ALA C 245 N CYS C 203
SHEET 4 AB1 4 ARG C 234 PRO C 235 -1 N ARG C 234 O GLN C 242
SHEET 1 AB2 4 ASP C 223 LEU C 224 0
SHEET 2 AB2 4 THR C 214 LEU C 219 -1 O LEU C 219 N ASP C 223
SHEET 3 AB2 4 THR C 258 HIS C 262 -1 O HIS C 260 N THR C 216
SHEET 4 AB2 4 LEU C 270 LEU C 272 -1 O LEU C 272 N CYS C 259
SHEET 1 AB3 4 LYS D 6 SER D 11 0
SHEET 2 AB3 4 ASN D 21 PHE D 30 -1 O ASN D 24 N TYR D 10
SHEET 3 AB3 4 PHE D 62 PHE D 70 -1 O TYR D 66 N CYS D 25
SHEET 4 AB3 4 GLU D 50 HIS D 51 -1 N GLU D 50 O TYR D 67
SHEET 1 AB4 4 LYS D 6 SER D 11 0
SHEET 2 AB4 4 ASN D 21 PHE D 30 -1 O ASN D 24 N TYR D 10
SHEET 3 AB4 4 PHE D 62 PHE D 70 -1 O TYR D 66 N CYS D 25
SHEET 4 AB4 4 SER D 55 PHE D 56 -1 N SER D 55 O TYR D 63
SHEET 1 AB5 4 GLU D 44 ARG D 45 0
SHEET 2 AB5 4 ILE D 35 LYS D 41 -1 N LYS D 41 O GLU D 44
SHEET 3 AB5 4 TYR D 78 HIS D 84 -1 O ALA D 79 N LEU D 40
SHEET 4 AB5 4 LYS D 91 LYS D 94 -1 O LYS D 91 N VAL D 82
SHEET 1 AB6 8 GLU E 46 PRO E 47 0
SHEET 2 AB6 8 THR E 31 ASP E 37 -1 N ARG E 35 O GLU E 46
SHEET 3 AB6 8 ARG E 21 VAL E 28 -1 N VAL E 28 O THR E 31
SHEET 4 AB6 8 HIS E 3 VAL E 12 -1 N ARG E 6 O TYR E 27
SHEET 5 AB6 8 THR E 94 VAL E 103 -1 O PHE E 95 N ALA E 11
SHEET 6 AB6 8 LEU E 109 TYR E 118 -1 O TYR E 113 N GLY E 100
SHEET 7 AB6 8 ARG E 121 LEU E 126 -1 O LEU E 126 N HIS E 114
SHEET 8 AB6 8 TRP E 133 ALA E 135 -1 O THR E 134 N ALA E 125
SHEET 1 AB7 4 LYS E 186 PRO E 193 0
SHEET 2 AB7 4 ASP E 198 PHE E 208 -1 O THR E 200 N HIS E 192
SHEET 3 AB7 4 PHE E 241 PRO E 250 -1 O ALA E 245 N CYS E 203
SHEET 4 AB7 4 GLU E 229 LEU E 230 -1 N GLU E 229 O ALA E 246
SHEET 1 AB8 4 LYS E 186 PRO E 193 0
SHEET 2 AB8 4 ASP E 198 PHE E 208 -1 O THR E 200 N HIS E 192
SHEET 3 AB8 4 PHE E 241 PRO E 250 -1 O ALA E 245 N CYS E 203
SHEET 4 AB8 4 ARG E 234 PRO E 235 -1 N ARG E 234 O GLN E 242
SHEET 1 AB9 3 THR E 214 GLN E 218 0
SHEET 2 AB9 3 THR E 258 HIS E 262 -1 O HIS E 260 N THR E 216
SHEET 3 AB9 3 LEU E 270 LEU E 272 -1 O LEU E 272 N CYS E 259
SHEET 1 AC1 4 LYS F 6 SER F 11 0
SHEET 2 AC1 4 ASN F 21 PHE F 30 -1 O TYR F 26 N GLN F 8
SHEET 3 AC1 4 PHE F 62 PHE F 70 -1 O PHE F 70 N ASN F 21
SHEET 4 AC1 4 GLU F 50 HIS F 51 -1 N GLU F 50 O TYR F 67
SHEET 1 AC2 4 LYS F 6 SER F 11 0
SHEET 2 AC2 4 ASN F 21 PHE F 30 -1 O TYR F 26 N GLN F 8
SHEET 3 AC2 4 PHE F 62 PHE F 70 -1 O PHE F 70 N ASN F 21
SHEET 4 AC2 4 SER F 55 PHE F 56 -1 N SER F 55 O TYR F 63
SHEET 1 AC3 4 GLU F 44 ARG F 45 0
SHEET 2 AC3 4 GLU F 36 LYS F 41 -1 N LYS F 41 O GLU F 44
SHEET 3 AC3 4 TYR F 78 ASN F 83 -1 O ALA F 79 N LEU F 40
SHEET 4 AC3 4 LYS F 91 LYS F 94 -1 O LYS F 91 N VAL F 82
SHEET 1 AC4 8 PHE G 45 PRO G 47 0
SHEET 2 AC4 8 THR G 31 ASP G 37 -1 N ARG G 35 O GLU G 46
SHEET 3 AC4 8 ARG G 21 VAL G 28 -1 N ALA G 24 O PHE G 36
SHEET 4 AC4 8 HIS G 3 VAL G 12 -1 N VAL G 12 O ARG G 21
SHEET 5 AC4 8 THR G 94 VAL G 103 -1 O VAL G 103 N HIS G 3
SHEET 6 AC4 8 LEU G 109 TYR G 118 -1 O LEU G 110 N ASP G 102
SHEET 7 AC4 8 ARG G 121 LEU G 126 -1 O ILE G 124 N PHE G 116
SHEET 8 AC4 8 TRP G 133 ALA G 135 -1 O THR G 134 N ALA G 125
SHEET 1 AC5 4 LYS G 186 ARG G 194 0
SHEET 2 AC5 4 ASP G 198 PHE G 208 -1 O TRP G 204 N HIS G 188
SHEET 3 AC5 4 PHE G 241 PRO G 250 -1 O ALA G 245 N CYS G 203
SHEET 4 AC5 4 GLU G 229 LEU G 230 -1 N GLU G 229 O ALA G 246
SHEET 1 AC6 4 LYS G 186 ARG G 194 0
SHEET 2 AC6 4 ASP G 198 PHE G 208 -1 O TRP G 204 N HIS G 188
SHEET 3 AC6 4 PHE G 241 PRO G 250 -1 O ALA G 245 N CYS G 203
SHEET 4 AC6 4 ARG G 234 PRO G 235 -1 N ARG G 234 O GLN G 242
SHEET 1 AC7 4 LEU G 224 THR G 225 0
SHEET 2 AC7 4 THR G 214 LEU G 219 -1 N TRP G 217 O THR G 225
SHEET 3 AC7 4 TYR G 257 HIS G 262 -1 O HIS G 260 N THR G 216
SHEET 4 AC7 4 LEU G 270 ARG G 273 -1 O LEU G 270 N VAL G 261
SHEET 1 AC8 4 LYS H 6 SER H 11 0
SHEET 2 AC8 4 ASN H 21 PHE H 30 -1 O ASN H 24 N TYR H 10
SHEET 3 AC8 4 PHE H 62 PHE H 70 -1 O PHE H 70 N ASN H 21
SHEET 4 AC8 4 GLU H 50 HIS H 51 -1 N GLU H 50 O TYR H 67
SHEET 1 AC9 4 LYS H 6 SER H 11 0
SHEET 2 AC9 4 ASN H 21 PHE H 30 -1 O ASN H 24 N TYR H 10
SHEET 3 AC9 4 PHE H 62 PHE H 70 -1 O PHE H 70 N ASN H 21
SHEET 4 AC9 4 SER H 55 PHE H 56 -1 N SER H 55 O TYR H 63
SHEET 1 AD1 4 GLU H 44 ARG H 45 0
SHEET 2 AD1 4 GLU H 36 LYS H 41 -1 N LYS H 41 O GLU H 44
SHEET 3 AD1 4 TYR H 78 ASN H 83 -1 O ALA H 79 N LEU H 40
SHEET 4 AD1 4 LYS H 91 LYS H 94 -1 O LYS H 91 N VAL H 82
SSBOND 1 CYS A 101 CYS A 164 1555 1555 2.06
SSBOND 2 CYS A 203 CYS A 259 1555 1555 2.03
SSBOND 3 CYS B 25 CYS B 80 1555 1555 2.03
SSBOND 4 CYS C 101 CYS C 164 1555 1555 2.06
SSBOND 5 CYS C 203 CYS C 259 1555 1555 2.02
SSBOND 6 CYS D 25 CYS D 80 1555 1555 2.03
SSBOND 7 CYS E 101 CYS E 164 1555 1555 2.05
SSBOND 8 CYS E 203 CYS E 259 1555 1555 2.03
SSBOND 9 CYS F 25 CYS F 80 1555 1555 2.04
SSBOND 10 CYS G 101 CYS G 164 1555 1555 2.06
SSBOND 11 CYS G 203 CYS G 259 1555 1555 2.02
SSBOND 12 CYS H 25 CYS H 80 1555 1555 2.04
CISPEP 1 TYR A 209 PRO A 210 0 5.14
CISPEP 2 HIS B 31 PRO B 32 0 6.88
CISPEP 3 TYR C 209 PRO C 210 0 5.44
CISPEP 4 HIS D 31 PRO D 32 0 6.44
CISPEP 5 TYR E 209 PRO E 210 0 5.44
CISPEP 6 HIS F 31 PRO F 32 0 6.94
CISPEP 7 TYR G 209 PRO G 210 0 5.19
CISPEP 8 HIS H 31 PRO H 32 0 6.75
SITE 1 AC1 4 GLU A 232 HOH A 457 LYS B 58 ASP B 59
SITE 1 AC2 1 ASP A 30
SITE 1 AC3 5 ASP A 212 ILE A 213 THR A 214 HIS A 263
SITE 2 AC3 5 LYS A 264
SITE 1 AC4 3 ASP C 212 THR C 214 HIS C 262
SITE 1 AC5 6 THR C 225 GLN C 226 HOH C 460 HOH D 202
SITE 2 AC5 6 TYR G 84 TYR G 85
SITE 1 AC6 5 GLU C 232 SER D 57 LYS D 58 ASP D 59
SITE 2 AC6 5 HOH D 203
SITE 1 AC7 3 ASP E 29 ASP E 30 TYR F 63
SITE 1 AC8 5 TYR G 27 ASP G 29 ASP G 30 TYR H 63
SITE 2 AC8 5 GOL H 101
SITE 1 AC9 4 GOL G 301 SER H 57 LYS H 58 HOH H 207
CRYST1 47.302 88.960 109.947 89.97 93.83 90.04 P 1 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 0.021141 0.000014 0.001416 0.00000
SCALE2 0.000000 0.011241 -0.000005 0.00000
SCALE3 0.000000 0.000000 0.009116 0.00000
TER 2246 TRP A 274
TER 3080 MET B 99
TER 3154 VAL P 9
TER 5406 TRP C 274
TER 6240 MET D 99
TER 6314 VAL Q 9
TER 8567 TRP E 274
TER 9401 MET F 99
TER 9475 VAL R 9
TER 11727 TRP G 274
TER 12564 MET H 99
TER 12638 VAL S 9
MASTER 467 0 9 28 126 0 13 613146 12 72 124
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