HEADER TRANSPORT PROTEIN/INHIBITOR 16-JAN-15 4XPF TITLE X-RAY STRUCTURE OF DROSOPHILA DOPAMINE TRANSPORTER WITH SUBSITEB TITLE 2 MUTATIONS (D121G/S426M) BOUND TO RTI-55 COMPND MOL_ID: 1; COMPND 2 MOLECULE: DOPAMINE TRANSPORTER-PROTEIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: ANTIBODY FRAGMENT HEAVY CHAIN-PROTEIN, 9D5-HEAVY CHAIN; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: ANTIBODY FRAGMENT HEAVY CHAIN-PROTEIN, 9D5-LIGHT CHAIN; COMPND 11 CHAIN: H; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER; SOURCE 3 ORGANISM_TAXID: 7227; SOURCE 4 GENE: DDAT; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: GNTI-, HEK293S; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PEG BACMAM; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 11 ORGANISM_COMMON: MOUSE; SOURCE 12 ORGANISM_TAXID: 10090; SOURCE 13 EXPRESSION_SYSTEM: MUS MUSCULUS; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 10090; SOURCE 15 EXPRESSION_SYSTEM_CELL_LINE: HYBRIDOMA; SOURCE 16 OTHER_DETAILS: HYBRIDOMA CELLS; SOURCE 17 MOL_ID: 3; SOURCE 18 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 19 ORGANISM_COMMON: MOUSE; SOURCE 20 ORGANISM_TAXID: 10090; SOURCE 21 EXPRESSION_SYSTEM: MUS MUSCULUS; SOURCE 22 EXPRESSION_SYSTEM_TAXID: 10090; SOURCE 23 EXPRESSION_SYSTEM_CELL_LINE: HYBRIDOMA; SOURCE 24 OTHER_DETAILS: HYBRIDOMA CELLS KEYWDS ALL ALPHA-HELICAL INTEGRAL MEMBRANE PROTEIN, TRANSPORT PROTEIN- KEYWDS 2 INHIBITOR COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR A.PENMATSA,K.H.WANG,E.GOUAUX REVDAT 1 06-MAY-15 4XPF 0 JRNL AUTH A.PENMATSA,K.H.WANG,E.GOUAUX JRNL TITL STRUCTURAL BASIS FOR NEUROTRANSMITTER AND PSYCHO STIMULANT JRNL TITL 2 RECOGNITION BY THE DROSOPHILA DOPAMINE TRANSPORTER JRNL REF NATURE 2015 JRNL REFN ESSN 1476-4687 REMARK 2 REMARK 2 RESOLUTION. 3.27 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 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) : 3.27 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.32 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 89.1 REMARK 3 NUMBER OF REFLECTIONS : 32039 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.244 REMARK 3 R VALUE (WORKING SET) : 0.241 REMARK 3 FREE R VALUE : 0.296 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010 REMARK 3 FREE R VALUE TEST SET COUNT : 1605 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 48.3289 - 7.2722 0.81 2652 156 0.2148 0.2705 REMARK 3 2 7.2722 - 5.7752 0.86 2742 129 0.2334 0.2693 REMARK 3 3 5.7752 - 5.0461 0.88 2754 143 0.1996 0.2454 REMARK 3 4 5.0461 - 4.5851 0.89 2800 131 0.1809 0.2541 REMARK 3 5 4.5851 - 4.2567 0.91 2788 152 0.1885 0.2499 REMARK 3 6 4.2567 - 4.0058 0.91 2810 144 0.2339 0.3309 REMARK 3 7 4.0058 - 3.8053 0.91 2795 147 0.3079 0.3545 REMARK 3 8 3.8053 - 3.6397 0.91 2774 141 0.3578 0.3872 REMARK 3 9 3.6397 - 3.4997 0.92 2819 151 0.3526 0.4009 REMARK 3 10 3.4997 - 3.3789 0.92 2772 175 0.3929 0.4363 REMARK 3 11 3.3789 - 3.2733 0.89 2728 136 0.4077 0.4422 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) : 0.600 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 36.190 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 114.2 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 110.3 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 : 0.005 7735 REMARK 3 ANGLE : 0.920 10559 REMARK 3 CHIRALITY : 0.037 1188 REMARK 3 PLANARITY : 0.004 1301 REMARK 3 DIHEDRAL : 13.907 2686 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: RESIDUE H CYS 134 AND RESIDUE H GLY 139 REMARK 3 ARE NOT PROPERLY LINKED: DISTANCE BETWEEN C AND N IS 10.88. REMARK 4 REMARK 4 4XPF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JAN-15. REMARK 100 THE DEPOSITION ID IS D_1000206071. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 24-NOV-13 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.8 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ALS REMARK 200 BEAMLINE : 5.0.2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.24 REMARK 200 MONOCHROMATOR : SI111 REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32190 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.270 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 (%) : 89.4 REMARK 200 DATA REDUNDANCY : 3.900 REMARK 200 R MERGE (I) : 0.12000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.27 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.39 REMARK 200 COMPLETENESS FOR SHELL (%) : 91.3 REMARK 200 DATA REDUNDANCY IN SHELL : 3.40 REMARK 200 R MERGE FOR SHELL (I) : 0.83800 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 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: 4M48 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 77.11 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.37 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 400 39%, BICINE 0.1M, PH 8.8, REMARK 280 VAPOR DIFFUSION, HANGING DROP REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 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 48.70750 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 83.48100 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 70.15600 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 83.48100 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 48.70750 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 70.15600 REMARK 290 SMTRY3 4 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 APPLY THE FOLLOWING TO CHAINS: A, L, H 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 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 162 OG REMARK 470 GLN A 163 CG CD OE1 NE2 REMARK 470 LYS A 236 CG CD CE NZ REMARK 470 LYS A 263 CG CD CE NZ REMARK 470 TYR A 305 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS A 306 CG CD CE NZ REMARK 470 GLU A 308 CG CD OE1 OE2 REMARK 470 VAL A 311 CG1 CG2 REMARK 470 LYS A 343 CG CD CE NZ REMARK 470 ARG A 442 CG CD NE CZ NH1 NH2 REMARK 470 VAL A 457 CG1 CG2 REMARK 470 ARG A 476 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 517 CG CD NE CZ NH1 NH2 REMARK 470 LEU A 580 CG CD1 CD2 REMARK 470 LEU A 586 CG CD1 CD2 REMARK 470 ARG A 587 CG CD NE CZ NH1 NH2 REMARK 470 SER L 128 OG REMARK 470 GLU L 155 CG CD OE1 OE2 REMARK 470 LYS L 170 CG CD CE NZ REMARK 470 LYS L 184 CG CD CE NZ REMARK 470 ARG L 189 CG CD NE CZ NH1 NH2 REMARK 470 GLU H 1 CG CD OE1 OE2 REMARK 470 GLN H 3 CG CD OE1 NE2 REMARK 470 THR H 28 OG1 CG2 REMARK 470 SER H 30 OG REMARK 470 ARG H 76 CG CD NE CZ NH1 NH2 REMARK 470 GLN H 111 CG CD OE1 NE2 REMARK 470 VAL H 189 CG1 CG2 REMARK 470 SER H 198 OG REMARK 470 ARG H 219 CG CD NE CZ NH1 NH2 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 SER H 192 OG SER H 196 1.71 REMARK 500 CD1 LEU H 130 N CYS H 146 1.76 REMARK 500 CE2 TYR A 124 O 42F A 603 1.95 REMARK 500 CD1 TRP H 194 CD1 ILE H 199 2.05 REMARK 500 CD2 TYR A 124 C15 42F A 603 2.11 REMARK 500 O SER L 31 OG1 THR L 52 2.14 REMARK 500 O THR H 69 N GLU H 82 2.16 REMARK 500 NZ LYS H 211 O HOH H 301 2.17 REMARK 500 O LEU A 254 NH1 ARG A 444 2.19 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 PRO A 596 C - N - CA ANGL. DEV. = 9.8 DEGREES REMARK 500 PRO L 96 C - N - CD ANGL. DEV. = 17.5 DEGREES REMARK 500 PRO L 142 C - N - CD ANGL. DEV. = 17.6 DEGREES REMARK 500 TYR L 187 CB - CA - C ANGL. DEV. = -12.6 DEGREES REMARK 500 PRO H 132 C - N - CD ANGL. DEV. = -27.8 DEGREES REMARK 500 PRO H 155 C - N - CD ANGL. DEV. = -31.5 DEGREES REMARK 500 PRO H 173 C - N - CD ANGL. DEV. = -13.1 DEGREES REMARK 500 SER H 198 N - CA - CB ANGL. DEV. = -10.9 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 ARG A 92 -0.57 69.94 REMARK 500 LEU A 102 -66.31 -104.01 REMARK 500 TYR A 123 -50.88 -129.76 REMARK 500 THR A 140 165.03 172.37 REMARK 500 ASN A 217 -62.44 -96.19 REMARK 500 THR A 260 -62.11 -99.16 REMARK 500 HIS A 372 -72.43 -102.60 REMARK 500 VAL A 391 -66.01 -131.81 REMARK 500 ARG A 444 -70.81 -74.61 REMARK 500 GLU A 445 70.31 34.76 REMARK 500 LEU A 446 -10.07 84.44 REMARK 500 TYR A 477 -59.37 -122.50 REMARK 500 ALA A 548 -134.63 57.44 REMARK 500 TRP L 48 -60.39 -103.53 REMARK 500 SER L 51 -131.15 62.01 REMARK 500 THR L 52 -51.59 -122.48 REMARK 500 ALA L 85 -175.05 -171.09 REMARK 500 LYS L 170 -70.93 -90.63 REMARK 500 ASN L 191 -64.47 -130.30 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 ARG A 444 GLU A 445 124.75 REMARK 500 ARG H 98 GLY H 99 147.76 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 NA A 607 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLY A 42 O REMARK 620 2 VAL A 45 O 83.9 REMARK 620 3 LEU A 417 O 165.6 87.0 REMARK 620 4 ASP A 420 OD1 105.2 140.0 75.0 REMARK 620 5 SER A 421 OG 90.1 79.1 99.2 138.3 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA A 606 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ALA A 44 O REMARK 620 2 ASN A 49 OD1 77.2 REMARK 620 3 SER A 320 O 78.0 153.4 REMARK 620 4 SER A 320 OG 127.2 125.1 65.2 REMARK 620 N 1 2 3 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue DMU A 601 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue 42F A 603 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 604 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 605 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 606 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 607 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 608 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4XNU RELATED DB: PDB REMARK 900 RELATED ID: 4XNX RELATED DB: PDB REMARK 900 RELATED ID: 4XP1 RELATED DB: PDB REMARK 900 RELATED ID: 4XP4 RELATED DB: PDB REMARK 900 RELATED ID: 4XP5 RELATED DB: PDB REMARK 900 RELATED ID: 4XP6 RELATED DB: PDB REMARK 900 RELATED ID: 4XP9 RELATED DB: PDB REMARK 900 RELATED ID: 4XPA RELATED DB: PDB REMARK 900 RELATED ID: 4XPB RELATED DB: PDB REMARK 900 RELATED ID: 4XPG RELATED DB: PDB REMARK 900 RELATED ID: 4XPH RELATED DB: PDB REMARK 900 RELATED ID: 4XPT RELATED DB: PDB DBREF 4XPF A 25 599 PDB 4XPF 4XPF 25 599 DBREF 4XPF L 1 214 PDB 4XPF 4XPF 1 214 DBREF 4XPF H 1 219 PDB 4XPF 4XPF 1 219 SEQRES 1 A 532 ASP GLU ARG GLU THR TRP SER GLY LYS VAL ASP PHE LEU SEQRES 2 A 532 LEU SER VAL ILE GLY PHE ALA VAL ASP LEU ALA ASN VAL SEQRES 3 A 532 TRP ARG PHE PRO TYR LEU CYS TYR LYS ASN GLY GLY GLY SEQRES 4 A 532 ALA PHE LEU VAL PRO TYR GLY ILE MET LEU ALA VAL GLY SEQRES 5 A 532 GLY ILE PRO LEU PHE TYR MET GLU LEU ALA LEU GLY GLN SEQRES 6 A 532 HIS ASN ARG LYS GLY ALA ILE THR CYS TRP GLY ARG LEU SEQRES 7 A 532 VAL PRO LEU PHE LYS GLY ILE GLY TYR ALA VAL VAL LEU SEQRES 8 A 532 ILE ALA PHE TYR VAL GLY PHE TYR TYR ASN VAL ILE ILE SEQRES 9 A 532 ALA TRP SER LEU ARG PHE PHE PHE ALA SER PHE THR ASN SEQRES 10 A 532 SER LEU PRO TRP THR SER CYS ASN ASN ILE TRP ASN THR SEQRES 11 A 532 PRO ASN CYS ARG PRO PHE GLU SER GLN GLY PHE GLN SER SEQRES 12 A 532 ALA ALA SER GLU TYR PHE ASN ARG TYR ILE LEU GLU LEU SEQRES 13 A 532 ASN ARG SER GLU GLY ILE HIS ASP LEU GLY ALA ILE LYS SEQRES 14 A 532 TRP ASP MET ALA LEU CYS LEU LEU ILE VAL TYR LEU ILE SEQRES 15 A 532 CYS TYR PHE SER LEU TRP LYS GLY ILE SER THR SER GLY SEQRES 16 A 532 LYS VAL VAL TRP PHE THR ALA LEU PHE PRO TYR ALA VAL SEQRES 17 A 532 LEU LEU ILE LEU LEU ILE ARG GLY LEU THR LEU PRO GLY SEQRES 18 A 532 SER PHE LEU GLY ILE GLN TYR TYR LEU THR PRO ASN PHE SEQRES 19 A 532 SER ALA ILE TYR LYS ALA GLU VAL TRP VAL ASP ALA ALA SEQRES 20 A 532 THR GLN VAL PHE PHE SER LEU GLY PRO GLY PHE GLY VAL SEQRES 21 A 532 LEU LEU ALA TYR ALA SER TYR ASN LYS TYR HIS ASN ASN SEQRES 22 A 532 VAL TYR LYS ASP ALA LEU LEU THR SER PHE ILE ASN SER SEQRES 23 A 532 ALA THR SER PHE ILE ALA GLY PHE VAL ILE PHE SER VAL SEQRES 24 A 532 LEU GLY TYR MET ALA HIS THR LEU GLY VAL ARG ILE GLU SEQRES 25 A 532 ASP VAL ALA THR GLU GLY PRO GLY LEU VAL PHE VAL VAL SEQRES 26 A 532 TYR PRO ALA ALA ILE ALA THR MET PRO ALA SER THR PHE SEQRES 27 A 532 TRP ALA LEU ILE PHE PHE MET MET LEU ALA THR LEU GLY SEQRES 28 A 532 LEU ASP SER SER PHE GLY GLY MET GLU ALA ILE ILE THR SEQRES 29 A 532 ALA LEU SER ASP GLU PHE PRO LYS ILE LYS ARG ASN ARG SEQRES 30 A 532 GLU LEU PHE VAL ALA GLY LEU PHE SER LEU TYR PHE VAL SEQRES 31 A 532 VAL GLY LEU ALA SER CYS THR GLN GLY GLY PHE TYR PHE SEQRES 32 A 532 PHE HIS LEU LEU ASP ARG TYR ALA ALA GLY TYR SER ILE SEQRES 33 A 532 LEU VAL ALA VAL PHE PHE GLU ALA ILE ALA VAL SER TRP SEQRES 34 A 532 ILE TYR GLY THR ASN ARG PHE SER GLU ASP ILE ARG ASP SEQRES 35 A 532 MET ILE GLY PHE PRO PRO GLY ARG TYR TRP GLN VAL CYS SEQRES 36 A 532 TRP ARG PHE VAL ALA PRO ILE PHE LEU LEU PHE ILE THR SEQRES 37 A 532 VAL TYR GLY LEU ILE GLY TYR GLU PRO LEU THR TYR ALA SEQRES 38 A 532 ASP TYR VAL TYR PRO SER TRP ALA ASN ALA LEU GLY TRP SEQRES 39 A 532 CYS ILE ALA GLY SER SER VAL VAL MET ILE PRO ALA VAL SEQRES 40 A 532 ALA ILE PHE LYS LEU LEU SER THR PRO GLY SER LEU ARG SEQRES 41 A 532 GLN ARG PHE THR ILE LEU THR THR PRO TRP ARG ASP SEQRES 1 L 214 GLU ASN VAL LEU THR GLN SER PRO ALA ILE MET SER THR SEQRES 2 L 214 SER PRO GLY GLU LYS VAL THR MET THR CYS ARG ALA SER SEQRES 3 L 214 SER SER VAL GLY SER SER TYR LEU HIS TRP TYR GLN GLN SEQRES 4 L 214 LYS SER GLY ALA SER PRO LYS LEU TRP ILE TYR SER THR SEQRES 5 L 214 SER ASN LEU ALA SER GLY VAL PRO ALA ARG PHE SER GLY SEQRES 6 L 214 SER GLY SER GLY THR SER TYR SER LEU THR ILE SER SER SEQRES 7 L 214 VAL GLU ALA GLU ASP ALA ALA THR TYR TYR CYS GLN GLN SEQRES 8 L 214 PHE SER GLY TYR PRO LEU THR PHE GLY SER GLY THR LYS SEQRES 9 L 214 LEU GLU MET LYS ARG ALA ASP ALA ALA PRO THR VAL SER SEQRES 10 L 214 ILE PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY SEQRES 11 L 214 ALA SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS SEQRES 12 L 214 ASP ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG SEQRES 13 L 214 GLN ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER SEQRES 14 L 214 LYS ASP SER THR TYR SER MET SER SER THR LEU THR LEU SEQRES 15 L 214 THR LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS SEQRES 16 L 214 GLU ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SEQRES 17 L 214 SER PHE ASN ARG ASN GLU SEQRES 1 H 215 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL LYS SEQRES 2 H 215 PRO GLY GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 H 215 PHE THR PHE SER SER TYR ALA MET SER TRP VAL ARG GLN SEQRES 4 H 215 SER PRO GLU LYS ARG LEU GLU TRP VAL ALA GLU ILE SER SEQRES 5 H 215 SER GLY GLY ARG TYR ILE TYR TYR SER ASP THR VAL THR SEQRES 6 H 215 GLY ARG PHE THR ILE SER ARG ASP ASN ALA ARG ASN ILE SEQRES 7 H 215 LEU HIS LEU GLU MET SER SER LEU ARG SER GLU ASP THR SEQRES 8 H 215 ALA MET TYR TYR CYS ALA ARG GLY GLU VAL ARG GLN ARG SEQRES 9 H 215 GLY PHE ASP TYR TRP GLY GLN GLY THR THR LEU THR VAL SEQRES 10 H 215 SER SER ALA LYS THR THR ALA PRO SER VAL TYR PRO LEU SEQRES 11 H 215 ALA PRO VAL CYS GLY SER SER VAL THR LEU GLY CYS LEU SEQRES 12 H 215 VAL LYS GLY TYR PHE PRO GLU PRO VAL THR LEU THR TRP SEQRES 13 H 215 ASN SER GLY SER LEU SER SER GLY VAL HIS THR PHE PRO SEQRES 14 H 215 ALA VAL LEU GLN SER ASP LEU TYR THR LEU SER SER SER SEQRES 15 H 215 VAL THR VAL THR SER SER THR TRP PRO SER GLN SER ILE SEQRES 16 H 215 THR CYS ASN VAL ALA HIS PRO ALA SER SER THR LYS VAL SEQRES 17 H 215 ASP LYS LYS ILE GLU PRO ARG HET DMU A 601 33 HET P4G A 602 29 HET 42F A 603 20 HET CLR A 604 28 HET CLR A 605 28 HET NA A 606 1 HET NA A 607 1 HET CL A 608 1 HETNAM DMU DECYL-BETA-D-MALTOPYRANOSIDE HETNAM P4G 1-ETHOXY-2-(2-ETHOXYETHOXY)ETHANE HETNAM 42F METHYL (1R,2S,3S,5S)-3-(4-IODOPHENYL)-8-METHYL-8- HETNAM 2 42F AZABICYCLO[3.2.1]OCTANE-2-CARBOXYLATE HETNAM CLR CHOLESTEROL HETNAM NA SODIUM ION HETNAM CL CHLORIDE ION HETSYN DMU DECYLMALTOSIDE FORMUL 4 DMU C22 H42 O11 FORMUL 5 P4G C8 H18 O3 FORMUL 6 42F C16 H20 I N O2 FORMUL 7 CLR 2(C27 H46 O) FORMUL 9 NA 2(NA 1+) FORMUL 11 CL CL 1- FORMUL 12 HOH *6(H2 O) HELIX 1 AA1 GLY A 32 VAL A 45 1 14 HELIX 2 AA2 ASP A 46 ARG A 52 1 7 HELIX 3 AA3 ARG A 52 ASN A 60 1 9 HELIX 4 AA4 GLY A 61 ALA A 64 5 4 HELIX 5 AA5 PHE A 65 VAL A 75 1 11 HELIX 6 AA6 GLY A 76 ASN A 91 1 16 HELIX 7 AA7 GLY A 94 ARG A 101 1 8 HELIX 8 AA8 VAL A 103 PHE A 106 5 4 HELIX 9 AA9 LYS A 107 GLY A 121 1 15 HELIX 10 AB1 PHE A 122 TYR A 124 5 3 HELIX 11 AB2 ASN A 125 ALA A 137 1 13 HELIX 12 AB3 LEU A 143 SER A 147 5 5 HELIX 13 AB4 ALA A 212 TYR A 219 1 8 HELIX 14 AB5 GLU A 222 SER A 226 5 5 HELIX 15 AB6 LYS A 236 TRP A 255 1 20 HELIX 16 AB7 LYS A 256 ALA A 269 1 14 HELIX 17 AB8 LEU A 270 LEU A 286 1 17 HELIX 18 AB9 GLY A 288 THR A 298 1 11 HELIX 19 AC1 ASN A 300 TYR A 305 5 6 HELIX 20 AC2 LYS A 306 GLY A 322 1 17 HELIX 21 AC3 GLY A 326 TYR A 334 1 9 HELIX 22 AC4 ASN A 340 THR A 373 1 34 HELIX 23 AC5 ARG A 377 ALA A 382 1 6 HELIX 24 AC6 GLY A 385 VAL A 391 1 7 HELIX 25 AC7 VAL A 391 ALA A 398 1 8 HELIX 26 AC8 ALA A 402 ASP A 435 1 34 HELIX 27 AC9 PRO A 438 ASN A 443 1 6 HELIX 28 AD1 LEU A 446 GLY A 459 1 14 HELIX 29 AD2 GLY A 466 ALA A 478 1 13 HELIX 30 AD3 TYR A 481 TRP A 496 1 16 HELIX 31 AD4 GLY A 499 GLY A 512 1 14 HELIX 32 AD5 GLY A 516 PHE A 525 1 10 HELIX 33 AD6 PHE A 525 GLY A 541 1 17 HELIX 34 AD7 PRO A 553 VAL A 569 1 17 HELIX 35 AD8 VAL A 569 THR A 582 1 14 HELIX 36 AD9 PHE A 590 THR A 595 1 6 HELIX 37 AE1 GLU L 80 ALA L 84 5 5 HELIX 38 AE2 SER L 122 SER L 128 1 7 HELIX 39 AE3 THR H 28 TYR H 32 5 5 HELIX 40 AE4 ARG H 87 THR H 91 5 5 HELIX 41 AE5 VAL H 101 GLY H 105 5 5 HELIX 42 AE6 SER H 192 GLN H 197 1 6 SHEET 1 AA1 2 CYS A 157 ARG A 158 0 SHEET 2 AA1 2 GLN A 209 SER A 210 1 O GLN A 209 N ARG A 158 SHEET 1 AA2 2 THR A 546 TYR A 547 0 SHEET 2 AA2 2 TYR A 550 VAL A 551 -1 O TYR A 550 N TYR A 547 SHEET 1 AA3 3 LEU L 4 SER L 7 0 SHEET 2 AA3 3 VAL L 19 VAL L 29 -1 O ARG L 24 N THR L 5 SHEET 3 AA3 3 PHE L 63 ILE L 76 -1 O LEU L 74 N MET L 21 SHEET 1 AA4 5 ILE L 10 THR L 13 0 SHEET 2 AA4 5 THR L 103 MET L 107 1 O GLU L 106 N MET L 11 SHEET 3 AA4 5 THR L 86 GLN L 91 -1 N TYR L 87 O THR L 103 SHEET 4 AA4 5 LEU L 34 GLN L 39 -1 N TYR L 37 O TYR L 88 SHEET 5 AA4 5 LYS L 46 ILE L 49 -1 O TRP L 48 N TRP L 36 SHEET 1 AA5 4 ILE L 10 THR L 13 0 SHEET 2 AA5 4 THR L 103 MET L 107 1 O GLU L 106 N MET L 11 SHEET 3 AA5 4 THR L 86 GLN L 91 -1 N TYR L 87 O THR L 103 SHEET 4 AA5 4 THR L 98 PHE L 99 -1 O THR L 98 N GLN L 91 SHEET 1 AA6 4 THR L 115 PHE L 119 0 SHEET 2 AA6 4 GLY L 130 PHE L 140 -1 O PHE L 136 N SER L 117 SHEET 3 AA6 4 TYR L 174 THR L 183 -1 O MET L 176 N LEU L 137 SHEET 4 AA6 4 VAL L 160 TRP L 164 -1 N LEU L 161 O THR L 179 SHEET 1 AA7 3 ASN L 146 ILE L 151 0 SHEET 2 AA7 3 SER L 192 THR L 198 -1 O THR L 198 N ASN L 146 SHEET 3 AA7 3 ILE L 206 ASN L 211 -1 O PHE L 210 N TYR L 193 SHEET 1 AA8 4 GLN H 3 SER H 7 0 SHEET 2 AA8 4 SER H 21 SER H 25 -1 O ALA H 23 N VAL H 5 SHEET 3 AA8 4 ILE H 78 MET H 83 -1 O LEU H 79 N CYS H 22 SHEET 4 AA8 4 PHE H 68 ASP H 73 -1 N ASP H 73 O ILE H 78 SHEET 1 AA9 6 LEU H 11 VAL H 12 0 SHEET 2 AA9 6 THR H 113 VAL H 117 1 O THR H 116 N VAL H 12 SHEET 3 AA9 6 ALA H 92 ARG H 98 -1 N TYR H 94 O THR H 113 SHEET 4 AA9 6 MET H 34 GLN H 39 -1 N VAL H 37 O TYR H 95 SHEET 5 AA9 6 LEU H 45 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AA9 6 ILE H 58 TYR H 60 -1 O TYR H 59 N GLU H 50 SHEET 1 AB1 4 LEU H 11 VAL H 12 0 SHEET 2 AB1 4 THR H 113 VAL H 117 1 O THR H 116 N VAL H 12 SHEET 3 AB1 4 ALA H 92 ARG H 98 -1 N TYR H 94 O THR H 113 SHEET 4 AB1 4 TYR H 108 TRP H 109 -1 O TYR H 108 N ARG H 98 SHEET 1 AB2 4 SER H 126 LEU H 130 0 SHEET 2 AB2 4 SER H 141 TYR H 151 -1 O GLY H 145 N LEU H 130 SHEET 3 AB2 4 TYR H 181 THR H 190 -1 O TYR H 181 N TYR H 151 SHEET 4 AB2 4 VAL H 169 THR H 171 -1 N HIS H 170 O SER H 186 SHEET 1 AB3 4 SER H 126 LEU H 130 0 SHEET 2 AB3 4 SER H 141 TYR H 151 -1 O GLY H 145 N LEU H 130 SHEET 3 AB3 4 TYR H 181 THR H 190 -1 O TYR H 181 N TYR H 151 SHEET 4 AB3 4 VAL H 175 LEU H 176 -1 N VAL H 175 O THR H 182 SHEET 1 AB4 3 THR H 157 TRP H 160 0 SHEET 2 AB4 3 THR H 200 HIS H 205 -1 O ASN H 202 N THR H 159 SHEET 3 AB4 3 THR H 210 LYS H 215 -1 O THR H 210 N HIS H 205 SSBOND 1 CYS A 148 CYS A 157 1555 1555 2.04 SSBOND 2 CYS L 23 CYS L 89 1555 1555 2.04 SSBOND 3 CYS L 135 CYS L 195 1555 1555 2.03 SSBOND 4 CYS H 22 CYS H 96 1555 1555 2.04 SSBOND 5 CYS H 146 CYS H 201 1555 1555 2.03 LINK O GLY A 42 NA NA A 607 1555 1555 2.27 LINK O ALA A 44 NA NA A 606 1555 1555 2.76 LINK O VAL A 45 NA NA A 607 1555 1555 2.04 LINK OD1 ASN A 49 NA NA A 606 1555 1555 3.09 LINK O SER A 320 NA NA A 606 1555 1555 3.01 LINK OG SER A 320 NA NA A 606 1555 1555 2.45 LINK O LEU A 417 NA NA A 607 1555 1555 2.35 LINK OD1 ASP A 420 NA NA A 607 1555 1555 2.27 LINK OG SER A 421 NA NA A 607 1555 1555 2.07 LINK CD1 LEU H 130 C GLY H 145 1555 1555 1.10 LINK CD1 LEU H 130 O GLY H 145 1555 1555 1.22 CISPEP 1 SER L 7 PRO L 8 0 11.33 CISPEP 2 TYR L 95 PRO L 96 0 -8.39 CISPEP 3 TYR L 141 PRO L 142 0 -9.93 CISPEP 4 PRO H 132 VAL H 133 0 -11.34 CISPEP 5 PHE H 152 PRO H 153 0 -16.16 CISPEP 6 GLU H 154 PRO H 155 0 25.77 CISPEP 7 TRP H 194 PRO H 195 0 11.90 SITE 1 AC1 5 ARG A 133 PHE A 136 TYR A 219 ASP A 238 SITE 2 AC1 5 ARG L 156 SITE 1 AC2 9 PHE A 43 ASP A 46 VAL A 120 GLY A 121 SITE 2 AC2 9 TYR A 123 TYR A 124 ASN A 125 SER A 422 SITE 3 AC2 9 GLY A 425 SITE 1 AC3 2 PHE A 350 TRP A 519 SITE 1 AC4 3 TYR A 273 LEU A 277 ILE A 351 SITE 1 AC5 5 ALA A 44 ASP A 46 ASN A 49 SER A 320 SITE 2 AC5 5 ASN A 352 SITE 1 AC6 5 GLY A 42 VAL A 45 LEU A 417 ASP A 420 SITE 2 AC6 5 SER A 421 SITE 1 AC7 4 TYR A 69 GLN A 316 SER A 320 SER A 356 CRYST1 97.415 140.312 166.962 90.00 90.00 90.00 P 21 21 21 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 0.010265 0.000000 0.000000 0.00000 SCALE2 0.000000 0.007127 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005989 0.00000