HEADER MEMBRANE PROTEIN/INHIBITOR 02-APR-18 6CX0
TITLE STRUCTURE OF ATTPC1 D376A
CAVEAT 6CX0 THE DISTANCE BETWEEN RESIDUE A SER 56 AND RESIDUE A GLU 59
CAVEAT 2 6CX0 IS 16.11 ANGSTROM. BUT THERE ARE ONLY 2 RESIDUES (NOT
CAVEAT 3 6CX0 ENOUGH SEQUENCE) TO COVER THE GAP REGION.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TWO PORE CALCIUM CHANNEL PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CALCIUM CHANNEL PROTEIN 1,ATCCH1,FATTY ACID OXYGENATION UP-
COMPND 5 REGULATED PROTEIN 2,VOLTAGE-DEPENDENT CALCIUM CHANNEL PROTEIN TPC1,
COMPND 6 ATTPC1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: MOUSE-EAR CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: TPC1, CCH1, FOU2, AT4G03560, F9H3.19, T5L23.5;
SOURCE 6 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: DSY5;
SOURCE 9 EXPRESSION_SYSTEM_VARIANT: -HIS;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: P423GAL1
KEYWDS ION CHANNEL, TWO-PORE CHANNEL, TPC1, RESTING-STATE, CLOSED, INACTIVE,
KEYWDS 2 MEMBRANE PROTEIN, MEMBRANE PROTEIN-INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.F.KINTZER,R.M.STROUD
REVDAT 4 04-OCT-23 6CX0 1 LINK
REVDAT 3 01-JAN-20 6CX0 1 REMARK
REVDAT 2 03-OCT-18 6CX0 1 JRNL
REVDAT 1 19-SEP-18 6CX0 0
JRNL AUTH A.F.KINTZER,E.M.GREEN,P.K.DOMINIK,M.BRIDGES,J.P.ARMACHE,
JRNL AUTH 2 D.DENEKA,S.S.KIM,W.HUBBELL,A.A.KOSSIAKOFF,Y.CHENG,R.M.STROUD
JRNL TITL STRUCTURAL BASIS FOR ACTIVATION OF VOLTAGE SENSOR DOMAINS IN
JRNL TITL 2 AN ION CHANNEL TPC1.
JRNL REF PROC. NATL. ACAD. SCI. V. 115 E9095 2018
JRNL REF 2 U.S.A.
JRNL REFN ESSN 1091-6490
JRNL PMID 30190435
JRNL DOI 10.1073/PNAS.1805651115
REMARK 2
REMARK 2 RESOLUTION. 3.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1_2575: ???)
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) : 41.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 46.5
REMARK 3 NUMBER OF REFLECTIONS : 8953
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.320
REMARK 3 R VALUE (WORKING SET) : 0.318
REMARK 3 FREE R VALUE : 0.352
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.960
REMARK 3 FREE R VALUE TEST SET COUNT : 444
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 41.0030 - 5.0470 0.93 5779 309 0.3152 0.3472
REMARK 3 2 5.0470 - 4.0071 0.38 2270 112 0.3244 0.3645
REMARK 3 3 4.0071 - 3.5009 0.08 460 23 0.3796 0.4289
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) : 0.500
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 51.070
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 : 0.003 5218
REMARK 3 ANGLE : 0.687 7098
REMARK 3 CHIRALITY : 0.040 810
REMARK 3 PLANARITY : 0.005 867
REMARK 3 DIHEDRAL : 16.873 3005
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 6CX0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-APR-18.
REMARK 100 THE DEPOSITION ID IS D_1000233634.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-FEB-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19231
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.500
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 (%) : 99.7
REMARK 200 DATA REDUNDANCY : 13.60
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.0800
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) : 4.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
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: 5DQQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 72.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SITTING DROP 2MICROLITER DROPS
REMARK 280 CRYSTCHEM 0.1 M GLYCINE, PH 9.3, 50 MM POTASSIUM CHLORIDE, 1 MM
REMARK 280 CALCIUM CHLORIDE, 35% PEG300, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 109.22500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 109.22500
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 44.23500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 77.21000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 44.23500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 77.21000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 109.22500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 44.23500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 77.21000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 109.22500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 44.23500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 77.21000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
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: 8700 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 65630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -191.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 11
REMARK 465 GLY A 12
REMARK 465 GLY A 13
REMARK 465 GLY A 14
REMARK 465 GLY A 15
REMARK 465 THR A 16
REMARK 465 ASP A 17
REMARK 465 ARG A 18
REMARK 465 VAL A 19
REMARK 465 ARG A 20
REMARK 465 ARG A 21
REMARK 465 SER A 22
REMARK 465 GLU A 23
REMARK 465 ALA A 24
REMARK 465 ILE A 25
REMARK 465 THR A 26
REMARK 465 HIS A 27
REMARK 465 GLY A 28
REMARK 465 THR A 29
REMARK 465 PRO A 30
REMARK 465 PHE A 31
REMARK 465 PHE A 57
REMARK 465 GLY A 58
REMARK 465 TYR A 173
REMARK 465 LEU A 174
REMARK 465 SER A 175
REMARK 465 PRO A 176
REMARK 465 LEU A 177
REMARK 465 ALA A 178
REMARK 465 PHE A 179
REMARK 465 ASP A 180
REMARK 465 PHE A 181
REMARK 465 LEU A 182
REMARK 465 PRO A 183
REMARK 465 GLU A 374
REMARK 465 LEU A 375
REMARK 465 ASP A 376
REMARK 465 ASP A 377
REMARK 465 THR A 378
REMARK 465 ARG A 379
REMARK 465 ASP A 380
REMARK 465 PHE A 381
REMARK 465 LYS A 382
REMARK 465 ILE A 383
REMARK 465 PHE A 408
REMARK 465 GLU A 409
REMARK 465 HIS A 410
REMARK 465 PHE A 411
REMARK 465 PRO A 412
REMARK 465 ASP A 519
REMARK 465 GLU A 520
REMARK 465 ASN A 521
REMARK 465 THR A 522
REMARK 465 PHE A 523
REMARK 465 VAL A 591
REMARK 465 ASN A 592
REMARK 465 ALA A 593
REMARK 465 CYS A 687
REMARK 465 GLN A 688
REMARK 465 GLY A 689
REMARK 465 GLN A 690
REMARK 465 ASP A 691
REMARK 465 SER A 692
REMARK 465 GLN A 693
REMARK 465 GLU A 694
REMARK 465 LYS A 695
REMARK 465 ARG A 696
REMARK 465 ASN A 697
REMARK 465 ARG A 698
REMARK 465 ARG A 699
REMARK 465 ARG A 700
REMARK 465 SER A 701
REMARK 465 ALA A 702
REMARK 465 GLY A 703
REMARK 465 SER A 704
REMARK 465 LYS A 705
REMARK 465 SER A 706
REMARK 465 ARG A 707
REMARK 465 SER A 708
REMARK 465 GLN A 709
REMARK 465 ARG A 710
REMARK 465 VAL A 711
REMARK 465 ASP A 712
REMARK 465 THR A 713
REMARK 465 LEU A 714
REMARK 465 LEU A 715
REMARK 465 HIS A 716
REMARK 465 HIS A 717
REMARK 465 MET A 718
REMARK 465 LEU A 719
REMARK 465 GLY A 720
REMARK 465 ASP A 721
REMARK 465 GLU A 722
REMARK 465 LEU A 723
REMARK 465 SER A 724
REMARK 465 LYS A 725
REMARK 465 PRO A 726
REMARK 465 GLU A 727
REMARK 465 CYS A 728
REMARK 465 SER A 729
REMARK 465 THR A 730
REMARK 465 SER A 731
REMARK 465 ASP A 732
REMARK 465 THR A 733
REMARK 465 LEU A 734
REMARK 465 VAL A 735
REMARK 465 PRO A 736
REMARK 465 ARG A 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 LYS A 33 CG CD CE NZ
REMARK 470 ARG A 62 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 69 CG CD NE CZ NH1 NH2
REMARK 470 TYR A 78 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 PHE A 171 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 276 CG CD CE NZ
REMARK 470 PHE A 524 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TRP A 529 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 529 CZ3 CH2
REMARK 470 GLU A 602 CG CD OE1 OE2
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 A 47 37.28 70.31
REMARK 500 ALA A 61 -94.71 -125.83
REMARK 500 PRO A 99 -150.80 -81.63
REMARK 500 CYS A 101 -87.00 -118.66
REMARK 500 TYR A 108 87.21 39.52
REMARK 500 GLU A 111 -2.55 -149.43
REMARK 500 TYR A 114 -143.25 60.95
REMARK 500 VAL A 247 43.01 -105.62
REMARK 500 SER A 250 -132.59 64.66
REMARK 500 THR A 264 9.46 55.75
REMARK 500 ARG A 358 -65.35 -107.86
REMARK 500 PRO A 361 -84.59 -97.46
REMARK 500 ARG A 398 -70.31 -99.54
REMARK 500 ALA A 418 -73.99 -44.57
REMARK 500 GLU A 457 13.82 59.34
REMARK 500 ALA A 604 -75.41 -133.30
REMARK 500 ASN A 612 -159.61 -130.85
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 CA A 805 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 124 OE2
REMARK 620 2 ASP A 170 OD2 67.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 802 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 239 OE1
REMARK 620 2 GLU A 239 OE2 48.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 803 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 240 OD2
REMARK 620 2 ASP A 454 OD2 86.2
REMARK 620 3 GLU A 528 OE1 85.1 2.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 804 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 335 OD1
REMARK 620 2 ASP A 337 OD1 65.5
REMARK 620 3 ASP A 337 OD2 91.0 51.4
REMARK 620 4 GLU A 341 O 61.6 121.3 105.9
REMARK 620 5 GLN A 346 OE1 118.5 104.9 131.8 121.3
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FJ7 A 806
DBREF 6CX0 A 12 733 UNP Q94KI8 TPC1_ARATH 12 733
SEQADV 6CX0 MET A 11 UNP Q94KI8 INITIATING METHIONINE
SEQADV 6CX0 LEU A 734 UNP Q94KI8 EXPRESSION TAG
SEQADV 6CX0 VAL A 735 UNP Q94KI8 EXPRESSION TAG
SEQADV 6CX0 PRO A 736 UNP Q94KI8 EXPRESSION TAG
SEQADV 6CX0 ARG A 737 UNP Q94KI8 EXPRESSION TAG
SEQRES 1 A 727 MET GLY GLY GLY GLY THR ASP ARG VAL ARG ARG SER GLU
SEQRES 2 A 727 ALA ILE THR HIS GLY THR PRO PHE GLN LYS ALA ALA ALA
SEQRES 3 A 727 LEU VAL ASP LEU ALA GLU ASP GLY ILE GLY LEU PRO VAL
SEQRES 4 A 727 GLU ILE LEU ASP GLN SER SER PHE GLY GLU SER ALA ARG
SEQRES 5 A 727 TYR TYR PHE ILE PHE THR ARG LEU ASP LEU ILE TRP SER
SEQRES 6 A 727 LEU ASN TYR PHE ALA LEU LEU PHE LEU ASN PHE PHE GLU
SEQRES 7 A 727 GLN PRO LEU TRP CYS GLU LYS ASN PRO LYS PRO SER CYS
SEQRES 8 A 727 LYS ASP ARG ASP TYR TYR TYR LEU GLY GLU LEU PRO TYR
SEQRES 9 A 727 LEU THR ASN ALA GLU SER ILE ILE TYR GLU VAL ILE THR
SEQRES 10 A 727 LEU ALA ILE LEU LEU VAL HIS THR PHE PHE PRO ILE SER
SEQRES 11 A 727 TYR GLU GLY SER ARG ILE PHE TRP THR SER ARG LEU ASN
SEQRES 12 A 727 LEU VAL LYS VAL ALA CYS VAL VAL ILE LEU PHE VAL ASP
SEQRES 13 A 727 VAL LEU VAL ASP PHE LEU TYR LEU SER PRO LEU ALA PHE
SEQRES 14 A 727 ASP PHE LEU PRO PHE ARG ILE ALA PRO TYR VAL ARG VAL
SEQRES 15 A 727 ILE ILE PHE ILE LEU SER ILE ARG GLU LEU ARG ASP THR
SEQRES 16 A 727 LEU VAL LEU LEU SER GLY MET LEU GLY THR TYR LEU ASN
SEQRES 17 A 727 ILE LEU ALA LEU TRP MET LEU PHE LEU LEU PHE ALA SER
SEQRES 18 A 727 TRP ILE ALA PHE VAL MET PHE GLU ASP THR GLN GLN GLY
SEQRES 19 A 727 LEU THR VAL PHE THR SER TYR GLY ALA THR LEU TYR GLN
SEQRES 20 A 727 MET PHE ILE LEU PHE THR THR SER ASN ASN PRO ASP VAL
SEQRES 21 A 727 TRP ILE PRO ALA TYR LYS SER SER ARG TRP SER SER VAL
SEQRES 22 A 727 PHE PHE VAL LEU TYR VAL LEU ILE GLY VAL TYR PHE VAL
SEQRES 23 A 727 THR ASN LEU ILE LEU ALA VAL VAL TYR ASP SER PHE LYS
SEQRES 24 A 727 GLU GLN LEU ALA LYS GLN VAL SER GLY MET ASP GLN MET
SEQRES 25 A 727 LYS ARG ARG MET LEU GLU LYS ALA PHE GLY LEU ILE ASP
SEQRES 26 A 727 SER ASP LYS ASN GLY GLU ILE ASP LYS ASN GLN CYS ILE
SEQRES 27 A 727 LYS LEU PHE GLU GLN LEU THR ASN TYR ARG THR LEU PRO
SEQRES 28 A 727 LYS ILE SER LYS GLU GLU PHE GLY LEU ILE PHE ASP GLU
SEQRES 29 A 727 LEU ASP ASP THR ARG ASP PHE LYS ILE ASN LYS ASP GLU
SEQRES 30 A 727 PHE ALA ASP LEU CYS GLN ALA ILE ALA LEU ARG PHE GLN
SEQRES 31 A 727 LYS GLU GLU VAL PRO SER LEU PHE GLU HIS PHE PRO GLN
SEQRES 32 A 727 ILE TYR HIS SER ALA LEU SER GLN GLN LEU ARG ALA PHE
SEQRES 33 A 727 VAL ARG SER PRO ASN PHE GLY TYR ALA ILE SER PHE ILE
SEQRES 34 A 727 LEU ILE ILE ASN PHE ILE ALA VAL VAL VAL GLU THR THR
SEQRES 35 A 727 LEU ASP ILE GLU GLU SER SER ALA GLN LYS PRO TRP GLN
SEQRES 36 A 727 VAL ALA GLU PHE VAL PHE GLY TRP ILE TYR VAL LEU GLU
SEQRES 37 A 727 MET ALA LEU LYS ILE TYR THR TYR GLY PHE GLU ASN TYR
SEQRES 38 A 727 TRP ARG GLU GLY ALA ASN ARG PHE ASP PHE LEU VAL THR
SEQRES 39 A 727 TRP VAL ILE VAL ILE GLY GLU THR ALA THR PHE ILE THR
SEQRES 40 A 727 PRO ASP GLU ASN THR PHE PHE SER ASN GLY GLU TRP ILE
SEQRES 41 A 727 ARG TYR LEU LEU LEU ALA ARG MET LEU ARG LEU ILE ARG
SEQRES 42 A 727 LEU LEU MET ASN VAL GLN ARG TYR ARG ALA PHE ILE ALA
SEQRES 43 A 727 THR PHE ILE THR LEU ILE PRO SER LEU MET PRO TYR LEU
SEQRES 44 A 727 GLY THR ILE PHE CYS VAL LEU CYS ILE TYR CYS SER ILE
SEQRES 45 A 727 GLY VAL GLN VAL PHE GLY GLY LEU VAL ASN ALA GLY ASN
SEQRES 46 A 727 LYS LYS LEU PHE GLU THR GLU LEU ALA GLU ASP ASP TYR
SEQRES 47 A 727 LEU LEU PHE ASN PHE ASN ASP TYR PRO ASN GLY MET VAL
SEQRES 48 A 727 THR LEU PHE ASN LEU LEU VAL MET GLY ASN TRP GLN VAL
SEQRES 49 A 727 TRP MET GLU SER TYR LYS ASP LEU THR GLY THR TRP TRP
SEQRES 50 A 727 SER ILE THR TYR PHE VAL SER PHE TYR VAL ILE THR ILE
SEQRES 51 A 727 LEU LEU LEU LEU ASN LEU VAL VAL ALA PHE VAL LEU GLU
SEQRES 52 A 727 ALA PHE PHE THR GLU LEU ASP LEU GLU GLU GLU GLU LYS
SEQRES 53 A 727 CYS GLN GLY GLN ASP SER GLN GLU LYS ARG ASN ARG ARG
SEQRES 54 A 727 ARG SER ALA GLY SER LYS SER ARG SER GLN ARG VAL ASP
SEQRES 55 A 727 THR LEU LEU HIS HIS MET LEU GLY ASP GLU LEU SER LYS
SEQRES 56 A 727 PRO GLU CYS SER THR SER ASP THR LEU VAL PRO ARG
HET CA A 801 1
HET CA A 802 1
HET CA A 803 1
HET CA A 804 1
HET CA A 805 1
HET FJ7 A 806 38
HETNAM CA CALCIUM ION
HETNAM FJ7 (1S,3R)-1-(3-{[4-(2-FLUOROPHENYL)PIPERAZIN-1-
HETNAM 2 FJ7 YL]METHYL}-4-METHOXYPHENYL)-2,3,4,9-TETRAHYDRO-1H-
HETNAM 3 FJ7 BETA-CARBOLINE-3-CARBOXYLIC ACID
FORMUL 2 CA 5(CA 2+)
FORMUL 7 FJ7 C30 H31 F N4 O3
HELIX 1 AA1 ALA A 34 LEU A 47 1 14
HELIX 2 AA2 ARG A 62 LEU A 70 1 9
HELIX 3 AA3 LEU A 70 GLU A 88 1 19
HELIX 4 AA4 THR A 116 PHE A 136 1 21
HELIX 5 AA5 PHE A 137 GLU A 142 1 6
HELIX 6 AA6 GLY A 143 SER A 150 1 8
HELIX 7 AA7 SER A 150 LEU A 172 1 23
HELIX 8 AA8 ILE A 186 LEU A 197 1 12
HELIX 9 AA9 ILE A 199 PHE A 238 1 40
HELIX 10 AB1 THR A 241 LEU A 245 5 5
HELIX 11 AB2 SER A 250 THR A 263 1 14
HELIX 12 AB3 ASN A 266 TRP A 271 1 6
HELIX 13 AB4 TRP A 271 SER A 278 1 8
HELIX 14 AB5 SER A 281 PHE A 295 1 15
HELIX 15 AB6 PHE A 295 ASP A 335 1 41
HELIX 16 AB7 ASP A 343 ARG A 358 1 16
HELIX 17 AB8 GLU A 367 ASP A 373 1 7
HELIX 18 AB9 LYS A 385 ARG A 398 1 14
HELIX 19 AC1 SER A 417 SER A 429 1 13
HELIX 20 AC2 SER A 429 GLU A 456 1 28
HELIX 21 AC3 ALA A 460 GLY A 487 1 28
HELIX 22 AC4 GLY A 487 GLU A 494 1 8
HELIX 23 AC5 GLU A 494 THR A 517 1 24
HELIX 24 AC6 GLY A 527 LEU A 533 1 7
HELIX 25 AC7 LEU A 534 ASN A 547 5 14
HELIX 26 AC8 VAL A 548 LEU A 565 1 18
HELIX 27 AC9 LEU A 565 PHE A 587 1 23
HELIX 28 AD1 LYS A 597 LEU A 603 1 7
HELIX 29 AD2 ASP A 615 VAL A 628 1 14
HELIX 30 AD3 TRP A 632 GLY A 644 1 13
HELIX 31 AD4 THR A 645 SER A 648 5 4
HELIX 32 AD5 ILE A 649 ILE A 660 1 12
HELIX 33 AD6 LEU A 662 LYS A 686 1 25
LINK OE2 GLU A 124 CA CA A 805 1555 1555 2.54
LINK OD2 ASP A 170 CA CA A 805 1555 1555 2.87
LINK OE1 GLU A 239 CA CA A 802 1555 4555 2.68
LINK OE2 GLU A 239 CA CA A 802 1555 4555 2.66
LINK OD2 ASP A 240 CA CA A 803 1555 4555 2.43
LINK OD1 ASP A 335 CA CA A 804 1555 1555 2.93
LINK OD1 ASP A 337 CA CA A 804 1555 1555 2.47
LINK OD2 ASP A 337 CA CA A 804 1555 1555 2.59
LINK O GLU A 341 CA CA A 804 1555 1555 2.48
LINK OE1 GLN A 346 CA CA A 804 1555 1555 2.94
LINK OD2 ASP A 454 CA CA A 803 1555 1555 2.66
LINK OE1 GLU A 528 CA CA A 803 1555 1555 2.46
CISPEP 1 SER A 100 CYS A 101 0 5.06
SITE 1 AC1 3 LEU A 609 ASN A 612 ASN A 625
SITE 1 AC2 1 GLU A 239
SITE 1 AC3 3 ASP A 240 ASP A 454 GLU A 528
SITE 1 AC4 7 ASP A 335 ASP A 337 ASN A 339 GLU A 341
SITE 2 AC4 7 ILE A 342 ASP A 343 GLN A 346
SITE 1 AC5 3 TRP A 92 GLU A 124 ASP A 170
SITE 1 AC6 3 PHE A 229 TRP A 232 TYR A 251
CRYST1 88.470 154.420 218.450 90.00 90.00 90.00 C 2 2 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.011303 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006476 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004578 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
