HEADER MEMBRANE PROTEIN 16-FEB-16 5I74
TITLE X-RAY STRUCTURE OF THE TS3 HUMAN SEROTONIN TRANSPORTER COMPLEXED WITH
TITLE 2 BR-CITALOPRAM AT THE CENTRAL SITE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SODIUM-DEPENDENT SEROTONIN TRANSPORTER;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SERT,5HT TRANSPORTER,5HTT,SOLUTE CARRIER FAMILY 6 MEMBER 4;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: 8B6 ANTIBODY, HEAVY CHAIN;
COMPND 8 CHAIN: B;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 3;
COMPND 11 MOLECULE: 8B6 ANTIBODY, LIGHT CHAIN;
COMPND 12 CHAIN: C;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: SLC6A4, HTT, SERT;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 10 ORGANISM_TAXID: 10090;
SOURCE 11 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 13 MOL_ID: 3;
SOURCE 14 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 15 ORGANISM_TAXID: 10090;
SOURCE 16 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.A.COLEMAN,E.M.GREEN,E.GOUAUX
REVDAT 5 29-JUL-20 5I74 1 COMPND REMARK HETNAM LINK
REVDAT 5 2 1 SITE
REVDAT 4 04-MAR-20 5I74 1 JRNL REMARK
REVDAT 3 04-MAY-16 5I74 1 JRNL
REVDAT 2 20-APR-16 5I74 1 JRNL
REVDAT 1 13-APR-16 5I74 0
JRNL AUTH J.A.COLEMAN,E.M.GREEN,E.GOUAUX
JRNL TITL X-RAY STRUCTURES AND MECHANISM OF THE HUMAN SEROTONIN
JRNL TITL 2 TRANSPORTER.
JRNL REF NATURE V. 532 334 2016
JRNL REFN ESSN 1476-4687
JRNL PMID 27049939
JRNL DOI 10.1038/NATURE17629
REMARK 2
REMARK 2 RESOLUTION. 3.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV_1634
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) : 3.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 101.68
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.400
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 39603
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.251
REMARK 3 R VALUE (WORKING SET) : 0.249
REMARK 3 FREE R VALUE : 0.296
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1980
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1101.7235 - 8.1807 0.99 2703 144 0.2551 0.2697
REMARK 3 2 8.1807 - 6.4936 1.00 2691 141 0.2663 0.2935
REMARK 3 3 6.4936 - 5.6728 1.00 2717 141 0.2470 0.3600
REMARK 3 4 5.6728 - 5.1542 1.00 2697 138 0.2251 0.2850
REMARK 3 5 5.1542 - 4.7847 1.00 2719 148 0.1951 0.2362
REMARK 3 6 4.7847 - 4.5026 1.00 2702 140 0.1875 0.3153
REMARK 3 7 4.5026 - 4.2771 1.00 2705 147 0.1973 0.2837
REMARK 3 8 4.2771 - 4.0910 1.00 2703 137 0.2214 0.2608
REMARK 3 9 4.0910 - 3.9335 1.00 2710 147 0.2585 0.3480
REMARK 3 10 3.9335 - 3.7977 1.00 2674 142 0.2635 0.2965
REMARK 3 11 3.7977 - 3.6790 1.00 2723 141 0.2918 0.3292
REMARK 3 12 3.6790 - 3.5738 0.99 2680 139 0.3316 0.3740
REMARK 3 13 3.5738 - 3.4797 0.99 2655 141 0.3507 0.4033
REMARK 3 14 3.4797 - 3.3948 0.93 2544 134 0.3853 0.4498
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) : 0.610
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.360
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 7837
REMARK 3 ANGLE : 1.005 10693
REMARK 3 CHIRALITY : 0.216 1209
REMARK 3 PLANARITY : 0.003 1317
REMARK 3 DIHEDRAL : 10.689 2676
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 5
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN B AND RESID 21:138)
REMARK 3 ORIGIN FOR THE GROUP (A): 54.7581 167.7348 52.8472
REMARK 3 T TENSOR
REMARK 3 T11: 1.1979 T22: 1.2526
REMARK 3 T33: 1.0964 T12: 0.0229
REMARK 3 T13: -0.2499 T23: 0.1725
REMARK 3 L TENSOR
REMARK 3 L11: 3.4450 L22: 5.5808
REMARK 3 L33: 2.9971 L12: 1.6087
REMARK 3 L13: -0.3903 L23: -1.9264
REMARK 3 S TENSOR
REMARK 3 S11: -0.2977 S12: -0.9492 S13: -0.2952
REMARK 3 S21: 0.5578 S22: -0.0607 S23: -1.7283
REMARK 3 S31: -0.6292 S32: -0.1929 S33: 0.2804
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN B AND RESID 139:237)
REMARK 3 ORIGIN FOR THE GROUP (A): 23.9917 159.3887 45.3075
REMARK 3 T TENSOR
REMARK 3 T11: 3.3294 T22: 3.2489
REMARK 3 T33: 2.3345 T12: -1.2140
REMARK 3 T13: 0.7023 T23: -0.6760
REMARK 3 L TENSOR
REMARK 3 L11: 3.9552 L22: 1.5072
REMARK 3 L33: 2.2219 L12: 1.1124
REMARK 3 L13: -1.6803 L23: 0.8672
REMARK 3 S TENSOR
REMARK 3 S11: -0.5072 S12: -0.1473 S13: -0.4829
REMARK 3 S21: -2.2608 S22: 0.2344 S23: 0.0930
REMARK 3 S31: 0.7594 S32: 1.5721 S33: 0.5971
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN C AND RESID 22:124)
REMARK 3 ORIGIN FOR THE GROUP (A): 44.8634 187.4159 53.6391
REMARK 3 T TENSOR
REMARK 3 T11: 1.6841 T22: 1.6235
REMARK 3 T33: 1.8001 T12: 0.5412
REMARK 3 T13: -0.3467 T23: -0.3432
REMARK 3 L TENSOR
REMARK 3 L11: 4.3000 L22: 4.6069
REMARK 3 L33: 4.4366 L12: 1.2111
REMARK 3 L13: -1.9262 L23: -1.3818
REMARK 3 S TENSOR
REMARK 3 S11: 0.1529 S12: 1.2929 S13: 0.8329
REMARK 3 S21: 0.5333 S22: 0.1014 S23: 1.8679
REMARK 3 S31: -0.4854 S32: -1.7015 S33: -0.1149
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN C AND RESID 125:234)
REMARK 3 ORIGIN FOR THE GROUP (A): 13.5896 166.5757 55.1462
REMARK 3 T TENSOR
REMARK 3 T11: 1.6458 T22: 5.9428
REMARK 3 T33: 3.7942 T12: -1.1364
REMARK 3 T13: 0.9332 T23: -0.7965
REMARK 3 L TENSOR
REMARK 3 L11: 1.2495 L22: 3.7077
REMARK 3 L33: 0.7311 L12: 0.8487
REMARK 3 L13: -0.0277 L23: -1.5684
REMARK 3 S TENSOR
REMARK 3 S11: -0.5716 S12: -0.5060 S13: -2.6481
REMARK 3 S21: -0.2972 S22: 0.3742 S23: 2.7440
REMARK 3 S31: 1.3743 S32: -3.9366 S33: -1.0646
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 74:615)
REMARK 3 ORIGIN FOR THE GROUP (A): 36.8520 186.2848 2.9308
REMARK 3 T TENSOR
REMARK 3 T11: 1.0732 T22: 1.3779
REMARK 3 T33: 1.1987 T12: 0.3276
REMARK 3 T13: -0.2576 T23: 0.0355
REMARK 3 L TENSOR
REMARK 3 L11: 2.9541 L22: 1.3580
REMARK 3 L33: 3.3384 L12: 0.4190
REMARK 3 L13: 1.7909 L23: -0.2722
REMARK 3 S TENSOR
REMARK 3 S11: -0.5507 S12: -0.4384 S13: 0.4869
REMARK 3 S21: 0.0473 S22: -0.0832 S23: 0.1017
REMARK 3 S31: -0.7964 S32: -0.4007 S33: 0.5259
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 5I74 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-FEB-16.
REMARK 100 THE DEPOSITION ID IS D_1000218381.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-NOV-15
REMARK 200 TEMPERATURE (KELVIN) : 100
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 : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.902
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41581
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.395
REMARK 200 RESOLUTION RANGE LOW (A) : 101.680
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 10.70
REMARK 200 R MERGE (I) : 0.06051
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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 (%): 63.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS PH 8.5, 125 MM NACL, 125
REMARK 280 MM MAGNESIUM CHLORIDE, 33.4% PEG 400, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 277K
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 70.08500
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 70.08500
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 64.79500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 82.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 64.79500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 82.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 70.08500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 64.79500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 82.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 70.08500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 64.79500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 82.00000
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6960 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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 APPLY THE FOLLOWING TO CHAINS: B, C
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 129.59000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 70.08500
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 THR A 616
REMARK 465 PRO A 617
REMARK 465 THR A 618
REMARK 465 LEU A 619
REMARK 465 VAL A 620
REMARK 465 PRO A 621
REMARK 465 ARG A 622
REMARK 465 SER B 238
REMARK 465 GLY B 239
REMARK 465 PRO B 240
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 SER A 75 OG
REMARK 470 GLN A 76 CG CD OE1 NE2
REMARK 470 ARG A 79 CG CD NE CZ NH1 NH2
REMARK 470 TRP A 82 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 82 CZ3 CH2
REMARK 470 ASN A 145 CG OD1 ND2
REMARK 470 LYS A 201 CG CD CE NZ
REMARK 470 LYS A 275 CG CD CE NZ
REMARK 470 ASP A 393 CG OD1 OD2
REMARK 470 GLU A 463 CG CD OE1 OE2
REMARK 470 ARG A 464 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 538 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 597 CG CD1 CD2
REMARK 470 ILE A 598 CG1 CG2 CD1
REMARK 470 ILE A 599 CG1 CG2 CD1
REMARK 470 THR A 600 OG1 CG2
REMARK 470 THR A 603 OG1 CG2
REMARK 470 PHE A 604 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 605 CG CD CE NZ
REMARK 470 GLU A 606 CG CD OE1 OE2
REMARK 470 ARG A 607 CG CD NE CZ NH1 NH2
REMARK 470 ILE A 608 CG1 CG2 CD1
REMARK 470 ILE A 609 CG1 CG2 CD1
REMARK 470 LYS A 610 CG CD CE NZ
REMARK 470 SER A 611 OG
REMARK 470 ILE A 612 CG1 CG2 CD1
REMARK 470 THR A 613 OG1 CG2
REMARK 470 GLU A 615 CG CD OE1 OE2
REMARK 470 GLU B 20 CG CD OE1 OE2
REMARK 470 ASN C 232 CG OD1 ND2
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 ILE A 148 -61.48 -104.62
REMARK 500 ILE A 154 -74.91 -122.63
REMARK 500 ASN A 217 -4.16 68.17
REMARK 500 HIS A 235 -74.17 -111.34
REMARK 500 ILE A 270 -55.98 -127.55
REMARK 500 ASN A 351 171.82 177.16
REMARK 500 GLU A 392 -139.88 42.45
REMARK 500 HIS A 456 -16.90 67.55
REMARK 500 ALA A 459 -1.60 69.45
REMARK 500 ALA A 496 -67.15 -126.35
REMARK 500 PHE A 515 -70.15 -116.78
REMARK 500 ALA A 543 -59.95 -123.51
REMARK 500 LYS B 86 -63.90 -97.90
REMARK 500 ARG B 121 135.52 -175.22
REMARK 500 PRO B 172 -166.17 -76.58
REMARK 500 SER C 50 -133.29 59.34
REMARK 500 SER C 70 70.72 55.28
REMARK 500 ALA C 71 -115.62 58.04
REMARK 500 ALA C 104 -177.14 -170.38
REMARK 500 ASN C 158 71.07 58.20
REMARK 500 TYR C 160 138.05 -177.34
REMARK 500 ILE C 170 -74.21 -75.30
REMARK 500 LYS C 189 -72.30 -111.42
REMARK 500 ASN C 210 -74.93 -115.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5I75 RELATED DB: PDB
REMARK 900 RELATED ID: 5I73 RELATED DB: PDB
REMARK 900 RELATED ID: 5I71 RELATED DB: PDB
REMARK 900 RELATED ID: 5I6X RELATED DB: PDB
REMARK 900 RELATED ID: 5I6Z RELATED DB: PDB
DBREF 5I74 A 76 618 UNP P31645 SC6A4_HUMAN 76 618
DBREF 5I74 B 20 240 PDB 5I74 5I74 20 240
DBREF 5I74 C 21 234 PDB 5I74 5I74 21 234
SEQADV 5I74 GLY A 74 UNP P31645 CLONING ARTIFACT
SEQADV 5I74 SER A 75 UNP P31645 CLONING ARTIFACT
SEQADV 5I74 ALA A 110 UNP P31645 TYR 110 ENGINEERED MUTATION
SEQADV 5I74 ALA A 291 UNP P31645 ILE 291 ENGINEERED MUTATION
SEQADV 5I74 SER A 439 UNP P31645 THR 439 ENGINEERED MUTATION
SEQADV 5I74 ALA A 554 UNP P31645 CYS 554 ENGINEERED MUTATION
SEQADV 5I74 ALA A 580 UNP P31645 CYS 580 ENGINEERED MUTATION
SEQADV 5I74 LEU A 619 UNP P31645 CLONING ARTIFACT
SEQADV 5I74 VAL A 620 UNP P31645 CLONING ARTIFACT
SEQADV 5I74 PRO A 621 UNP P31645 CLONING ARTIFACT
SEQADV 5I74 ARG A 622 UNP P31645 CLONING ARTIFACT
SEQRES 1 A 549 GLY SER GLN GLY GLU ARG GLU THR TRP GLY LYS LYS VAL
SEQRES 2 A 549 ASP PHE LEU LEU SER VAL ILE GLY TYR ALA VAL ASP LEU
SEQRES 3 A 549 GLY ASN VAL TRP ARG PHE PRO TYR ILE CYS ALA GLN ASN
SEQRES 4 A 549 GLY GLY GLY ALA PHE LEU LEU PRO TYR THR ILE MET ALA
SEQRES 5 A 549 ILE PHE GLY GLY ILE PRO LEU PHE TYR MET GLU LEU ALA
SEQRES 6 A 549 LEU GLY GLN TYR HIS ARG ASN GLY CYS ILE SER ILE TRP
SEQRES 7 A 549 ARG LYS ILE CYS PRO ILE PHE LYS GLY ILE GLY TYR ALA
SEQRES 8 A 549 ILE CYS ILE ILE ALA PHE TYR ILE ALA SER TYR TYR ASN
SEQRES 9 A 549 THR ILE MET ALA TRP ALA LEU TYR TYR LEU ILE SER SER
SEQRES 10 A 549 PHE THR ASP GLN LEU PRO TRP THR SER CYS LYS ASN SER
SEQRES 11 A 549 TRP ASN THR GLY ASN CYS THR ASN TYR PHE SER GLU ASP
SEQRES 12 A 549 ASN ILE THR TRP THR LEU HIS SER THR SER PRO ALA GLU
SEQRES 13 A 549 GLU PHE TYR THR ARG HIS VAL LEU GLN ILE HIS ARG SER
SEQRES 14 A 549 LYS GLY LEU GLN ASP LEU GLY GLY ILE SER TRP GLN LEU
SEQRES 15 A 549 ALA LEU CYS ILE MET LEU ILE PHE THR VAL ILE TYR PHE
SEQRES 16 A 549 SER ILE TRP LYS GLY VAL LYS THR SER GLY LYS VAL VAL
SEQRES 17 A 549 TRP VAL THR ALA THR PHE PRO TYR ILE ALA LEU SER VAL
SEQRES 18 A 549 LEU LEU VAL ARG GLY ALA THR LEU PRO GLY ALA TRP ARG
SEQRES 19 A 549 GLY VAL LEU PHE TYR LEU LYS PRO ASN TRP GLN LYS LEU
SEQRES 20 A 549 LEU GLU THR GLY VAL TRP ILE ASP ALA ALA ALA GLN ILE
SEQRES 21 A 549 PHE PHE SER LEU GLY PRO GLY PHE GLY VAL LEU LEU ALA
SEQRES 22 A 549 PHE ALA SER TYR ASN LYS PHE ASN ASN ASN CYS TYR GLN
SEQRES 23 A 549 ASP ALA LEU VAL THR SER VAL VAL ASN CYS MET THR SER
SEQRES 24 A 549 PHE VAL SER GLY PHE VAL ILE PHE THR VAL LEU GLY TYR
SEQRES 25 A 549 MET ALA GLU MET ARG ASN GLU ASP VAL SER GLU VAL ALA
SEQRES 26 A 549 LYS ASP ALA GLY PRO SER LEU LEU PHE ILE THR TYR ALA
SEQRES 27 A 549 GLU ALA ILE ALA ASN MET PRO ALA SER THR PHE PHE ALA
SEQRES 28 A 549 ILE ILE PHE PHE LEU MET LEU ILE THR LEU GLY LEU ASP
SEQRES 29 A 549 SER SER PHE ALA GLY LEU GLU GLY VAL ILE THR ALA VAL
SEQRES 30 A 549 LEU ASP GLU PHE PRO HIS VAL TRP ALA LYS ARG ARG GLU
SEQRES 31 A 549 ARG PHE VAL LEU ALA VAL VAL ILE THR CYS PHE PHE GLY
SEQRES 32 A 549 SER LEU VAL THR LEU THR PHE GLY GLY ALA TYR VAL VAL
SEQRES 33 A 549 LYS LEU LEU GLU GLU TYR ALA THR GLY PRO ALA VAL LEU
SEQRES 34 A 549 THR VAL ALA LEU ILE GLU ALA VAL ALA VAL SER TRP PHE
SEQRES 35 A 549 TYR GLY ILE THR GLN PHE CYS ARG ASP VAL LYS GLU MET
SEQRES 36 A 549 LEU GLY PHE SER PRO GLY TRP PHE TRP ARG ILE CYS TRP
SEQRES 37 A 549 VAL ALA ILE SER PRO LEU PHE LEU LEU PHE ILE ILE ALA
SEQRES 38 A 549 SER PHE LEU MET SER PRO PRO GLN LEU ARG LEU PHE GLN
SEQRES 39 A 549 TYR ASN TYR PRO TYR TRP SER ILE ILE LEU GLY TYR ALA
SEQRES 40 A 549 ILE GLY THR SER SER PHE ILE CYS ILE PRO THR TYR ILE
SEQRES 41 A 549 ALA TYR ARG LEU ILE ILE THR PRO GLY THR PHE LYS GLU
SEQRES 42 A 549 ARG ILE ILE LYS SER ILE THR PRO GLU THR PRO THR LEU
SEQRES 43 A 549 VAL PRO ARG
SEQRES 1 B 221 GLU VAL GLN LEU GLN GLN SER GLY PRO GLU LEU VAL LYS
SEQRES 2 B 221 PRO GLY ALA SER VAL LYS ILE SER CYS LYS ALA SER GLY
SEQRES 3 B 221 TYR THR PHE THR ASP TYR TYR MET ASN TRP VAL LYS GLN
SEQRES 4 B 221 SER HIS GLY LYS SER LEU GLU TRP ILE GLY ASN ILE ASN
SEQRES 5 B 221 PRO ASN ASN GLY GLY THR SER TYR ASN GLN LYS PHE LYS
SEQRES 6 B 221 GLY LYS ALA THR LEU THR VAL ASP LYS SER SER THR THR
SEQRES 7 B 221 ALA TYR MET GLU LEU ARG SER LEU THR SER GLU ASP SER
SEQRES 8 B 221 ALA VAL TYR TYR CYS THR ARG SER PRO VAL ARG PRO TYR
SEQRES 9 B 221 TYR PHE ASP TYR TRP GLY GLN GLY THR THR LEU THR VAL
SEQRES 10 B 221 SER SER ALA LYS THR THR PRO PRO SER VAL TYR PRO LEU
SEQRES 11 B 221 ALA PRO GLY CYS GLY ASP THR THR GLY SER SER VAL THR
SEQRES 12 B 221 LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU SER VAL
SEQRES 13 B 221 THR VAL THR TRP ASN SER GLY SER LEU SER SER SER VAL
SEQRES 14 B 221 HIS THR PHE PRO ALA LEU LEU GLN SER GLY LEU TYR THR
SEQRES 15 B 221 MET SER SER SER VAL THR VAL PRO SER SER THR TRP PRO
SEQRES 16 B 221 SER GLN THR VAL THR CYS SER VAL ALA HIS PRO ALA SER
SEQRES 17 B 221 SER THR THR VAL ASP LYS LYS LEU GLU PRO SER GLY PRO
SEQRES 1 C 214 ASP ILE VAL MET THR GLN SER HIS LYS PHE MET SER THR
SEQRES 2 C 214 SER VAL GLY ASP ARG VAL SER ILE THR CYS LYS ALA SER
SEQRES 3 C 214 GLN ASP VAL SER THR ALA VAL ALA TRP TYR GLN GLN LYS
SEQRES 4 C 214 PRO GLY GLN SER PRO LYS LEU LEU ILE TYR SER ALA SER
SEQRES 5 C 214 TYR ARG TYR THR GLY VAL PRO ASP ARG PHE THR GLY SER
SEQRES 6 C 214 GLY SER GLY THR ASP PHE THR PHE THR ILE SER SER VAL
SEQRES 7 C 214 GLN ALA GLU ASP LEU ALA VAL TYR TYR CYS GLN GLN HIS
SEQRES 8 C 214 TYR SER ILE PRO ARG THR PHE GLY GLY GLY THR LYS LEU
SEQRES 9 C 214 GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE
SEQRES 10 C 214 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA
SEQRES 11 C 214 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP
SEQRES 12 C 214 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN
SEQRES 13 C 214 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS
SEQRES 14 C 214 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR
SEQRES 15 C 214 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU
SEQRES 16 C 214 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER
SEQRES 17 C 214 PHE ASN ARG ASN GLU CYS
HET 69D A 700 24
HET NAG A 701 14
HET CLR A 702 28
HET D12 A 703 12
HET HEX A 704 6
HET NAG A 705 14
HETNAM 69D (1S)-1-(4-BROMOPHENYL)-1-[3-(DIMETHYLAMINO)PROPYL]-1,3-
HETNAM 2 69D DIHYDRO-2-BENZOFURAN-5-CARBONITRILE
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM CLR CHOLESTEROL
HETNAM D12 DODECANE
HETNAM HEX HEXANE
FORMUL 4 69D C20 H21 BR N2 O
FORMUL 5 NAG 2(C8 H15 N O6)
FORMUL 6 CLR C27 H46 O
FORMUL 7 D12 C12 H26
FORMUL 8 HEX C6 H14
HELIX 1 AA1 LYS A 84 VAL A 97 1 14
HELIX 2 AA2 ASP A 98 TRP A 103 1 6
HELIX 3 AA3 TRP A 103 ASN A 112 1 10
HELIX 4 AA4 GLY A 113 ALA A 116 5 4
HELIX 5 AA5 PHE A 117 PHE A 127 1 11
HELIX 6 AA6 GLY A 128 ARG A 144 1 17
HELIX 7 AA7 ILE A 148 LYS A 153 1 6
HELIX 8 AA8 CYS A 155 ILE A 157 5 3
HELIX 9 AA9 PHE A 158 SER A 189 1 32
HELIX 10 AB1 SER A 190 THR A 192 5 3
HELIX 11 AB2 SER A 226 HIS A 235 1 10
HELIX 12 AB3 GLN A 238 SER A 242 5 5
HELIX 13 AB4 SER A 252 PHE A 268 1 17
HELIX 14 AB5 GLY A 273 VAL A 280 1 8
HELIX 15 AB6 VAL A 280 THR A 301 1 22
HELIX 16 AB7 ALA A 305 LYS A 314 1 10
HELIX 17 AB8 GLU A 322 GLY A 338 1 17
HELIX 18 AB9 GLY A 342 TYR A 350 1 9
HELIX 19 AC1 ASN A 356 ARG A 390 1 35
HELIX 20 AC2 ASP A 393 ALA A 398 1 6
HELIX 21 AC3 GLY A 402 ILE A 408 1 7
HELIX 22 AC4 ILE A 408 ASN A 416 1 9
HELIX 23 AC5 ALA A 419 PHE A 454 1 36
HELIX 24 AC6 ARG A 461 SER A 477 1 17
HELIX 25 AC7 GLY A 484 ALA A 496 1 13
HELIX 26 AC8 ALA A 496 PHE A 515 1 20
HELIX 27 AC9 GLY A 517 LEU A 529 1 13
HELIX 28 AD1 GLY A 534 ALA A 543 1 10
HELIX 29 AD2 ALA A 543 SER A 559 1 17
HELIX 30 AD3 TRP A 573 ILE A 587 1 15
HELIX 31 AD4 ILE A 587 THR A 600 1 14
HELIX 32 AD5 THR A 603 THR A 613 1 11
HELIX 33 AD6 THR B 47 TYR B 51 5 5
HELIX 34 AD7 THR B 106 SER B 110 5 5
HELIX 35 AD8 SER B 181 SER B 183 5 3
HELIX 36 AD9 GLN C 99 LEU C 103 5 5
HELIX 37 AE1 SER C 141 SER C 147 1 7
HELIX 38 AE2 LYS C 203 GLU C 207 1 5
SHEET 1 AA1 2 ARG A 564 LEU A 565 0
SHEET 2 AA1 2 TYR A 568 ASN A 569 -1 O TYR A 568 N LEU A 565
SHEET 1 AA2 4 GLN B 22 GLN B 25 0
SHEET 2 AA2 4 VAL B 37 SER B 44 -1 O LYS B 42 N GLN B 24
SHEET 3 AA2 4 THR B 97 LEU B 102 -1 O LEU B 102 N VAL B 37
SHEET 4 AA2 4 ALA B 87 ASP B 92 -1 N THR B 90 O TYR B 99
SHEET 1 AA3 6 GLU B 29 VAL B 31 0
SHEET 2 AA3 6 THR B 132 VAL B 136 1 O THR B 135 N GLU B 29
SHEET 3 AA3 6 ALA B 111 SER B 118 -1 N TYR B 113 O THR B 132
SHEET 4 AA3 6 TYR B 52 GLN B 58 -1 N GLN B 58 O VAL B 112
SHEET 5 AA3 6 LEU B 64 ASN B 71 -1 O ILE B 67 N TRP B 55
SHEET 6 AA3 6 GLY B 76 TYR B 79 -1 O SER B 78 N ASN B 69
SHEET 1 AA4 4 GLU B 29 VAL B 31 0
SHEET 2 AA4 4 THR B 132 VAL B 136 1 O THR B 135 N GLU B 29
SHEET 3 AA4 4 ALA B 111 SER B 118 -1 N TYR B 113 O THR B 132
SHEET 4 AA4 4 TYR B 127 TRP B 128 -1 O TYR B 127 N ARG B 117
SHEET 1 AA5 4 SER B 145 LEU B 149 0
SHEET 2 AA5 4 SER B 160 TYR B 170 -1 O LYS B 168 N SER B 145
SHEET 3 AA5 4 LEU B 199 PRO B 209 -1 O TYR B 200 N TYR B 170
SHEET 4 AA5 4 HIS B 189 GLN B 196 -1 N HIS B 189 O SER B 205
SHEET 1 AA6 3 THR B 176 TRP B 179 0
SHEET 2 AA6 3 THR B 219 HIS B 224 -1 O SER B 221 N THR B 178
SHEET 3 AA6 3 THR B 229 LYS B 234 -1 O LYS B 233 N CYS B 220
SHEET 1 AA7 5 PHE C 30 SER C 34 0
SHEET 2 AA7 5 THR C 122 LYS C 127 1 O LYS C 127 N THR C 33
SHEET 3 AA7 5 VAL C 105 GLN C 110 -1 N TYR C 106 O THR C 122
SHEET 4 AA7 5 ALA C 54 GLN C 58 -1 N GLN C 58 O VAL C 105
SHEET 5 AA7 5 PRO C 64 TYR C 69 -1 O LYS C 65 N GLN C 57
SHEET 1 AA8 4 PHE C 30 SER C 34 0
SHEET 2 AA8 4 THR C 122 LYS C 127 1 O LYS C 127 N THR C 33
SHEET 3 AA8 4 VAL C 105 GLN C 110 -1 N TYR C 106 O THR C 122
SHEET 4 AA8 4 THR C 117 PHE C 118 -1 O THR C 117 N GLN C 110
SHEET 1 AA9 3 VAL C 39 LYS C 44 0
SHEET 2 AA9 3 ASP C 90 ILE C 95 -1 O ILE C 95 N VAL C 39
SHEET 3 AA9 3 PHE C 82 SER C 85 -1 N THR C 83 O THR C 94
SHEET 1 AB1 4 THR C 134 PHE C 138 0
SHEET 2 AB1 4 GLY C 149 PHE C 159 -1 O ASN C 157 N THR C 134
SHEET 3 AB1 4 TYR C 193 THR C 202 -1 O SER C 197 N CYS C 154
SHEET 4 AB1 4 VAL C 179 TRP C 183 -1 N LEU C 180 O THR C 198
SHEET 1 AB2 3 ASN C 165 LYS C 169 0
SHEET 2 AB2 3 TYR C 212 THR C 217 -1 O GLU C 215 N LYS C 167
SHEET 3 AB2 3 ILE C 225 PHE C 229 -1 O LYS C 227 N CYS C 214
SSBOND 1 CYS A 200 CYS A 209 1555 1555 2.03
SSBOND 2 CYS B 41 CYS B 115 1555 1555 2.03
SSBOND 3 CYS B 153 CYS C 234 1555 1555 2.03
SSBOND 4 CYS B 165 CYS B 220 1555 1555 2.03
SSBOND 5 CYS C 43 CYS C 108 1555 1555 2.03
SSBOND 6 CYS C 154 CYS C 214 1555 1555 2.03
LINK ND2 ASN A 208 C1 NAG A 701 1555 1555 1.44
LINK ND2 ASN A 217 C1 NAG A 705 1555 1555 1.44
CISPEP 1 GLY A 249 GLY A 250 0 -1.21
CISPEP 2 ARG B 121 PRO B 122 0 -7.71
CISPEP 3 PHE B 171 PRO B 172 0 -6.77
CISPEP 4 SER B 183 LEU B 184 0 -0.39
CISPEP 5 TRP B 213 PRO B 214 0 -9.65
CISPEP 6 ILE C 114 PRO C 115 0 -6.13
CISPEP 7 TYR C 160 PRO C 161 0 1.13
CRYST1 129.590 164.000 140.170 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 0.007717 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006098 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007134 0.00000
(ATOM LINES ARE NOT SHOWN.)
END