HEADER HORMONE RECEPTOR/ANTAGONIST 01-FEB-12 4DJH
TITLE STRUCTURE OF THE HUMAN KAPPA OPIOID RECEPTOR IN COMPLEX WITH JDTIC
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KAPPA-TYPE OPIOID RECEPTOR, LYSOZYME;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP P41145 RESIDUES 43-261, UNP P00720 RESIDUES 2-161, UNP
COMPND 5 P41145 RESIDUES 362-358;
COMPND 6 SYNONYM: K-OR-1, KOR-1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ENTEROBACTERIA PHAGE T4;
SOURCE 3 ORGANISM_COMMON: HUMAN, BACTERIOPHAGE T4;
SOURCE 4 ORGANISM_TAXID: 9606, 10665;
SOURCE 5 GENE: OPRK, OPRK1, OPRK, E;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1
KEYWDS JDTIC, GPCR NEWTORK, PSI-BIOLOGY, KOR, HKOR, KOP, STRUCTURAL
KEYWDS 2 GENOMICS, PROTEIN STRUCTURE INITIATIVE, GPCR NETWORK, G-PROTEIN
KEYWDS 3 COUPLED RECEPTOR, GPCR, 7TM, KAPPA OPIOID RECEPTOR, DYNORPHIN,
KEYWDS 4 MEMBRANE PROTEIN, TRANSMEMBRANE, HORMONE RECEPTOR, HYDROLASE,
KEYWDS 5 HORMONE RECEPTOR-ANTAGONIST COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.WU,D.WACKER,V.KATRITCH,M.MILENI,G.W.HAN,E.VARDY,W.LIU,A.A.THOMPSON,
AUTHOR 2 X.P.HUANG,F.I.CARROLL,S.W.MASCARELLA,R.B.WESTKAEMPER,P.D.MOSIER,
AUTHOR 3 B.L.ROTH,V.CHEREZOV,R.C.STEVENS,GPCR NETWORK (GPCR)
REVDAT 5 13-SEP-23 4DJH 1 REMARK SEQADV LINK
REVDAT 4 26-JUL-17 4DJH 1 SOURCE REMARK
REVDAT 3 08-AUG-12 4DJH 1 JRNL KEYWDS
REVDAT 2 30-MAY-12 4DJH 1 JRNL
REVDAT 1 21-MAR-12 4DJH 0
JRNL AUTH H.WU,D.WACKER,M.MILENI,V.KATRITCH,G.W.HAN,E.VARDY,W.LIU,
JRNL AUTH 2 A.A.THOMPSON,X.P.HUANG,F.I.CARROLL,S.W.MASCARELLA,
JRNL AUTH 3 R.B.WESTKAEMPER,P.D.MOSIER,B.L.ROTH,V.CHEREZOV,R.C.STEVENS
JRNL TITL TRUCTURE OF THE HUMAN KAPPA-OPIOID RECEPTOR IN COMPLEX WITH
JRNL TITL 2 JDTIC
JRNL REF NATURE V. 485 327 2012
JRNL REFN ISSN 0028-0836
JRNL PMID 22437504
JRNL DOI 10.1038/NATURE10939
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.3_928)
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) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.86
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 37023
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.229
REMARK 3 R VALUE (WORKING SET) : 0.227
REMARK 3 FREE R VALUE : 0.265
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1851
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 35.8642 - 6.2380 0.98 3759 185 0.2030 0.2292
REMARK 3 2 6.2380 - 4.9554 0.98 3569 200 0.2268 0.2572
REMARK 3 3 4.9554 - 4.3302 0.99 3590 189 0.1937 0.2230
REMARK 3 4 4.3302 - 3.9349 0.99 3534 179 0.2103 0.2287
REMARK 3 5 3.9349 - 3.6531 0.99 3553 188 0.2143 0.2800
REMARK 3 6 3.6531 - 3.4379 0.99 3522 197 0.2475 0.2996
REMARK 3 7 3.4379 - 3.2659 0.99 3504 191 0.2627 0.3120
REMARK 3 8 3.2659 - 3.1238 0.98 3480 194 0.2692 0.3483
REMARK 3 9 3.1238 - 3.0036 0.96 3416 172 0.3188 0.3373
REMARK 3 10 3.0036 - 2.9000 0.92 3245 156 0.3763 0.4846
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.86
REMARK 3 K_SOL : 0.30
REMARK 3 B_SOL : 49.00
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.540
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.470
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) : 6.59620
REMARK 3 B22 (A**2) : -2.37900
REMARK 3 B33 (A**2) : -4.21720
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.005 7218
REMARK 3 ANGLE : 0.767 9833
REMARK 3 CHIRALITY : 0.039 1179
REMARK 3 PLANARITY : 0.003 1200
REMARK 3 DIHEDRAL : 13.168 2521
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 55:261)
REMARK 3 ORIGIN FOR THE GROUP (A): 4.6371 -21.1548 49.2538
REMARK 3 T TENSOR
REMARK 3 T11: 0.6972 T22: 0.4607
REMARK 3 T33: 0.4009 T12: 0.0246
REMARK 3 T13: -0.0077 T23: -0.0332
REMARK 3 L TENSOR
REMARK 3 L11: 3.0389 L22: 2.6630
REMARK 3 L33: 0.7683 L12: -0.4119
REMARK 3 L13: 0.4691 L23: 1.1810
REMARK 3 S TENSOR
REMARK 3 S11: -0.0959 S12: 0.0973 S13: 0.1202
REMARK 3 S21: 0.0876 S22: 0.0754 S23: -0.3103
REMARK 3 S31: 0.3814 S32: 0.2641 S33: 0.0422
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 1002:1161)
REMARK 3 ORIGIN FOR THE GROUP (A): -24.5103 -10.5759 3.3733
REMARK 3 T TENSOR
REMARK 3 T11: 0.3492 T22: 0.8854
REMARK 3 T33: 0.5481 T12: 0.0214
REMARK 3 T13: -0.0002 T23: 0.0758
REMARK 3 L TENSOR
REMARK 3 L11: 2.2730 L22: 2.7927
REMARK 3 L33: 4.5169 L12: 0.2642
REMARK 3 L13: 0.2335 L23: -1.4661
REMARK 3 S TENSOR
REMARK 3 S11: 0.0841 S12: -0.7230 S13: -0.3896
REMARK 3 S21: 0.2728 S22: -0.0417 S23: 0.2822
REMARK 3 S31: -0.2846 S32: -0.0690 S33: 0.0237
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 263:347)
REMARK 3 ORIGIN FOR THE GROUP (A): -3.3462 -26.7166 43.8287
REMARK 3 T TENSOR
REMARK 3 T11: 0.6302 T22: 0.3994
REMARK 3 T33: 0.5035 T12: -0.0823
REMARK 3 T13: 0.0097 T23: -0.0013
REMARK 3 L TENSOR
REMARK 3 L11: 4.0035 L22: 3.0869
REMARK 3 L33: 1.1365 L12: -0.1525
REMARK 3 L13: 0.4481 L23: 0.1480
REMARK 3 S TENSOR
REMARK 3 S11: -0.1114 S12: 0.4115 S13: -0.0333
REMARK 3 S21: 0.0448 S22: -0.0559 S23: 0.1707
REMARK 3 S31: 1.0484 S32: -0.1977 S33: 0.1950
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN B AND RESID 55:261)
REMARK 3 ORIGIN FOR THE GROUP (A): 2.8313 -64.0876 49.7661
REMARK 3 T TENSOR
REMARK 3 T11: 0.6386 T22: 0.4233
REMARK 3 T33: 0.3426 T12: -0.0004
REMARK 3 T13: -0.0416 T23: 0.0196
REMARK 3 L TENSOR
REMARK 3 L11: 1.9258 L22: 2.7825
REMARK 3 L33: 1.5448 L12: -0.2194
REMARK 3 L13: 0.7902 L23: -0.3037
REMARK 3 S TENSOR
REMARK 3 S11: -0.1406 S12: -0.2933 S13: 0.1768
REMARK 3 S21: 0.8008 S22: 0.0396 S23: -0.0401
REMARK 3 S31: -0.4380 S32: -0.2996 S33: 0.1120
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN B AND RESID 1002:1161)
REMARK 3 ORIGIN FOR THE GROUP (A): 36.1971 -64.4232 7.5263
REMARK 3 T TENSOR
REMARK 3 T11: 0.3788 T22: 0.8963
REMARK 3 T33: 0.4169 T12: 0.0176
REMARK 3 T13: 0.0240 T23: 0.0355
REMARK 3 L TENSOR
REMARK 3 L11: 2.7010 L22: 2.2448
REMARK 3 L33: 2.9089 L12: -0.6687
REMARK 3 L13: 1.3883 L23: -1.3554
REMARK 3 S TENSOR
REMARK 3 S11: -0.0510 S12: 0.4267 S13: 0.2116
REMARK 3 S21: -0.2501 S22: 0.0658 S23: -0.0091
REMARK 3 S31: -0.0141 S32: -0.2441 S33: -0.0061
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN B AND RESID 263:347)
REMARK 3 ORIGIN FOR THE GROUP (A): 10.2808 -57.4901 44.8133
REMARK 3 T TENSOR
REMARK 3 T11: 0.7469 T22: 0.4532
REMARK 3 T33: 0.6533 T12: -0.0990
REMARK 3 T13: -0.1113 T23: 0.0214
REMARK 3 L TENSOR
REMARK 3 L11: 3.4196 L22: 2.7330
REMARK 3 L33: 4.2934 L12: -0.3387
REMARK 3 L13: 0.5193 L23: -1.1185
REMARK 3 S TENSOR
REMARK 3 S11: -0.1099 S12: 0.2715 S13: 0.2306
REMARK 3 S21: 0.3851 S22: 0.0930 S23: -0.0933
REMARK 3 S31: -1.2316 S32: 0.3129 S33: 0.0041
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THERE ARE SOME UNKNOWN DENSITIES
REMARK 3 LOCATED NEAR THE LIGAND BINDING SITE AND AT THE END OF THE SIDE
REMARK 3 CHAIN OF CYS345 ON BOTH A AND B CHAINS. THEY HAVE NOT BEEN
REMARK 3 MODELLED
REMARK 4
REMARK 4 4DJH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-FEB-12.
REMARK 100 THE DEPOSITION ID IS D_1000070406.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-DEC-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 60
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0330
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : DOUBLE CRYSTAL MONOCHROMATOR AND
REMARK 200 K-B PAIR OF BIOMORPH MIRRORS FOR
REMARK 200 VERTICAL AND HORIZONTAL FOCUSING
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38323
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
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 (%) : 97.1
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.18000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.95000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.300
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: POLY ALA MODEL OF PDB ENTRY 3ODU. ENSEMBLE OF T4L
REMARK 200 MODELS FROM PDB ENTRIES 2RH1, 3EML,3ODU, 3PBL, AND 3RZE.
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM CITRATE PH 6.0, 30%
REMARK 280 (V/V) PEG400, 400 MM POTASSIUM NITRATE, LIPIDIC CUBIC PHASE,
REMARK 280 TEMPERATURE 293K
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 27.44800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 102.64400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 73.64850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 102.64400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.44800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 73.64850
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THE DIMERIC QUATERNARY STRUCTURE HAS NOT BEEN CONFIRMED
REMARK 300 EXPERIMENTALLY
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 44690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2730 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 44330 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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: A
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -73.64850
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 102.64400
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 38
REMARK 465 GLY A 39
REMARK 465 THR A 40
REMARK 465 THR A 41
REMARK 465 MET A 42
REMARK 465 GLY A 43
REMARK 465 SER A 44
REMARK 465 GLU A 45
REMARK 465 ASP A 46
REMARK 465 ALA A 47
REMARK 465 GLN A 48
REMARK 465 LEU A 49
REMARK 465 GLU A 50
REMARK 465 PRO A 51
REMARK 465 ALA A 52
REMARK 465 HIS A 53
REMARK 465 ILE A 54
REMARK 465 THR A 302
REMARK 465 SER A 303
REMARK 465 HIS A 304
REMARK 465 SER A 305
REMARK 465 THR A 306
REMARK 465 LEU A 348
REMARK 465 LYS A 349
REMARK 465 MET A 350
REMARK 465 ARG A 351
REMARK 465 MET A 352
REMARK 465 GLU A 353
REMARK 465 ARG A 354
REMARK 465 GLN A 355
REMARK 465 SER A 356
REMARK 465 THR A 357
REMARK 465 SER A 358
REMARK 465 GLY B 38
REMARK 465 GLY B 39
REMARK 465 THR B 40
REMARK 465 THR B 41
REMARK 465 MET B 42
REMARK 465 GLY B 43
REMARK 465 SER B 44
REMARK 465 GLU B 45
REMARK 465 ASP B 46
REMARK 465 ALA B 47
REMARK 465 GLN B 48
REMARK 465 LEU B 49
REMARK 465 GLU B 50
REMARK 465 PRO B 51
REMARK 465 ALA B 52
REMARK 465 HIS B 53
REMARK 465 ILE B 54
REMARK 465 SER B 301
REMARK 465 THR B 302
REMARK 465 SER B 303
REMARK 465 HIS B 304
REMARK 465 LEU B 348
REMARK 465 LYS B 349
REMARK 465 MET B 350
REMARK 465 ARG B 351
REMARK 465 MET B 352
REMARK 465 GLU B 353
REMARK 465 ARG B 354
REMARK 465 GLN B 355
REMARK 465 SER B 356
REMARK 465 THR B 357
REMARK 465 SER B 358
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 ILE A 85 CG1 CG2 CD1
REMARK 470 THR A 88 OG1 CG2
REMARK 470 LYS A 89 CD CE NZ
REMARK 470 LYS A 165 NZ
REMARK 470 LEU A 167 CG CD1 CD2
REMARK 470 PHE A 169 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 200 CG CD CE NZ
REMARK 470 ASP A 217 CG OD1 OD2
REMARK 470 ARG A 257 NE CZ NH1 NH2
REMARK 470 LEU A 259 CG CD1 CD2
REMARK 470 GLU A1022 CG CD OE1 OE2
REMARK 470 LYS A1043 CE NZ
REMARK 470 LYS A1065 CD CE NZ
REMARK 470 LYS A1083 CE NZ
REMARK 470 LYS A1124 CE NZ
REMARK 470 ARG A1137 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 265 CG CD CE NZ
REMARK 470 ARG A 267 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 270 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 271 CG CD NE CZ NH1 NH2
REMARK 470 VAL A 296 CG1 CG2
REMARK 470 SER A 301 OG
REMARK 470 GLU A 335 CG CD OE1 OE2
REMARK 470 ARG A 342 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 86 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 89 CD CE NZ
REMARK 470 LYS B 132 CG CD CE NZ
REMARK 470 LYS B 165 CD CE NZ
REMARK 470 LYS B 200 CG CD CE NZ
REMARK 470 ARG B 202 CD NE CZ NH1 NH2
REMARK 470 GLU B 203 CG CD OE1 OE2
REMARK 470 ASP B 204 CG OD1 OD2
REMARK 470 LYS B 254 CG CD CE NZ
REMARK 470 GLU B1005 CG CD OE1 OE2
REMARK 470 ARG B1014 CD NE CZ NH1 NH2
REMARK 470 LYS B1016 CG CD CE NZ
REMARK 470 LYS B1035 CG CD CE NZ
REMARK 470 SER B1036 OG
REMARK 470 LYS B1043 CG CD CE NZ
REMARK 470 SER B1044 OG
REMARK 470 ASP B1047 CG OD1 OD2
REMARK 470 LYS B1048 CG CD CE NZ
REMARK 470 LYS B1065 CG CD CE NZ
REMARK 470 ARG B1119 CZ NH1 NH2
REMARK 470 LYS B1124 CD CE NZ
REMARK 470 ARG B1137 CG CD NE CZ NH1 NH2
REMARK 470 LYS B1147 CG CD CE NZ
REMARK 470 ARG B 263 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 264 CG CD OE1 OE2
REMARK 470 LYS B 265 CG CD CE NZ
REMARK 470 ARG B 267 CG CD NE CZ NH1 NH2
REMARK 470 ASN B 268 CG OD1 ND2
REMARK 470 LEU B 269 CG CD1 CD2
REMARK 470 ARG B 271 CZ NH1 NH2
REMARK 470 VAL B 296 CG1 CG2
REMARK 470 GLU B 335 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 GLU A 203 -165.87 55.29
REMARK 500 ASP A 217 -46.19 84.60
REMARK 500 PHE A 235 -72.98 -146.88
REMARK 500 ASP A1020 -179.02 -58.53
REMARK 500 PRO A1037 42.47 -83.17
REMARK 500 PHE A1114 37.58 -93.58
REMARK 500 ASN B 122 -4.98 73.20
REMARK 500 HIS B 162 56.97 -141.41
REMARK 500 ASP B 204 -5.34 77.59
REMARK 500 ASP B 217 -36.84 82.26
REMARK 500 PHE B 235 -70.92 -150.22
REMARK 500 ASP B1020 -166.89 -73.51
REMARK 500 PRO B1037 43.39 -92.58
REMARK 500 LEU B1039 -31.54 73.01
REMARK 500 ALA B1049 -20.71 79.94
REMARK 500 GLU B1108 -70.45 -36.75
REMARK 500 PHE B1114 47.73 -86.02
REMARK 500 LYS B 265 -111.98 66.69
REMARK 500 ASP B 266 53.14 -91.79
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 OLC B 1302
REMARK 610 OLC B 1303
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE JDC A 1300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT A 1301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE JDC B 1300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC B 1302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC B 1303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 1304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 1305
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: GPCR-56 RELATED DB: TARGETTRACK
DBREF 4DJH A 43 261 UNP P41145 OPRK_HUMAN 43 261
DBREF 4DJH A 1002 1161 UNP P00720 LYS_BPT4 2 161
DBREF 4DJH A 263 358 UNP P41145 OPRK_HUMAN 263 358
DBREF 4DJH B 43 261 UNP P41145 OPRK_HUMAN 43 261
DBREF 4DJH B 1002 1161 UNP P00720 LYS_BPT4 2 161
DBREF 4DJH B 263 358 UNP P41145 OPRK_HUMAN 263 358
SEQADV 4DJH GLY A 38 UNP P41145 EXPRESSION TAG
SEQADV 4DJH GLY A 39 UNP P41145 EXPRESSION TAG
SEQADV 4DJH THR A 40 UNP P41145 EXPRESSION TAG
SEQADV 4DJH THR A 41 UNP P41145 EXPRESSION TAG
SEQADV 4DJH MET A 42 UNP P41145 EXPRESSION TAG
SEQADV 4DJH LEU A 135 UNP P41145 ILE 135 ENGINEERED MUTATION
SEQADV 4DJH THR A 1054 UNP P00720 CYS 54 ENGINEERED MUTATION
SEQADV 4DJH ALA A 1097 UNP P00720 CYS 97 ENGINEERED MUTATION
SEQADV 4DJH GLY B 38 UNP P41145 EXPRESSION TAG
SEQADV 4DJH GLY B 39 UNP P41145 EXPRESSION TAG
SEQADV 4DJH THR B 40 UNP P41145 EXPRESSION TAG
SEQADV 4DJH THR B 41 UNP P41145 EXPRESSION TAG
SEQADV 4DJH MET B 42 UNP P41145 EXPRESSION TAG
SEQADV 4DJH LEU B 135 UNP P41145 ILE 135 ENGINEERED MUTATION
SEQADV 4DJH THR B 1054 UNP P00720 CYS 54 ENGINEERED MUTATION
SEQADV 4DJH ALA B 1097 UNP P00720 CYS 97 ENGINEERED MUTATION
SEQRES 1 A 480 GLY GLY THR THR MET GLY SER GLU ASP ALA GLN LEU GLU
SEQRES 2 A 480 PRO ALA HIS ILE SER PRO ALA ILE PRO VAL ILE ILE THR
SEQRES 3 A 480 ALA VAL TYR SER VAL VAL PHE VAL VAL GLY LEU VAL GLY
SEQRES 4 A 480 ASN SER LEU VAL MET PHE VAL ILE ILE ARG TYR THR LYS
SEQRES 5 A 480 MET LYS THR ALA THR ASN ILE TYR ILE PHE ASN LEU ALA
SEQRES 6 A 480 LEU ALA ASP ALA LEU VAL THR THR THR MET PRO PHE GLN
SEQRES 7 A 480 SER THR VAL TYR LEU MET ASN SER TRP PRO PHE GLY ASP
SEQRES 8 A 480 VAL LEU CYS LYS ILE VAL LEU SER ILE ASP TYR TYR ASN
SEQRES 9 A 480 MET PHE THR SER ILE PHE THR LEU THR MET MET SER VAL
SEQRES 10 A 480 ASP ARG TYR ILE ALA VAL CYS HIS PRO VAL LYS ALA LEU
SEQRES 11 A 480 ASP PHE ARG THR PRO LEU LYS ALA LYS ILE ILE ASN ILE
SEQRES 12 A 480 CYS ILE TRP LEU LEU SER SER SER VAL GLY ILE SER ALA
SEQRES 13 A 480 ILE VAL LEU GLY GLY THR LYS VAL ARG GLU ASP VAL ASP
SEQRES 14 A 480 VAL ILE GLU CYS SER LEU GLN PHE PRO ASP ASP ASP TYR
SEQRES 15 A 480 SER TRP TRP ASP LEU PHE MET LYS ILE CYS VAL PHE ILE
SEQRES 16 A 480 PHE ALA PHE VAL ILE PRO VAL LEU ILE ILE ILE VAL CYS
SEQRES 17 A 480 TYR THR LEU MET ILE LEU ARG LEU LYS SER VAL ARG LEU
SEQRES 18 A 480 LEU SER GLY ASN ILE PHE GLU MET LEU ARG ILE ASP GLU
SEQRES 19 A 480 GLY LEU ARG LEU LYS ILE TYR LYS ASP THR GLU GLY TYR
SEQRES 20 A 480 TYR THR ILE GLY ILE GLY HIS LEU LEU THR LYS SER PRO
SEQRES 21 A 480 SER LEU ASN ALA ALA LYS SER GLU LEU ASP LYS ALA ILE
SEQRES 22 A 480 GLY ARG ASN THR ASN GLY VAL ILE THR LYS ASP GLU ALA
SEQRES 23 A 480 GLU LYS LEU PHE ASN GLN ASP VAL ASP ALA ALA VAL ARG
SEQRES 24 A 480 GLY ILE LEU ARG ASN ALA LYS LEU LYS PRO VAL TYR ASP
SEQRES 25 A 480 SER LEU ASP ALA VAL ARG ARG ALA ALA LEU ILE ASN MET
SEQRES 26 A 480 VAL PHE GLN MET GLY GLU THR GLY VAL ALA GLY PHE THR
SEQRES 27 A 480 ASN SER LEU ARG MET LEU GLN GLN LYS ARG TRP ASP GLU
SEQRES 28 A 480 ALA ALA VAL ASN LEU ALA LYS SER ARG TRP TYR ASN GLN
SEQRES 29 A 480 THR PRO ASN ARG ALA LYS ARG VAL ILE THR THR PHE ARG
SEQRES 30 A 480 THR GLY THR TRP ASP ALA TYR ARG GLU LYS ASP ARG ASN
SEQRES 31 A 480 LEU ARG ARG ILE THR ARG LEU VAL LEU VAL VAL VAL ALA
SEQRES 32 A 480 VAL PHE VAL VAL CYS TRP THR PRO ILE HIS ILE PHE ILE
SEQRES 33 A 480 LEU VAL GLU ALA LEU GLY SER THR SER HIS SER THR ALA
SEQRES 34 A 480 ALA LEU SER SER TYR TYR PHE CYS ILE ALA LEU GLY TYR
SEQRES 35 A 480 THR ASN SER SER LEU ASN PRO ILE LEU TYR ALA PHE LEU
SEQRES 36 A 480 ASP GLU ASN PHE LYS ARG CYS PHE ARG ASP PHE CYS PHE
SEQRES 37 A 480 PRO LEU LYS MET ARG MET GLU ARG GLN SER THR SER
SEQRES 1 B 480 GLY GLY THR THR MET GLY SER GLU ASP ALA GLN LEU GLU
SEQRES 2 B 480 PRO ALA HIS ILE SER PRO ALA ILE PRO VAL ILE ILE THR
SEQRES 3 B 480 ALA VAL TYR SER VAL VAL PHE VAL VAL GLY LEU VAL GLY
SEQRES 4 B 480 ASN SER LEU VAL MET PHE VAL ILE ILE ARG TYR THR LYS
SEQRES 5 B 480 MET LYS THR ALA THR ASN ILE TYR ILE PHE ASN LEU ALA
SEQRES 6 B 480 LEU ALA ASP ALA LEU VAL THR THR THR MET PRO PHE GLN
SEQRES 7 B 480 SER THR VAL TYR LEU MET ASN SER TRP PRO PHE GLY ASP
SEQRES 8 B 480 VAL LEU CYS LYS ILE VAL LEU SER ILE ASP TYR TYR ASN
SEQRES 9 B 480 MET PHE THR SER ILE PHE THR LEU THR MET MET SER VAL
SEQRES 10 B 480 ASP ARG TYR ILE ALA VAL CYS HIS PRO VAL LYS ALA LEU
SEQRES 11 B 480 ASP PHE ARG THR PRO LEU LYS ALA LYS ILE ILE ASN ILE
SEQRES 12 B 480 CYS ILE TRP LEU LEU SER SER SER VAL GLY ILE SER ALA
SEQRES 13 B 480 ILE VAL LEU GLY GLY THR LYS VAL ARG GLU ASP VAL ASP
SEQRES 14 B 480 VAL ILE GLU CYS SER LEU GLN PHE PRO ASP ASP ASP TYR
SEQRES 15 B 480 SER TRP TRP ASP LEU PHE MET LYS ILE CYS VAL PHE ILE
SEQRES 16 B 480 PHE ALA PHE VAL ILE PRO VAL LEU ILE ILE ILE VAL CYS
SEQRES 17 B 480 TYR THR LEU MET ILE LEU ARG LEU LYS SER VAL ARG LEU
SEQRES 18 B 480 LEU SER GLY ASN ILE PHE GLU MET LEU ARG ILE ASP GLU
SEQRES 19 B 480 GLY LEU ARG LEU LYS ILE TYR LYS ASP THR GLU GLY TYR
SEQRES 20 B 480 TYR THR ILE GLY ILE GLY HIS LEU LEU THR LYS SER PRO
SEQRES 21 B 480 SER LEU ASN ALA ALA LYS SER GLU LEU ASP LYS ALA ILE
SEQRES 22 B 480 GLY ARG ASN THR ASN GLY VAL ILE THR LYS ASP GLU ALA
SEQRES 23 B 480 GLU LYS LEU PHE ASN GLN ASP VAL ASP ALA ALA VAL ARG
SEQRES 24 B 480 GLY ILE LEU ARG ASN ALA LYS LEU LYS PRO VAL TYR ASP
SEQRES 25 B 480 SER LEU ASP ALA VAL ARG ARG ALA ALA LEU ILE ASN MET
SEQRES 26 B 480 VAL PHE GLN MET GLY GLU THR GLY VAL ALA GLY PHE THR
SEQRES 27 B 480 ASN SER LEU ARG MET LEU GLN GLN LYS ARG TRP ASP GLU
SEQRES 28 B 480 ALA ALA VAL ASN LEU ALA LYS SER ARG TRP TYR ASN GLN
SEQRES 29 B 480 THR PRO ASN ARG ALA LYS ARG VAL ILE THR THR PHE ARG
SEQRES 30 B 480 THR GLY THR TRP ASP ALA TYR ARG GLU LYS ASP ARG ASN
SEQRES 31 B 480 LEU ARG ARG ILE THR ARG LEU VAL LEU VAL VAL VAL ALA
SEQRES 32 B 480 VAL PHE VAL VAL CYS TRP THR PRO ILE HIS ILE PHE ILE
SEQRES 33 B 480 LEU VAL GLU ALA LEU GLY SER THR SER HIS SER THR ALA
SEQRES 34 B 480 ALA LEU SER SER TYR TYR PHE CYS ILE ALA LEU GLY TYR
SEQRES 35 B 480 THR ASN SER SER LEU ASN PRO ILE LEU TYR ALA PHE LEU
SEQRES 36 B 480 ASP GLU ASN PHE LYS ARG CYS PHE ARG ASP PHE CYS PHE
SEQRES 37 B 480 PRO LEU LYS MET ARG MET GLU ARG GLN SER THR SER
HET JDC A1300 34
HET CIT A1301 13
HET JDC B1300 34
HET OLC B1302 16
HET OLC B1303 21
HET PEG B1304 7
HET PEG B1305 7
HETNAM JDC (3R)-7-HYDROXY-N-{(2S)-1-[(3R,4R)-4-(3-HYDROXYPHENYL)-
HETNAM 2 JDC 3,4-DIMETHYLPIPERIDIN-1-YL]-3-METHYLBUTAN-2-YL}-1,2,3,
HETNAM 3 JDC 4-TETRAHYDROISOQUINOLINE-3-CARBOXAMIDE
HETNAM CIT CITRIC ACID
HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN OLC 1-OLEOYL-R-GLYCEROL
FORMUL 3 JDC 2(C28 H39 N3 O3)
FORMUL 4 CIT C6 H8 O7
FORMUL 6 OLC 2(C21 H40 O4)
FORMUL 8 PEG 2(C4 H10 O3)
FORMUL 10 HOH *25(H2 O)
HELIX 1 1 PRO A 56 TYR A 87 1 32
HELIX 2 2 THR A 88 LYS A 91 5 4
HELIX 3 3 THR A 92 THR A 110 1 19
HELIX 4 4 THR A 111 ASN A 122 1 12
HELIX 5 5 PHE A 126 VAL A 160 1 35
HELIX 6 6 PHE A 169 LEU A 196 1 28
HELIX 7 7 ASP A 218 ALA A 234 1 17
HELIX 8 8 PHE A 235 SER A 260 1 26
HELIX 9 9 ASN A 1002 GLU A 1011 1 10
HELIX 10 10 SER A 1038 GLY A 1051 1 14
HELIX 11 11 THR A 1059 ASN A 1081 1 23
HELIX 12 12 LYS A 1083 LEU A 1091 1 9
HELIX 13 13 ASP A 1092 GLY A 1113 1 22
HELIX 14 14 PHE A 1114 GLN A 1123 1 10
HELIX 15 15 ARG A 1125 LYS A 1135 1 11
HELIX 16 16 SER A 1136 THR A 1142 1 7
HELIX 17 17 THR A 1142 GLY A 1156 1 15
HELIX 18 18 ASP A 266 GLY A 300 1 35
HELIX 19 19 ALA A 308 ASP A 334 1 27
HELIX 20 20 ASP A 334 PHE A 346 1 13
HELIX 21 21 PRO B 56 TYR B 87 1 32
HELIX 22 22 THR B 88 LYS B 91 5 4
HELIX 23 23 THR B 92 THR B 110 1 19
HELIX 24 24 THR B 111 ASN B 122 1 12
HELIX 25 25 PHE B 126 HIS B 162 1 37
HELIX 26 26 HIS B 162 ARG B 170 1 9
HELIX 27 27 THR B 171 LEU B 196 1 26
HELIX 28 28 ASP B 218 ALA B 234 1 17
HELIX 29 29 PHE B 235 LEU B 258 1 24
HELIX 30 30 ASN B 1002 GLY B 1012 1 11
HELIX 31 31 LEU B 1039 GLY B 1051 1 13
HELIX 32 32 THR B 1059 ASN B 1081 1 23
HELIX 33 33 LEU B 1084 LEU B 1091 1 8
HELIX 34 34 ASP B 1092 GLY B 1107 1 16
HELIX 35 35 GLY B 1107 GLY B 1113 1 7
HELIX 36 36 PHE B 1114 GLN B 1123 1 10
HELIX 37 37 ARG B 1125 ALA B 1134 1 10
HELIX 38 38 SER B 1136 THR B 1142 1 7
HELIX 39 39 THR B 1142 GLY B 1156 1 15
HELIX 40 40 TRP B 1158 ARG B 263 5 5
HELIX 41 41 ARG B 270 GLY B 300 1 31
HELIX 42 42 ALA B 308 ASP B 334 1 27
HELIX 43 43 ASP B 334 PHE B 346 1 13
SHEET 1 A 2 GLY A 197 VAL A 201 0
SHEET 2 A 2 ILE A 208 LEU A 212 -1 O GLU A 209 N LYS A 200
SHEET 1 B 3 ARG A1014 LYS A1019 0
SHEET 2 B 3 TYR A1025 GLY A1028 -1 O THR A1026 N TYR A1018
SHEET 3 B 3 HIS A1031 THR A1034 -1 O LEU A1033 N TYR A1025
SHEET 1 C 2 GLY B 197 VAL B 201 0
SHEET 2 C 2 ILE B 208 LEU B 212 -1 O SER B 211 N GLY B 198
SHEET 1 D 3 ARG B1014 LYS B1019 0
SHEET 2 D 3 TYR B1025 GLY B1028 -1 O THR B1026 N TYR B1018
SHEET 3 D 3 HIS B1031 THR B1034 -1 O LEU B1033 N TYR B1025
SSBOND 1 CYS A 131 CYS A 210 1555 1555 2.03
SSBOND 2 CYS B 131 CYS B 210 1555 1555 2.03
LINK C GLY A 261 N ASN A1002 1555 1555 1.33
LINK N ARG A 263 C TYR A1161 1555 1555 1.33
LINK C GLY B 261 N ASN B1002 1555 1555 1.33
LINK N ARG B 263 C TYR B1161 1555 1555 1.33
SITE 1 AC1 14 THR A 111 GLN A 115 VAL A 134 ASP A 138
SITE 2 AC1 14 TYR A 139 LYS A 227 VAL A 230 TRP A 287
SITE 3 AC1 14 ILE A 290 ILE A 294 ILE A 316 TYR A 320
SITE 4 AC1 14 HOH A1303 HOH A1304
SITE 1 AC2 4 GLY A1012 ARG A1014 TYR A1018 HOH A1308
SITE 1 AC3 16 THR B 111 GLN B 115 LEU B 135 ASP B 138
SITE 2 AC3 16 MET B 142 CYS B 210 LYS B 227 VAL B 230
SITE 3 AC3 16 TRP B 287 ILE B 294 ILE B 316 TYR B 320
SITE 4 AC3 16 HOH B1307 HOH B1313 HOH B1314 HOH B1316
SITE 1 AC4 9 TRP A 221 TYR B 97 ASP B 155 ILE B 158
SITE 2 AC4 9 PHE B 169 LYS B 174 ILE B 178 CYS B 181
SITE 3 AC4 9 OLC B1303
SITE 1 AC5 7 GLY A 300 SER A 301 TYR B 157 HIS B 162
SITE 2 AC5 7 PRO B 163 VAL B 164 OLC B1302
SITE 1 AC6 1 LEU B 299
SITE 1 AC7 7 PRO A1037 SER A1038 LEU A1039 THR B 92
SITE 2 AC7 7 THR B 94 ARG B 270 ILE B 272
CRYST1 54.896 147.297 205.288 90.00 90.00 90.00 P 21 21 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 0.018216 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006789 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004871 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
