HEADER TRANSPORT PROTEIN/INHIBITOR 16-JAN-15 4XP9 TITLE X-RAY STRUCTURE OF DROSOPHILA DOPAMINE TRANSPORTER BOUND TO TITLE 2 PSYCHOSTIMULANT D-AMPHETAMINE COMPND MOL_ID: 1; COMPND 2 MOLECULE: DOPAMINE TRANSPORTER; COMPND 3 CHAIN: C; COMPND 4 SYNONYM: DOPAMINE TRANSPORTER,ISOFORM A,GH22929P; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: ANTIBODY FRAGMENT HEAVY CHAIN-PROTEIN, 9D5-HEAVY CHAIN; COMPND 9 CHAIN: L; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: ANTIBODY FRAGMENT LIGHT CHAIN-PROTEIN, 9D5-LIGHT CHAIN; COMPND 13 CHAIN: H; COMPND 14 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER; SOURCE 3 ORGANISM_COMMON: FRUIT FLY; SOURCE 4 ORGANISM_TAXID: 7227; SOURCE 5 GENE: DAT, CG8380, DMEL_CG8380; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: GNTI-HEK293S; 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 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 17 ORGANISM_COMMON: MOUSE; SOURCE 18 ORGANISM_TAXID: 10090; SOURCE 19 EXPRESSION_SYSTEM: MUS MUSCULUS; SOURCE 20 EXPRESSION_SYSTEM_TAXID: 10090 KEYWDS INTEGRAL MEMBRANE PROTEIN, ALL-ALPHA HELICAL ANTIDEPRESSANT COMPLEX, KEYWDS 2 MEMBRANE PROTEIN, PROTEIN TRANSPORT, TRANSPORT PROTEIN-INHIBITOR KEYWDS 3 COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR P.ARAVIND,K.WANG,E.GOUAUX REVDAT 2 27-MAY-15 4XP9 1 JRNL REVDAT 1 06-MAY-15 4XP9 0 JRNL AUTH K.H.WANG,A.PENMATSA,E.GOUAUX JRNL TITL NEUROTRANSMITTER AND PSYCHOSTIMULANT RECOGNITION BY THE JRNL TITL 2 DOPAMINE TRANSPORTER. JRNL REF NATURE 2015 JRNL REFN ESSN 1476-4687 JRNL PMID 25970245 JRNL DOI 10.1038/NATURE14431 REMARK 2 REMARK 2 RESOLUTION. 2.80 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) : 2.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.72 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.040 REMARK 3 COMPLETENESS FOR RANGE (%) : 96.8 REMARK 3 NUMBER OF REFLECTIONS : 55464 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.212 REMARK 3 R VALUE (WORKING SET) : 0.211 REMARK 3 FREE R VALUE : 0.242 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.880 REMARK 3 FREE R VALUE TEST SET COUNT : 5175 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 46.7309 - 8.6673 0.96 3318 201 0.2022 0.2115 REMARK 3 2 8.6673 - 6.8866 0.99 3464 164 0.1601 0.1879 REMARK 3 3 6.8866 - 6.0181 1.00 3430 207 0.2027 0.2223 REMARK 3 4 6.0181 - 5.4688 1.00 3474 176 0.2015 0.2426 REMARK 3 5 5.4688 - 5.0773 1.00 3440 189 0.1906 0.2316 REMARK 3 6 5.0773 - 4.7783 1.00 3488 180 0.1792 0.2177 REMARK 3 7 4.7783 - 4.5392 1.00 3470 163 0.1711 0.2279 REMARK 3 8 4.5392 - 4.3418 1.00 3460 192 0.1731 0.2013 REMARK 3 9 4.3418 - 4.1747 1.00 3460 163 0.1787 0.2034 REMARK 3 10 4.1747 - 4.0307 1.00 3493 154 0.1870 0.2391 REMARK 3 11 4.0307 - 3.9048 1.00 3461 162 0.2040 0.2601 REMARK 3 12 3.9048 - 3.7932 1.00 3416 223 0.2078 0.2423 REMARK 3 13 3.7932 - 3.6934 0.99 3465 178 0.2245 0.2581 REMARK 3 14 3.6934 - 3.6033 1.00 3464 182 0.2324 0.2730 REMARK 3 15 3.6033 - 3.5214 1.00 3454 167 0.2339 0.2643 REMARK 3 16 3.5214 - 3.4465 1.00 3482 189 0.2363 0.2566 REMARK 3 17 3.4465 - 3.3776 1.00 3492 173 0.2442 0.2454 REMARK 3 18 3.3776 - 3.3139 1.00 3438 171 0.2493 0.2925 REMARK 3 19 3.3139 - 3.2547 1.00 3483 183 0.2627 0.2969 REMARK 3 20 3.2547 - 3.1995 1.00 3492 157 0.2722 0.3281 REMARK 3 21 3.1995 - 3.1479 0.99 3408 179 0.2705 0.3089 REMARK 3 22 3.1479 - 3.0995 0.98 3436 202 0.2862 0.3171 REMARK 3 23 3.0995 - 3.0539 0.98 3390 147 0.2871 0.3014 REMARK 3 24 3.0539 - 3.0109 0.97 3449 148 0.3044 0.2713 REMARK 3 25 3.0109 - 2.9703 0.94 3243 166 0.3092 0.3293 REMARK 3 26 2.9703 - 2.9317 0.93 3244 160 0.3156 0.3211 REMARK 3 27 2.9317 - 2.8950 0.93 3179 187 0.3445 0.3734 REMARK 3 28 2.8950 - 2.8602 0.94 3262 152 0.3408 0.3791 REMARK 3 29 2.8602 - 2.8269 0.84 2938 146 0.3807 0.3508 REMARK 3 30 2.8269 - 2.7952 0.62 2112 114 0.4002 0.4374 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) : 0.370 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.970 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 85.19 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 7859 REMARK 3 ANGLE : 1.168 10723 REMARK 3 CHIRALITY : 0.044 1207 REMARK 3 PLANARITY : 0.006 1321 REMARK 3 DIHEDRAL : 13.208 2695 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 4XP9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JAN-15. REMARK 100 THE DEPOSITION ID IS D_1000206063. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 19-SEP-14 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ALS REMARK 200 BEAMLINE : 8.2.1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.00 REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55464 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.6 REMARK 200 DATA REDUNDANCY : 3.700 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 18.1000 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 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 (%): 76.94 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.33 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 600 (36%), MOPS (0.1M), PH 7.0, REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K 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 48.67400 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 83.38000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 70.37400 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 83.38000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 48.67400 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 70.37400 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: C, H, L 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 LEU C 562 REMARK 465 VAL C 563 REMARK 465 PRO C 564 REMARK 465 ARG C 565 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 C 33 CG CD CE NZ REMARK 470 LYS C 215 CG CD CE NZ REMARK 470 LYS C 222 CG CD CE NZ REMARK 470 TYR C 264 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS C 265 CG CD CE NZ REMARK 470 GLU C 267 CG CD OE1 OE2 REMARK 470 LYS C 398 CG CD CE NZ REMARK 470 ARG C 401 CG CD NE CZ NH1 NH2 REMARK 470 ARG C 546 CG CD NE CZ NH1 NH2 REMARK 470 GLN C 559 CG CD OE1 NE2 REMARK 470 SER L 128 OG REMARK 470 SER L 169 OG REMARK 470 LYS L 170 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 SER H 30 OG 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 OD2 ASP C 379 O HOH C 701 2.10 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 H 132 C - N - CA ANGL. DEV. = 10.2 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 ASP C 46 -156.09 -139.37 REMARK 500 ARG C 52 -45.91 -130.51 REMARK 500 VAL C 350 -66.37 -136.06 REMARK 500 ALA C 507 -126.35 41.84 REMARK 500 TRP L 48 -51.43 -141.92 REMARK 500 THR L 52 -64.66 73.07 REMARK 500 ALA L 85 -178.49 -173.41 REMARK 500 ALA L 131 105.02 -167.05 REMARK 500 GLU L 152 -131.24 60.92 REMARK 500 LYS L 170 -78.15 -85.82 REMARK 500 SER H 85 64.84 25.96 REMARK 500 THR H 138 -168.41 -164.98 REMARK 500 LYS H 211 72.14 -159.15 REMARK 500 PRO H 218 48.03 -84.04 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 C 610 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLY C 42 O REMARK 620 2 VAL C 45 O 79.1 REMARK 620 3 LEU C 376 O 165.0 86.1 REMARK 620 4 ASP C 379 OD2 86.9 107.6 95.2 REMARK 620 5 SER C 380 OG 87.3 95.8 96.8 154.4 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA C 609 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ALA C 44 O REMARK 620 2 ASN C 49 OD1 87.7 REMARK 620 3 SER C 279 O 74.0 160.1 REMARK 620 4 SER C 279 OG 147.7 120.4 79.4 REMARK 620 5 ASN C 311 OD1 83.3 88.3 97.0 82.1 REMARK 620 6 HOH C 705 O 96.7 87.0 87.6 100.1 175.3 REMARK 620 N 1 2 3 4 5 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 C 601 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue MAL C 603 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue MPO C 604 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CLR C 605 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue 1WE C 606 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue P4G C 607 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue NA C 609 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue NA C 610 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 611 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 602 bound REMARK 800 to ASN C 141 REMARK 900 REMARK 900 RELATED ENTRIES 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: 4XPA RELATED DB: PDB REMARK 900 RELATED ID: 4XPB RELATED DB: PDB REMARK 900 RELATED ID: 4XPF 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 4XP9 C 25 560 UNP Q7K4Y6 Q7K4Y6_DROME 25 601 DBREF 4XP9 L 1 213 PDB 4XP9 4XP9 1 213 DBREF 4XP9 H 1 219 PDB 4XP9 4XP9 1 219 SEQADV 4XP9 ALA C 74 UNP Q7K4Y6 VAL 74 ENGINEERED MUTATION SEQADV 4XP9 C UNP Q7K4Y6 SER 162 DELETION SEQADV 4XP9 C UNP Q7K4Y6 GLN 163 DELETION SEQADV 4XP9 C UNP Q7K4Y6 ASN 164 DELETION SEQADV 4XP9 C UNP Q7K4Y6 ALA 165 DELETION SEQADV 4XP9 C UNP Q7K4Y6 SER 166 DELETION SEQADV 4XP9 C UNP Q7K4Y6 ARG 167 DELETION SEQADV 4XP9 C UNP Q7K4Y6 VAL 168 DELETION SEQADV 4XP9 C UNP Q7K4Y6 PRO 169 DELETION SEQADV 4XP9 C UNP Q7K4Y6 VAL 170 DELETION SEQADV 4XP9 C UNP Q7K4Y6 ILE 171 DELETION SEQADV 4XP9 C UNP Q7K4Y6 GLY 172 DELETION SEQADV 4XP9 C UNP Q7K4Y6 ASN 173 DELETION SEQADV 4XP9 C UNP Q7K4Y6 TYR 174 DELETION SEQADV 4XP9 C UNP Q7K4Y6 SER 175 DELETION SEQADV 4XP9 C UNP Q7K4Y6 ASP 176 DELETION SEQADV 4XP9 C UNP Q7K4Y6 LEU 177 DELETION SEQADV 4XP9 C UNP Q7K4Y6 TYR 178 DELETION SEQADV 4XP9 C UNP Q7K4Y6 ALA 179 DELETION SEQADV 4XP9 C UNP Q7K4Y6 MET 180 DELETION SEQADV 4XP9 C UNP Q7K4Y6 GLY 181 DELETION SEQADV 4XP9 C UNP Q7K4Y6 ASN 182 DELETION SEQADV 4XP9 C UNP Q7K4Y6 GLN 183 DELETION SEQADV 4XP9 C UNP Q7K4Y6 SER 184 DELETION SEQADV 4XP9 C UNP Q7K4Y6 LEU 185 DELETION SEQADV 4XP9 C UNP Q7K4Y6 LEU 186 DELETION SEQADV 4XP9 C UNP Q7K4Y6 TYR 187 DELETION SEQADV 4XP9 C UNP Q7K4Y6 ASN 188 DELETION SEQADV 4XP9 C UNP Q7K4Y6 GLU 189 DELETION SEQADV 4XP9 C UNP Q7K4Y6 THR 190 DELETION SEQADV 4XP9 C UNP Q7K4Y6 TYR 191 DELETION SEQADV 4XP9 C UNP Q7K4Y6 MET 192 DELETION SEQADV 4XP9 C UNP Q7K4Y6 ASN 193 DELETION SEQADV 4XP9 C UNP Q7K4Y6 GLY 194 DELETION SEQADV 4XP9 C UNP Q7K4Y6 SER 195 DELETION SEQADV 4XP9 C UNP Q7K4Y6 SER 196 DELETION SEQADV 4XP9 C UNP Q7K4Y6 LEU 197 DELETION SEQADV 4XP9 C UNP Q7K4Y6 ASP 198 DELETION SEQADV 4XP9 C UNP Q7K4Y6 THR 199 DELETION SEQADV 4XP9 C UNP Q7K4Y6 SER 200 DELETION SEQADV 4XP9 C UNP Q7K4Y6 ALA 201 DELETION SEQADV 4XP9 C UNP Q7K4Y6 VAL 202 DELETION SEQADV 4XP9 ALA C 374 UNP Q7K4Y6 LEU 415 ENGINEERED MUTATION SEQADV 4XP9 LEU C 561 UNP Q7K4Y6 EXPRESSION TAG SEQADV 4XP9 LEU C 562 UNP Q7K4Y6 EXPRESSION TAG SEQADV 4XP9 VAL C 563 UNP Q7K4Y6 EXPRESSION TAG SEQADV 4XP9 PRO C 564 UNP Q7K4Y6 EXPRESSION TAG SEQADV 4XP9 ARG C 565 UNP Q7K4Y6 EXPRESSION TAG SEQRES 1 C 541 ASP GLU ARG GLU THR TRP SER GLY LYS VAL ASP PHE LEU SEQRES 2 C 541 LEU SER VAL ILE GLY PHE ALA VAL ASP LEU ALA ASN VAL SEQRES 3 C 541 TRP ARG PHE PRO TYR LEU CYS TYR LYS ASN GLY GLY GLY SEQRES 4 C 541 ALA PHE LEU VAL PRO TYR GLY ILE MET LEU ALA VAL GLY SEQRES 5 C 541 GLY ILE PRO LEU PHE TYR MET GLU LEU ALA LEU GLY GLN SEQRES 6 C 541 HIS ASN ARG LYS GLY ALA ILE THR CYS TRP GLY ARG LEU SEQRES 7 C 541 VAL PRO LEU PHE LYS GLY ILE GLY TYR ALA VAL VAL LEU SEQRES 8 C 541 ILE ALA PHE TYR VAL ASP PHE TYR TYR ASN VAL ILE ILE SEQRES 9 C 541 ALA TRP SER LEU ARG PHE PHE PHE ALA SER PHE THR ASN SEQRES 10 C 541 SER LEU PRO TRP THR SER CYS ASN ASN ILE TRP ASN THR SEQRES 11 C 541 PRO ASN CYS ARG PRO PHE GLU GLY HIS VAL GLU GLY PHE SEQRES 12 C 541 GLN SER ALA ALA SER GLU TYR PHE ASN ARG TYR ILE LEU SEQRES 13 C 541 GLU LEU ASN ARG SER GLU GLY ILE HIS ASP LEU GLY ALA SEQRES 14 C 541 ILE LYS TRP ASP MET ALA LEU CYS LEU LEU ILE VAL TYR SEQRES 15 C 541 LEU ILE CYS TYR PHE SER LEU TRP LYS GLY ILE SER THR SEQRES 16 C 541 SER GLY LYS VAL VAL TRP PHE THR ALA LEU PHE PRO TYR SEQRES 17 C 541 ALA VAL LEU LEU ILE LEU LEU ILE ARG GLY LEU THR LEU SEQRES 18 C 541 PRO GLY SER PHE LEU GLY ILE GLN TYR TYR LEU THR PRO SEQRES 19 C 541 ASN PHE SER ALA ILE TYR LYS ALA GLU VAL TRP VAL ASP SEQRES 20 C 541 ALA ALA THR GLN VAL PHE PHE SER LEU GLY PRO GLY PHE SEQRES 21 C 541 GLY VAL LEU LEU ALA TYR ALA SER TYR ASN LYS TYR HIS SEQRES 22 C 541 ASN ASN VAL TYR LYS ASP ALA LEU LEU THR SER PHE ILE SEQRES 23 C 541 ASN SER ALA THR SER PHE ILE ALA GLY PHE VAL ILE PHE SEQRES 24 C 541 SER VAL LEU GLY TYR MET ALA HIS THR LEU GLY VAL ARG SEQRES 25 C 541 ILE GLU ASP VAL ALA THR GLU GLY PRO GLY LEU VAL PHE SEQRES 26 C 541 VAL VAL TYR PRO ALA ALA ILE ALA THR MET PRO ALA SER SEQRES 27 C 541 THR PHE TRP ALA LEU ILE PHE PHE MET MET LEU ALA THR SEQRES 28 C 541 LEU GLY LEU ASP SER SER PHE GLY GLY SER GLU ALA ILE SEQRES 29 C 541 ILE THR ALA LEU SER ASP GLU PHE PRO LYS ILE LYS ARG SEQRES 30 C 541 ASN ARG GLU LEU PHE VAL ALA GLY LEU PHE SER LEU TYR SEQRES 31 C 541 PHE VAL VAL GLY LEU ALA SER CYS THR GLN GLY GLY PHE SEQRES 32 C 541 TYR PHE PHE HIS LEU LEU ASP ARG TYR ALA ALA GLY TYR SEQRES 33 C 541 SER ILE LEU VAL ALA VAL PHE PHE GLU ALA ILE ALA VAL SEQRES 34 C 541 SER TRP ILE TYR GLY THR ASN ARG PHE SER GLU ASP ILE SEQRES 35 C 541 ARG ASP MET ILE GLY PHE PRO PRO GLY ARG TYR TRP GLN SEQRES 36 C 541 VAL CYS TRP ARG PHE VAL ALA PRO ILE PHE LEU LEU PHE SEQRES 37 C 541 ILE THR VAL TYR GLY LEU ILE GLY TYR GLU PRO LEU THR SEQRES 38 C 541 TYR ALA ASP TYR VAL TYR PRO SER TRP ALA ASN ALA LEU SEQRES 39 C 541 GLY TRP CYS ILE ALA GLY SER SER VAL VAL MET ILE PRO SEQRES 40 C 541 ALA VAL ALA ILE PHE LYS LEU LEU SER THR PRO GLY SER SEQRES 41 C 541 LEU ARG GLN ARG PHE THR ILE LEU THR THR PRO TRP ARG SEQRES 42 C 541 ASP GLN GLN LEU LEU VAL PRO ARG SEQRES 1 L 213 GLU ASN VAL LEU THR GLN SER PRO ALA ILE MET SER THR SEQRES 2 L 213 SER PRO GLY GLU LYS VAL THR MET THR CYS ARG ALA SER SEQRES 3 L 213 SER SER VAL GLY SER SER TYR LEU HIS TRP TYR GLN GLN SEQRES 4 L 213 LYS SER GLY ALA SER PRO LYS LEU TRP ILE TYR SER THR SEQRES 5 L 213 SER ASN LEU ALA SER GLY VAL PRO ALA ARG PHE SER GLY SEQRES 6 L 213 SER GLY SER GLY THR SER TYR SER LEU THR ILE SER SER SEQRES 7 L 213 VAL GLU ALA GLU ASP ALA ALA THR TYR TYR CYS GLN GLN SEQRES 8 L 213 PHE SER GLY TYR PRO LEU THR PHE GLY SER GLY THR LYS SEQRES 9 L 213 LEU GLU MET LYS ARG ALA ASP ALA ALA PRO THR VAL SER SEQRES 10 L 213 ILE PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY SEQRES 11 L 213 ALA SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS SEQRES 12 L 213 ASP ILE ASN VAL LYS TRP LYS ILE GLU GLY SER GLU ARG SEQRES 13 L 213 GLN ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER SEQRES 14 L 213 LYS ASP SER THR TYR SER MET SER SER THR LEU THR LEU SEQRES 15 L 213 THR LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS SEQRES 16 L 213 GLU ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SEQRES 17 L 213 SER PHE ASN ARG ASN SEQRES 1 H 219 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL LYS SEQRES 2 H 219 PRO GLY GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 H 219 PHE THR PHE SER SER TYR ALA MET SER TRP VAL ARG GLN SEQRES 4 H 219 SER PRO GLU LYS ARG LEU GLU TRP VAL ALA GLU ILE SER SEQRES 5 H 219 SER GLY GLY ARG TYR ILE TYR TYR SER ASP THR VAL THR SEQRES 6 H 219 GLY ARG PHE THR ILE SER ARG ASP ASN ALA ARG ASN ILE SEQRES 7 H 219 LEU HIS LEU GLU MET SER SER LEU ARG SER GLU ASP THR SEQRES 8 H 219 ALA MET TYR TYR CYS ALA ARG GLY GLU VAL ARG GLN ARG SEQRES 9 H 219 GLY PHE ASP TYR TRP GLY GLN GLY THR THR LEU THR VAL SEQRES 10 H 219 SER SER ALA LYS THR THR ALA PRO SER VAL TYR PRO LEU SEQRES 11 H 219 ALA PRO VAL CYS GLY ASP THR THR GLY SER SER VAL THR SEQRES 12 H 219 LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL SEQRES 13 H 219 THR LEU THR TRP ASN SER GLY SER LEU SER SER GLY VAL SEQRES 14 H 219 HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR SEQRES 15 H 219 LEU SER SER SER VAL THR VAL THR SER SER THR TRP PRO SEQRES 16 H 219 SER GLN SER ILE THR CYS ASN VAL ALA HIS PRO ALA SER SEQRES 17 H 219 SER THR LYS VAL ASP LYS LYS ILE GLU PRO ARG HET Y01 C 601 35 HET NAG C 602 14 HET MAL C 603 23 HET MPO C 604 13 HET CLR C 605 28 HET 1WE C 606 10 HET P4G C 607 29 HET P4G C 608 29 HET NA C 609 1 HET NA C 610 1 HET CL C 611 1 HETNAM Y01 CHOLESTEROL HEMISUCCINATE HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM MAL MALTOSE HETNAM MPO 3[N-MORPHOLINO]PROPANE SULFONIC ACID HETNAM CLR CHOLESTEROL HETNAM 1WE (2S)-1-PHENYLPROPAN-2-AMINE HETNAM P4G 1-ETHOXY-2-(2-ETHOXYETHOXY)ETHANE HETNAM NA SODIUM ION HETNAM CL CHLORIDE ION HETSYN 1WE DEXTROAMPHETAMINE, D-AMPHETAMINE, DEXAMPHETAMINE, HETSYN 2 1WE DEXEDRINE, DEXTROSTAT FORMUL 4 Y01 C31 H50 O4 FORMUL 5 NAG C8 H15 N O6 FORMUL 6 MAL C12 H22 O11 FORMUL 7 MPO C7 H15 N O4 S FORMUL 8 CLR C27 H46 O FORMUL 9 1WE C9 H13 N FORMUL 10 P4G 2(C8 H18 O3) FORMUL 12 NA 2(NA 1+) FORMUL 14 CL CL 1- FORMUL 15 HOH *33(H2 O) HELIX 1 AA1 GLY C 32 VAL C 45 1 14 HELIX 2 AA2 ASP C 46 ARG C 52 1 7 HELIX 3 AA3 ARG C 52 ASN C 60 1 9 HELIX 4 AA4 GLY C 61 ALA C 64 5 4 HELIX 5 AA5 PHE C 65 GLY C 76 1 12 HELIX 6 AA6 GLY C 76 ARG C 92 1 17 HELIX 7 AA7 GLY C 94 VAL C 103 1 10 HELIX 8 AA8 PRO C 104 PHE C 106 5 3 HELIX 9 AA9 LYS C 107 ALA C 137 1 31 HELIX 10 AB1 LEU C 143 SER C 147 5 5 HELIX 11 AB2 SER C 169 TYR C 178 1 10 HELIX 12 AB3 GLU C 181 SER C 185 5 5 HELIX 13 AB4 LYS C 195 TRP C 214 1 20 HELIX 14 AB5 GLY C 216 THR C 244 1 29 HELIX 15 AB6 GLY C 247 THR C 257 1 11 HELIX 16 AB7 ASN C 259 TYR C 264 5 6 HELIX 17 AB8 LYS C 265 LEU C 280 1 16 HELIX 18 AB9 GLY C 285 SER C 292 1 8 HELIX 19 AC1 ASN C 299 LEU C 333 1 35 HELIX 20 AC2 ARG C 336 ALA C 341 1 6 HELIX 21 AC3 GLY C 344 VAL C 350 1 7 HELIX 22 AC4 VAL C 350 THR C 358 1 9 HELIX 23 AC5 ALA C 361 PHE C 396 1 36 HELIX 24 AC6 PHE C 396 ASN C 402 1 7 HELIX 25 AC7 ASN C 402 LEU C 419 1 18 HELIX 26 AC8 ALA C 420 THR C 423 5 4 HELIX 27 AC9 GLY C 425 ALA C 437 1 13 HELIX 28 AD1 ALA C 438 ILE C 456 1 19 HELIX 29 AD2 GLY C 458 GLY C 471 1 14 HELIX 30 AD3 GLY C 475 PHE C 484 1 10 HELIX 31 AD4 PHE C 484 GLY C 500 1 17 HELIX 32 AD5 PRO C 512 VAL C 528 1 17 HELIX 33 AD6 VAL C 528 LEU C 539 1 12 HELIX 34 AD7 SER C 544 THR C 553 1 10 HELIX 35 AD8 PRO C 555 GLN C 560 1 6 HELIX 36 AD9 GLY L 30 SER L 32 5 3 HELIX 37 AE1 GLU L 80 ALA L 84 5 5 HELIX 38 AE2 SER L 122 THR L 127 1 6 HELIX 39 AE3 LYS L 184 ARG L 189 1 6 HELIX 40 AE4 THR H 28 TYR H 32 5 5 HELIX 41 AE5 ARG H 87 THR H 91 5 5 HELIX 42 AE6 SER H 162 SER H 164 5 3 HELIX 43 AE7 PRO H 206 SER H 209 5 4 SHEET 1 AA1 2 THR C 505 TYR C 506 0 SHEET 2 AA1 2 TYR C 509 VAL C 510 -1 O TYR C 509 N TYR C 506 SHEET 1 AA2 4 LEU L 4 SER L 7 0 SHEET 2 AA2 4 VAL L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AA2 4 SER L 71 ILE L 76 -1 O TYR L 72 N CYS L 23 SHEET 4 AA2 4 PHE L 63 SER L 68 -1 N SER L 66 O SER L 73 SHEET 1 AA3 6 ILE L 10 THR L 13 0 SHEET 2 AA3 6 THR L 103 MET L 107 1 O GLU L 106 N MET L 11 SHEET 3 AA3 6 THR L 86 GLN L 91 -1 N TYR L 87 O THR L 103 SHEET 4 AA3 6 LEU L 34 GLN L 39 -1 N TYR L 37 O TYR L 88 SHEET 5 AA3 6 LYS L 46 TYR L 50 -1 O ILE L 49 N TRP L 36 SHEET 6 AA3 6 ASN L 54 LEU L 55 -1 O ASN L 54 N TYR L 50 SHEET 1 AA4 4 ILE L 10 THR L 13 0 SHEET 2 AA4 4 THR L 103 MET L 107 1 O GLU L 106 N MET L 11 SHEET 3 AA4 4 THR L 86 GLN L 91 -1 N TYR L 87 O THR L 103 SHEET 4 AA4 4 THR L 98 PHE L 99 -1 O THR L 98 N GLN L 91 SHEET 1 AA5 4 THR L 115 PHE L 119 0 SHEET 2 AA5 4 GLY L 130 PHE L 140 -1 O VAL L 134 N PHE L 119 SHEET 3 AA5 4 TYR L 174 THR L 183 -1 O LEU L 182 N ALA L 131 SHEET 4 AA5 4 VAL L 160 TRP L 164 -1 N LEU L 161 O THR L 179 SHEET 1 AA6 4 SER L 154 ARG L 156 0 SHEET 2 AA6 4 ILE L 145 ILE L 151 -1 N TRP L 149 O ARG L 156 SHEET 3 AA6 4 SER L 192 HIS L 199 -1 O THR L 194 N LYS L 150 SHEET 4 AA6 4 SER L 202 ASN L 211 -1 O ILE L 206 N ALA L 197 SHEET 1 AA7 4 GLU H 6 SER H 7 0 SHEET 2 AA7 4 LYS H 19 ALA H 23 -1 O SER H 21 N SER H 7 SHEET 3 AA7 4 ILE H 78 GLU H 82 -1 O LEU H 79 N CYS H 22 SHEET 4 AA7 4 THR H 69 ASP H 73 -1 N THR H 69 O GLU H 82 SHEET 1 AA8 6 LEU H 11 VAL H 12 0 SHEET 2 AA8 6 THR H 113 VAL H 117 1 O THR H 116 N VAL H 12 SHEET 3 AA8 6 ALA H 92 ARG H 98 -1 N TYR H 94 O THR H 113 SHEET 4 AA8 6 MET H 34 GLN H 39 -1 N VAL H 37 O TYR H 95 SHEET 5 AA8 6 LEU H 45 ILE H 51 -1 O ILE H 51 N MET H 34 SHEET 6 AA8 6 ILE H 58 TYR H 60 -1 O TYR H 59 N GLU H 50 SHEET 1 AA9 4 LEU H 11 VAL H 12 0 SHEET 2 AA9 4 THR H 113 VAL H 117 1 O THR H 116 N VAL H 12 SHEET 3 AA9 4 ALA H 92 ARG H 98 -1 N TYR H 94 O THR H 113 SHEET 4 AA9 4 TYR H 108 TRP H 109 -1 O TYR H 108 N ARG H 98 SHEET 1 AB1 4 SER H 126 LEU H 130 0 SHEET 2 AB1 4 SER H 141 TYR H 151 -1 O LEU H 147 N TYR H 128 SHEET 3 AB1 4 TYR H 181 THR H 190 -1 O VAL H 187 N LEU H 144 SHEET 4 AB1 4 VAL H 169 LEU H 176 -1 N HIS H 170 O SER H 186 SHEET 1 AB2 3 THR H 157 TRP H 160 0 SHEET 2 AB2 3 THR H 200 HIS H 205 -1 O ALA H 204 N THR H 157 SHEET 3 AB2 3 THR H 210 LYS H 215 -1 O VAL H 212 N VAL H 203 SSBOND 1 CYS C 148 CYS C 157 1555 1555 2.08 SSBOND 2 CYS L 23 CYS L 89 1555 1555 2.11 SSBOND 3 CYS L 135 CYS L 195 1555 1555 2.05 SSBOND 4 CYS H 22 CYS H 96 1555 1555 2.07 SSBOND 5 CYS H 146 CYS H 201 1555 1555 2.05 LINK O GLY C 42 NA NA C 610 1555 1555 2.28 LINK O ALA C 44 NA NA C 609 1555 1555 2.44 LINK O VAL C 45 NA NA C 610 1555 1555 2.55 LINK OD1 ASN C 49 NA NA C 609 1555 1555 2.40 LINK ND2 ASN C 141 C1 NAG C 602 1555 1555 1.47 LINK O SER C 279 NA NA C 609 1555 1555 2.79 LINK OG SER C 279 NA NA C 609 1555 1555 2.33 LINK OD1 ASN C 311 NA NA C 609 1555 1555 2.77 LINK O LEU C 376 NA NA C 610 1555 1555 2.34 LINK OD2 ASP C 379 NA NA C 610 1555 1555 2.92 LINK OG SER C 380 NA NA C 610 1555 1555 2.65 LINK NA NA C 609 O HOH C 705 1555 1555 2.72 CISPEP 1 ASP C 25 GLU C 26 0 0.05 CISPEP 2 SER L 7 PRO L 8 0 -5.00 CISPEP 3 TYR L 95 PRO L 96 0 -3.86 CISPEP 4 TYR L 141 PRO L 142 0 -0.61 CISPEP 5 GLY H 135 ASP H 136 0 -22.33 CISPEP 6 THR H 137 THR H 138 0 -17.76 CISPEP 7 THR H 138 GLY H 139 0 3.59 CISPEP 8 PHE H 152 PRO H 153 0 -4.73 CISPEP 9 GLU H 154 PRO H 155 0 4.58 CISPEP 10 TRP H 194 PRO H 195 0 -3.65 SITE 1 AC1 5 TYR C 301 PHE C 309 GLY C 475 TYR C 477 SITE 2 AC1 5 TRP C 478 SITE 1 AC2 4 ARG C 133 ALA C 137 PRO C 144 TYR C 178 SITE 1 AC3 1 GLU C 181 SITE 1 AC4 5 VAL C 34 LEU C 37 LEU C 229 TYR C 232 SITE 2 AC4 5 ILE C 310 SITE 1 AC5 9 PHE C 43 ALA C 44 ASP C 46 PHE C 278 SITE 2 AC5 9 SER C 279 LEU C 280 GLY C 281 PHE C 284 SITE 3 AC5 9 HOH C 705 SITE 1 AC6 1 PHE C 536 SITE 1 AC7 5 ALA C 44 ASN C 49 SER C 279 ASN C 311 SITE 2 AC7 5 HOH C 705 SITE 1 AC8 5 GLY C 42 VAL C 45 LEU C 376 ASP C 379 SITE 2 AC8 5 SER C 380 SITE 1 AC9 4 TYR C 69 GLN C 275 SER C 279 SER C 315 SITE 1 AD1 2 THR C 140 ASN C 141 CRYST1 97.348 140.748 166.760 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 0.010272 0.000000 0.000000 0.00000 SCALE2 0.000000 0.007105 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005997 0.00000