HEADER METAL TRANSPORT 11-AUG-11 3TE3
TITLE COILED-COIL OLIGOMERIZATION DOMAIN OF THE POLYCYSTIN TRANSIENT
TITLE 2 RECEPTOR POTENTIAL CHANNEL PKD2L1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYCYSTIC KIDNEY DISEASE 2-LIKE 1 PROTEIN;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 FRAGMENT: UNP RESIDUES 699-737;
COMPND 5 SYNONYM: POLYCYSTIN-2 HOMOLOG, POLYCYSTIN-2L1, POLYCYSTIN-L,
COMPND 6 POLYCYSTIN-L1;
COMPND 7 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: PKD2L1, PKD2L, PKDL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMIND;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PEV-L8
KEYWDS TRIMERIC COILED-COIL, OLIGOMERIZATION DOMAIN, C-TERMINAL CYTOPLASMIC
KEYWDS 2 REGULATORY DOMAIN, METAL TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR D.A.YERNOOL,K.M.MOLLAND
REVDAT 4 28-FEB-24 3TE3 1 REMARK
REVDAT 3 08-NOV-17 3TE3 1 AUTHOR REMARK
REVDAT 2 08-FEB-12 3TE3 1 JRNL
REVDAT 1 18-JAN-12 3TE3 0
JRNL AUTH K.L.MOLLAND,L.N.PAUL,D.A.YERNOOL
JRNL TITL CRYSTAL STRUCTURE AND CHARACTERIZATION OF COILED-COIL DOMAIN
JRNL TITL 2 OF THE TRANSIENT RECEPTOR POTENTIAL CHANNEL PKD2L1.
JRNL REF BIOCHIM.BIOPHYS.ACTA V.1824 413 2011
JRNL REFN ISSN 0006-3002
JRNL PMID 22193359
JRNL DOI 10.1016/J.BBAPAP.2011.12.002
REMARK 2
REMARK 2 RESOLUTION. 2.69 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7_650)
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) : 2.69
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.09
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 8840
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.255
REMARK 3 R VALUE (WORKING SET) : 0.253
REMARK 3 FREE R VALUE : 0.290
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.720
REMARK 3 FREE R VALUE TEST SET COUNT : 417
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 29.0928 - 3.8831 1.00 3019 143 0.2655 0.2781
REMARK 3 2 3.8831 - 3.0833 0.98 2799 122 0.2225 0.3057
REMARK 3 3 3.0833 - 2.6940 0.94 2605 152 0.2626 0.3046
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.72
REMARK 3 K_SOL : 0.35
REMARK 3 B_SOL : 66.89
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.420
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.870
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 57.17
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 57.17
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.85460
REMARK 3 B22 (A**2) : 5.85460
REMARK 3 B33 (A**2) : -11.70920
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.022 1711
REMARK 3 ANGLE : 1.121 2115
REMARK 3 CHIRALITY : 0.067 261
REMARK 3 PLANARITY : 0.004 268
REMARK 3 DIHEDRAL : 18.113 539
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 3TE3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-AUG-11.
REMARK 100 THE DEPOSITION ID IS D_1000067368.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-AUG-10
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97857
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 8840
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.690
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 11.30
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.69
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 123.86067
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 61.93033
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 92.89550
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 30.96517
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 154.82583
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 123.86067
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 61.93033
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 30.96517
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 92.89550
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 154.82583
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 6650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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: 3940 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 6510 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 699
REMARK 465 LYS A 734
REMARK 465 LEU A 735
REMARK 465 LYS A 736
REMARK 465 MET A 737
REMARK 465 GLY B 699
REMARK 465 GLY B 700
REMARK 465 LYS B 736
REMARK 465 MET B 737
REMARK 465 GLY C 699
REMARK 465 GLY C 700
REMARK 465 GLY D 699
REMARK 465 LYS D 734
REMARK 465 LEU D 735
REMARK 465 LYS D 736
REMARK 465 MET D 737
REMARK 465 GLY E 732
REMARK 465 SER E 733
REMARK 465 LYS E 734
REMARK 465 LEU E 735
REMARK 465 LYS E 736
REMARK 465 MET E 737
REMARK 465 MET F 737
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 TRP A 701 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 701 CZ3 CH2
REMARK 470 VAL A 702 CG1 CG2
REMARK 470 SER A 703 OG
REMARK 470 GLU A 706 CG CD OE1 OE2
REMARK 470 ASP A 729 CG OD1 OD2
REMARK 470 TRP B 701 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 701 CZ3 CH2
REMARK 470 VAL B 702 CG1 CG2
REMARK 470 SER B 703 OG
REMARK 470 GLU B 705 CG CD OE1 OE2
REMARK 470 MET B 709 CG SD CE
REMARK 470 LYS B 734 CG CD CE NZ
REMARK 470 LEU B 735 CG CD1 CD2
REMARK 470 TRP C 701 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP C 701 CZ3 CH2
REMARK 470 SER C 703 OG
REMARK 470 LYS C 734 CG CD CE NZ
REMARK 470 LEU C 735 CG CD1 CD2
REMARK 470 MET C 737 CG SD CE
REMARK 470 VAL D 702 CG1 CG2
REMARK 470 TYR E 708 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLN E 727 CG CD OE1 NE2
REMARK 470 SER F 703 OG
REMARK 470 GLU F 705 CG CD OE1 OE2
REMARK 470 LYS F 734 CG CD CE NZ
REMARK 470 LEU F 735 CG CD1 CD2
REMARK 470 LYS F 736 CG CD CE NZ
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 CB SER A 733 O HOH A 7 2.14
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 VAL A 702 -66.35 -109.17
REMARK 500 SER A 703 74.79 58.50
REMARK 500 SER B 703 -74.17 -134.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 AUTHOR STATES THAT THE REGION CRYSTALLIZED IS ONLY PART OF ORIGINAL
REMARK 999 PROTEIN TARGET DUE TO IN-DROP PROTEOLYSIS. THEY HAVE ATTEMPTED TO
REMARK 999 CRYSTALLIZE THE ENTIRE 137 AA PROTEIN, HOWEVER, MASS SPECTROSCOPIC
REMARK 999 ANALYSIS OF THE CRYSTALS REVEALED THAT THERE HAD BEEN SOME
REMARK 999 PROTEOLYSIS DURING THE CRYSTALLIZATION PROCESS, AND THE CRYSTAL
REMARK 999 ONLY HAD A MASS OF 4338 DA. THIS MASS CORRESPONDS TO THE COILED-
REMARK 999 COIL DOMAIN OF THE FULL LENGTH PROTEIN. SERRES RECORD IN THE PDB
REMARK 999 FILE REPRESETS UNP RESIDUES 699-737.
DBREF 3TE3 A 699 737 UNP Q9P0L9 PK2L1_HUMAN 699 737
DBREF 3TE3 B 699 737 UNP Q9P0L9 PK2L1_HUMAN 699 737
DBREF 3TE3 C 699 737 UNP Q9P0L9 PK2L1_HUMAN 699 737
DBREF 3TE3 D 699 737 UNP Q9P0L9 PK2L1_HUMAN 699 737
DBREF 3TE3 E 699 737 UNP Q9P0L9 PK2L1_HUMAN 699 737
DBREF 3TE3 F 699 737 UNP Q9P0L9 PK2L1_HUMAN 699 737
SEQRES 1 A 39 GLY GLY TRP VAL SER GLY GLU GLU PHE TYR MET LEU THR
SEQRES 2 A 39 ARG ARG VAL LEU GLN LEU GLU THR VAL LEU GLU GLY VAL
SEQRES 3 A 39 VAL SER GLN ILE ASP ALA VAL GLY SER LYS LEU LYS MET
SEQRES 1 B 39 GLY GLY TRP VAL SER GLY GLU GLU PHE TYR MET LEU THR
SEQRES 2 B 39 ARG ARG VAL LEU GLN LEU GLU THR VAL LEU GLU GLY VAL
SEQRES 3 B 39 VAL SER GLN ILE ASP ALA VAL GLY SER LYS LEU LYS MET
SEQRES 1 C 39 GLY GLY TRP VAL SER GLY GLU GLU PHE TYR MET LEU THR
SEQRES 2 C 39 ARG ARG VAL LEU GLN LEU GLU THR VAL LEU GLU GLY VAL
SEQRES 3 C 39 VAL SER GLN ILE ASP ALA VAL GLY SER LYS LEU LYS MET
SEQRES 1 D 39 GLY GLY TRP VAL SER GLY GLU GLU PHE TYR MET LEU THR
SEQRES 2 D 39 ARG ARG VAL LEU GLN LEU GLU THR VAL LEU GLU GLY VAL
SEQRES 3 D 39 VAL SER GLN ILE ASP ALA VAL GLY SER LYS LEU LYS MET
SEQRES 1 E 39 GLY GLY TRP VAL SER GLY GLU GLU PHE TYR MET LEU THR
SEQRES 2 E 39 ARG ARG VAL LEU GLN LEU GLU THR VAL LEU GLU GLY VAL
SEQRES 3 E 39 VAL SER GLN ILE ASP ALA VAL GLY SER LYS LEU LYS MET
SEQRES 1 F 39 GLY GLY TRP VAL SER GLY GLU GLU PHE TYR MET LEU THR
SEQRES 2 F 39 ARG ARG VAL LEU GLN LEU GLU THR VAL LEU GLU GLY VAL
SEQRES 3 F 39 VAL SER GLN ILE ASP ALA VAL GLY SER LYS LEU LYS MET
FORMUL 7 HOH *8(H2 O)
HELIX 1 1 SER A 703 GLY A 732 1 30
HELIX 2 2 GLY B 704 LYS B 734 1 31
HELIX 3 3 SER C 703 SER C 733 1 31
HELIX 4 4 SER D 703 GLY D 732 1 30
HELIX 5 5 SER E 703 ASP E 729 1 27
HELIX 6 6 SER F 703 LEU F 735 1 33
CRYST1 74.634 74.634 185.791 90.00 90.00 120.00 P 65 2 2 72
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 0.013399 0.007736 0.000000 0.00000
SCALE2 0.000000 0.015472 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005382 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
