HEADER HYDROLASE/PROTEIN BINDING 12-NOV-18 6IRD
TITLE COMPLEX STRUCTURE OF INADL PDZ89 AND PLCB4 C-TERMINAL CC-PBM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE;
COMPND 3 CHAIN: B;
COMPND 4 FRAGMENT: C-TERMINAL CC-PBM;
COMPND 5 EC: 3.1.4.11;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: INAD-LIKE PROTEIN;
COMPND 10 CHAIN: C;
COMPND 11 FRAGMENT: PDZ89;
COMPND 12 SYNONYM: HINADL,PALS1-ASSOCIATED TIGHT JUNCTION PROTEIN,PROTEIN
COMPND 13 ASSOCIATED TO TIGHT JUNCTIONS;
COMPND 14 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: PLCB4;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: PATJ, INADL;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS PDZ SUPRAMODULE, PHOSPHOLIPASE C BETA, HYDROLASE-PROTEIN BINDING
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR F.YE,J.LI,Y.HUANG,W.LIU,M.ZHANG
REVDAT 2 28-OCT-20 6IRD 1 JRNL LINK
REVDAT 1 23-JAN-19 6IRD 0
JRNL AUTH F.YE,Y.HUANG,J.LI,Y.MA,C.XIE,Z.LIU,X.DENG,J.WAN,T.XUE,W.LIU,
JRNL AUTH 2 M.ZHANG
JRNL TITL AN UNEXPECTED INAD PDZ TANDEM-MEDIATED PLC BETA BINDING IN
JRNL TITL 2 DROSOPHILA PHOTO RECEPTORS.
JRNL REF ELIFE V. 7 2018
JRNL REFN ESSN 2050-084X
JRNL PMID 30526850
JRNL DOI 10.7554/ELIFE.41848
REMARK 2
REMARK 2 RESOLUTION. 2.81 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.14_3260: ???)
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) : 2.81
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.310
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.4
REMARK 3 NUMBER OF REFLECTIONS : 12434
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.247
REMARK 3 R VALUE (WORKING SET) : 0.244
REMARK 3 FREE R VALUE : 0.302
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.860
REMARK 3 FREE R VALUE TEST SET COUNT : 604
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 3.0936 - 2.8128 0.54 1757 106 0.3153 0.3287
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) : 0.410
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.500
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.86
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
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 6IRD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-NOV-18.
REMARK 100 THE DEPOSITION ID IS D_1300008898.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-MAR-18
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 : SSRF
REMARK 200 BEAMLINE : BL17U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97918
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14070
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : 0.11700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 6.90
REMARK 200 R MERGE FOR SHELL (I) : 0.93800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AUTOSOL, SHELXD
REMARK 200 STARTING MODEL: 3R0H
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M MGCL2, 0.1M BIS-TRIS PH6.5, 20%
REMARK 280 W/V POLYETHYLENE GLYCOL 3350, LIQUID DIFFUSION, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 66.79167
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 133.58333
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 133.58333
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 66.79167
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24900 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C
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 GLU B -1
REMARK 465 GLY B 0
REMARK 465 GLU B 1
REMARK 465 LEU B 2
REMARK 465 ILE B 3
REMARK 465 PRO B 4
REMARK 465 GLN B 5
REMARK 465 LYS B 75
REMARK 465 GLY B 76
REMARK 465 GLY B 77
REMARK 465 SER B 78
REMARK 465 ASN B 79
REMARK 465 LEU C 266
REMARK 465 SER C 267
REMARK 465 VAL C 268
REMARK 465 ASP C 269
REMARK 465 PRO C 270
REMARK 465 ASP C 363A
REMARK 465 GLU C 363B
REMARK 465 ALA C 363C
REMARK 465 HIS C 363D
REMARK 465 TYR C 363E
REMARK 465 ARG C 363F
REMARK 465 ASP C 363G
REMARK 465 GLU C 363H
REMARK 465 GLU C 363I
REMARK 465 ASN C 363J
REMARK 465 ALA C 460
REMARK 465 GLY C 461
REMARK 465 SER C 462
REMARK 465 TRP C 463
REMARK 465 THR C 464
REMARK 465 SER C 465
REMARK 465 ALA C 466
REMARK 465 ARG C 467
REMARK 465 THR C 468
REMARK 465 THR C 469
REMARK 465 GLY C 470
REMARK 465 GLY C 471
REMARK 465 GLY C 472
REMARK 465 SER C 473
REMARK 465 GLY C 474
REMARK 465 GLY C 475
REMARK 465 GLY C 476
REMARK 465 GLY C 477
REMARK 465 SER C 478
REMARK 465 GLY C 479
REMARK 465 GLY C 480
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 B 12 CG CD CE NZ
REMARK 470 GLN B 25 CG CD OE1 NE2
REMARK 470 LYS B 32 CG CD CE NZ
REMARK 470 GLU B 65 CG CD OE1 OE2
REMARK 470 LYS B 66 CG CD CE NZ
REMARK 470 GLU B 69 CG CD OE1 OE2
REMARK 470 LYS B 70 CG CD CE NZ
REMARK 470 MET B 72 CG SD CE
REMARK 470 LYS B 73 CG CD CE NZ
REMARK 470 LYS B 74 CG CD CE NZ
REMARK 470 LYS B 84 CG CD CE NZ
REMARK 470 LYS B 85 CG CD CE NZ
REMARK 470 GLU B 86 CG CD OE1 OE2
REMARK 470 LYS B 90 CG CD CE NZ
REMARK 470 GLN B 92 CG CD OE1 NE2
REMARK 470 LYS B 99 CG CD CE NZ
REMARK 470 LYS B 101 CG CD CE NZ
REMARK 470 GLU B 104 CG CD OE1 OE2
REMARK 470 ARG B 128 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 141 CG CD CE NZ
REMARK 470 ARG B 166 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 171 CG CD CE NZ
REMARK 470 GLU B 175 CG CD OE1 OE2
REMARK 470 LYS B 178 CG CD CE NZ
REMARK 470 GLN B 182 CG CD OE1 NE2
REMARK 470 ASP B 183 CG OD1 OD2
REMARK 470 LYS B 184 CG CD CE NZ
REMARK 470 LYS B 187 CG CD CE NZ
REMARK 470 LYS B 189 CG CD CE NZ
REMARK 470 LYS B 220 CG CD CE NZ
REMARK 470 LYS B 227 CG CD CE NZ
REMARK 470 GLU B 234 CG CD OE1 OE2
REMARK 470 LYS B 238 CG CD CE NZ
REMARK 470 GLU B 255 CG CD OE1 OE2
REMARK 470 GLU C 280 CG CD OE1 OE2
REMARK 470 GLU C 284 CG CD OE1 OE2
REMARK 470 LYS C 287 CG CD CE NZ
REMARK 470 ARG C 289 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 315 CG CD OE1 OE2
REMARK 470 ARG C 320 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 332 CG CD OE1 OE2
REMARK 470 ARG C 339 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 344 CG CD OE1 OE2
REMARK 470 GLU C 345 CG CD OE1 OE2
REMARK 470 ARG C 351 CG CD NE CZ NH1 NH2
REMARK 470 GLN C 352 CG CD OE1 NE2
REMARK 470 GLN C 355 CG CD OE1 NE2
REMARK 470 LYS C 356 CG CD CE NZ
REMARK 470 ARG C 358 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 383 CG CD CE NZ
REMARK 470 ARG C 386 CG CD NE CZ NH1 NH2
REMARK 470 ASN C 397 CG OD1 ND2
REMARK 470 LYS C 408 CG CD CE NZ
REMARK 470 GLN C 420 CG CD OE1 NE2
REMARK 470 GLN C 423 CG CD OE1 NE2
REMARK 470 ARG C 459 CG CD NE CZ NH1 NH2
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 B 81 CA - CB - CG ANGL. DEV. = 18.0 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 LEU B 81 -128.84 61.11
REMARK 500 GLN C 352 4.38 -68.14
REMARK 500 PRO C 354 -166.70 -68.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 AU B 303 AU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR C 272 O
REMARK 620 2 CYS C 273 SG 90.0
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AU B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AU B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AU B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AU B 304
DBREF 6IRD B 1 264 UNP Q91UZ1 Q91UZ1_MOUSE 912 1175
DBREF 6IRD C 266 469 UNP Q8NI35 INADL_HUMAN 1421 1625
SEQADV 6IRD GLU B -1 UNP Q91UZ1 EXPRESSION TAG
SEQADV 6IRD GLY B 0 UNP Q91UZ1 EXPRESSION TAG
SEQADV 6IRD ALA B 15 UNP Q91UZ1 LYS 926 ENGINEERED MUTATION
SEQADV 6IRD ALA B 19 UNP Q91UZ1 LYS 930 ENGINEERED MUTATION
SEQADV 6IRD ALA B 22 UNP Q91UZ1 LYS 933 ENGINEERED MUTATION
SEQADV 6IRD ALA B 23 UNP Q91UZ1 LYS 934 ENGINEERED MUTATION
SEQADV 6IRD ALA B 26 UNP Q91UZ1 LYS 937 ENGINEERED MUTATION
SEQADV 6IRD ALA B 33 UNP Q91UZ1 LYS 944 ENGINEERED MUTATION
SEQADV 6IRD ALA B 34 UNP Q91UZ1 LYS 945 ENGINEERED MUTATION
SEQADV 6IRD ALA B 37 UNP Q91UZ1 LYS 948 ENGINEERED MUTATION
SEQADV 6IRD GLY C 470 UNP Q8NI35 EXPRESSION TAG
SEQADV 6IRD GLY C 471 UNP Q8NI35 EXPRESSION TAG
SEQADV 6IRD GLY C 472 UNP Q8NI35 EXPRESSION TAG
SEQADV 6IRD SER C 473 UNP Q8NI35 EXPRESSION TAG
SEQADV 6IRD GLY C 474 UNP Q8NI35 EXPRESSION TAG
SEQADV 6IRD GLY C 475 UNP Q8NI35 EXPRESSION TAG
SEQADV 6IRD GLY C 476 UNP Q8NI35 EXPRESSION TAG
SEQADV 6IRD GLY C 477 UNP Q8NI35 EXPRESSION TAG
SEQADV 6IRD SER C 478 UNP Q8NI35 EXPRESSION TAG
SEQADV 6IRD GLY C 479 UNP Q8NI35 EXPRESSION TAG
SEQADV 6IRD GLY C 480 UNP Q8NI35 EXPRESSION TAG
SEQRES 1 B 266 GLU GLY GLU LEU ILE PRO GLN VAL ARG ILE GLU ASP LEU
SEQRES 2 B 266 LYS GLN MET ALA ALA TYR LEU ALA HIS LEU ALA ALA GLN
SEQRES 3 B 266 GLN ALA GLU LEU ASN SER LEU LYS ALA ALA HIS ALA ALA
SEQRES 4 B 266 GLU HIS SER THR MET GLN LYS LEU HIS CYS THR GLN VAL
SEQRES 5 B 266 ASP LYS ILE VAL ALA GLN TYR ASP LYS GLU LYS SER THR
SEQRES 6 B 266 HIS GLU LYS ILE LEU GLU LYS ALA MET LYS LYS LYS GLY
SEQRES 7 B 266 GLY SER ASN CYS LEU GLU ILE LYS LYS GLU THR GLU ILE
SEQRES 8 B 266 LYS ILE GLN THR LEU THR THR ASP HIS LYS SER LYS VAL
SEQRES 9 B 266 LYS GLU ILE VAL ALA GLN HIS THR LYS GLU TRP SER GLU
SEQRES 10 B 266 MET ILE ASN THR HIS SER ALA GLU GLU GLN GLU ILE ARG
SEQRES 11 B 266 ASP LEU HIS LEU SER GLN GLN CYS GLU LEU LEU ARG LYS
SEQRES 12 B 266 LEU LEU ILE ASN ALA HIS GLU GLN GLN THR GLN GLN LEU
SEQRES 13 B 266 LYS LEU SER HIS ASP ARG GLU SER LYS GLU MET ARG ALA
SEQRES 14 B 266 HIS GLN ALA LYS ILE SER MET GLU ASN SER LYS ALA ILE
SEQRES 15 B 266 SER GLN ASP LYS SER ILE LYS ASN LYS ALA GLU ARG GLU
SEQRES 16 B 266 ARG ARG VAL ARG GLU LEU ASN SER SER ASN THR LYS LYS
SEQRES 17 B 266 PHE LEU GLU GLU ARG LYS ARG LEU ALA MET LYS GLN SER
SEQRES 18 B 266 LYS GLU MET ASP GLN LEU LYS LYS VAL GLN LEU GLU HIS
SEQRES 19 B 266 LEU GLU PHE LEU GLU LYS GLN ASN GLU GLN ALA LYS GLU
SEQRES 20 B 266 MET GLN GLN MET VAL LYS LEU GLU ALA GLU MET ASP ARG
SEQRES 21 B 266 ARG PRO ALA THR VAL VAL
SEQRES 1 C 216 LEU SER VAL ASP PRO ALA THR CYS PRO ILE VAL PRO GLY
SEQRES 2 C 216 GLN GLU MET ILE ILE GLU ILE SER LYS GLY ARG SER GLY
SEQRES 3 C 216 LEU GLY LEU SER ILE VAL GLY GLY LYS ASP THR PRO LEU
SEQRES 4 C 216 ASN ALA ILE VAL ILE HIS GLU VAL TYR GLU GLU GLY ALA
SEQRES 5 C 216 ALA ALA ARG ASP GLY ARG LEU TRP ALA GLY ASP GLN ILE
SEQRES 6 C 216 LEU GLU VAL ASN GLY VAL ASP LEU ARG ASN SER SER HIS
SEQRES 7 C 216 GLU GLU ALA ILE THR ALA LEU ARG GLN THR PRO GLN LYS
SEQRES 8 C 216 VAL ARG LEU VAL VAL TYR ARG ASP GLU ALA HIS TYR ARG
SEQRES 9 C 216 ASP GLU GLU ASN LEU GLU ILE PHE PRO VAL ASP LEU GLN
SEQRES 10 C 216 LYS LYS ALA GLY ARG GLY LEU GLY LEU SER ILE VAL GLY
SEQRES 11 C 216 LYS ARG ASN GLY SER GLY VAL PHE ILE SER ASP ILE VAL
SEQRES 12 C 216 LYS GLY GLY ALA ALA ASP LEU ASP GLY ARG LEU ILE GLN
SEQRES 13 C 216 GLY ASP GLN ILE LEU SER VAL ASN GLY GLU ASP MET ARG
SEQRES 14 C 216 ASN ALA SER GLN GLU THR VAL ALA THR ILE LEU LYS CYS
SEQRES 15 C 216 ALA GLN GLY LEU VAL GLN LEU GLU ILE GLY ARG LEU ARG
SEQRES 16 C 216 ALA GLY SER TRP THR SER ALA ARG THR THR GLY GLY GLY
SEQRES 17 C 216 SER GLY GLY GLY GLY SER GLY GLY
HET AU B 301 1
HET AU B 302 1
HET AU B 303 1
HET AU B 304 1
HET AU C 501 1
HETNAM AU GOLD ION
FORMUL 3 AU 5(AU 1+)
HELIX 1 AA1 VAL B 6 LYS B 12 1 7
HELIX 2 AA2 MET B 14 LYS B 74 1 61
HELIX 3 AA3 LEU B 81 GLN B 182 1 102
HELIX 4 AA4 ASN B 188 ARG B 258 1 71
HELIX 5 AA5 GLY C 316 GLY C 322 1 7
HELIX 6 AA6 SER C 342 GLN C 352 1 11
HELIX 7 AA7 GLY C 410 GLY C 416 1 7
HELIX 8 AA8 SER C 436 ALA C 447 1 12
SHEET 1 AA1 3 THR B 262 VAL B 263 0
SHEET 2 AA1 3 SER C 391 VAL C 393 -1 O ILE C 392 N THR B 262
SHEET 3 AA1 3 PHE C 402 ILE C 403 -1 O PHE C 402 N VAL C 393
SHEET 1 AA2 5 MET C 281 SER C 286 0
SHEET 2 AA2 5 LYS C 356 TYR C 362 -1 O LEU C 359 N ILE C 283
SHEET 3 AA2 5 GLN C 329 VAL C 333 -1 N LEU C 331 O VAL C 360
SHEET 4 AA2 5 ILE C 307 VAL C 312 -1 N ILE C 307 O ILE C 330
SHEET 5 AA2 5 LEU C 294 VAL C 297 -1 N SER C 295 O HIS C 310
SHEET 1 AA3 4 MET C 281 SER C 286 0
SHEET 2 AA3 4 LYS C 356 TYR C 362 -1 O LEU C 359 N ILE C 283
SHEET 3 AA3 4 GLN C 329 VAL C 333 -1 N LEU C 331 O VAL C 360
SHEET 4 AA3 4 VAL C 336 ASP C 337 -1 O VAL C 336 N VAL C 333
SHEET 1 AA4 4 GLU C 374 GLN C 381 0
SHEET 2 AA4 4 LEU C 450 ARG C 457 -1 O VAL C 451 N LEU C 380
SHEET 3 AA4 4 GLN C 423 VAL C 427 -1 N GLN C 423 O GLY C 456
SHEET 4 AA4 4 GLU C 430 ASP C 431 -1 O GLU C 430 N VAL C 427
LINK SG CYS B 47 AU AU B 302 1555 1555 2.48
LINK SG CYS B 136 AU AU B 301 1555 1555 2.32
LINK AU AU B 303 O THR C 272 2555 1555 2.80
LINK AU AU B 303 SG CYS C 273 2555 1555 2.23
SITE 1 AC1 2 CYS B 136 GLU B 137
SITE 1 AC2 3 CYS B 47 THR B 48 ASP B 51
SITE 1 AC3 3 THR C 272 CYS C 273 PRO C 274
SITE 1 AC4 1 GLN B 239
CRYST1 69.089 69.089 200.375 90.00 90.00 120.00 P 31 2 1 6
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 0.014474 0.008357 0.000000 0.00000
SCALE2 0.000000 0.016713 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004991 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
