HEADER IMMUNE SYSTEM 29-APR-15 4ZJS
TITLE CRYSTAL STRUCTURE OF A CHIMERIC ACETYLCHOLINE BINDING PROTEIN FROM
TITLE 2 APLYSIA CALIFORNICA (AC-ACHBP) CONTAINING THE MAIN IMMUNOGENIC REGION
TITLE 3 (MIR) FROM THE HUMAN ALPHA 1 SUBUNIT OF THE MUSCLE NICOTINIC
TITLE 4 ACETYLCHOLINE RECEPTOR IN COMPLEX WITH ANATOXIN-A.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINE RECEPTOR SUBUNIT ALPHA,SOLUBLE ACETYLCHOLINE
COMPND 3 RECEPTOR,ACETYLCHOLINE RECEPTOR SUBUNIT ALPHA,SOLUBLE ACETYLCHOLINE
COMPND 4 RECEPTOR;
COMPND 5 CHAIN: A, B, C, D, E;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, APLYSIA CALIFORNICA;
SOURCE 3 ORGANISM_COMMON: HUMAN, CALIFORNIA SEA HARE;
SOURCE 4 ORGANISM_TAXID: 9606, 6500;
SOURCE 5 GENE: CHRNA1, ACHRA, CHNRA;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606
KEYWDS ANATOXIN-A, NICOTINIC, RECEPTOR, ACETYLCHOLINE, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR T.T.TALLEY,J.BOBANGO,J.WU,J.F.PARK,J.LUO,J.LINDSATROM,P.TAYLOR
REVDAT 2 27-SEP-23 4ZJS 1 SOURCE REMARK
REVDAT 1 13-MAY-15 4ZJS 0
JRNL AUTH J.LUO,P.TAYLOR,M.LOSEN,M.H.DE BAETS,G.D.SHELTON,J.LINDSTROM
JRNL TITL MAIN IMMUNOGENIC REGION STRUCTURE PROMOTES BINDING OF
JRNL TITL 2 CONFORMATION-DEPENDENT MYASTHENIA GRAVIS AUTOANTIBODIES,
JRNL TITL 3 NICOTINIC ACETYLCHOLINE RECEPTOR CONFORMATION MATURATION,
JRNL TITL 4 AND AGONIST SENSITIVITY.
JRNL REF J. NEUROSCI. V. 29 13898 2009
JRNL REFN ESSN 1529-2401
JRNL PMID 19890000
JRNL DOI 10.1523/JNEUROSCI.2833-09.2009
REMARK 2
REMARK 2 RESOLUTION. 2.23 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) : 2.23
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.93
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 71956
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.780
REMARK 3 FREE R VALUE TEST SET COUNT : 1999
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 48.9445 - 5.3727 1.00 5169 147 0.1822 0.1777
REMARK 3 2 5.3727 - 4.2652 1.00 5046 146 0.1526 0.1770
REMARK 3 3 4.2652 - 3.7263 1.00 5027 144 0.1658 0.2030
REMARK 3 4 3.7263 - 3.3857 1.00 5011 141 0.1956 0.2048
REMARK 3 5 3.3857 - 3.1431 1.00 4986 139 0.2167 0.2353
REMARK 3 6 3.1431 - 2.9578 0.99 4976 143 0.2271 0.3237
REMARK 3 7 2.9578 - 2.8097 0.99 4943 139 0.2384 0.3176
REMARK 3 8 2.8097 - 2.6874 0.99 4944 144 0.2297 0.2933
REMARK 3 9 2.6874 - 2.5839 1.00 4979 141 0.2340 0.2686
REMARK 3 10 2.5839 - 2.4948 1.00 4915 141 0.2287 0.2745
REMARK 3 11 2.4948 - 2.4168 1.00 5022 148 0.2098 0.2329
REMARK 3 12 2.4168 - 2.3477 1.00 4977 142 0.2154 0.2712
REMARK 3 13 2.3477 - 2.2859 1.00 4987 142 0.2215 0.2941
REMARK 3 14 2.2859 - 2.2301 1.00 4975 142 0.2267 0.2641
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) : 0.260
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.600
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 36.57
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.11
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 8306
REMARK 3 ANGLE : 1.034 11364
REMARK 3 CHIRALITY : 0.040 1301
REMARK 3 PLANARITY : 0.004 1459
REMARK 3 DIHEDRAL : 13.278 2890
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 4ZJS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-APR-15.
REMARK 100 THE DEPOSITION ID IS D_1000209422.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-AUG-09
REMARK 200 TEMPERATURE (KELVIN) : 88
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : .999
REMARK 200 MONOCHROMATOR : NULL
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 : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 72156
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.230
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY : 37.90
REMARK 200 R MERGE (I) : 0.19100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.23
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.27
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 17.20
REMARK 200 R MERGE FOR SHELL (I) : 0.95200
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: 2BYN, 2PGZ, 2BYP, 2BYS, 2BYR, 3C84, AND A HOMOLOGY
REMARK 200 MODEL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 17. 25.5% PEG 4000, 0.085 M TRIS HCL
REMARK 280 PH 8.5, 0.17 M LITHIUM SULFATE, 15% GLYCEROL, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 297K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z,-X,-Y
REMARK 290 7555 -Z,-X,Y
REMARK 290 8555 -Z,X,-Y
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z,-X
REMARK 290 11555 Y,-Z,-X
REMARK 290 12555 -Y,-Z,X
REMARK 290 13555 X+1/2,Y+1/2,Z+1/2
REMARK 290 14555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 15555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 16555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 17555 Z+1/2,X+1/2,Y+1/2
REMARK 290 18555 Z+1/2,-X+1/2,-Y+1/2
REMARK 290 19555 -Z+1/2,-X+1/2,Y+1/2
REMARK 290 20555 -Z+1/2,X+1/2,-Y+1/2
REMARK 290 21555 Y+1/2,Z+1/2,X+1/2
REMARK 290 22555 -Y+1/2,Z+1/2,-X+1/2
REMARK 290 23555 Y+1/2,-Z+1/2,-X+1/2
REMARK 290 24555 -Y+1/2,-Z+1/2,X+1/2
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 0.00000
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 0.00000
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 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 103.80200
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 103.80200
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 103.80200
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 103.80200
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 103.80200
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 103.80200
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 103.80200
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 103.80200
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 103.80200
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 103.80200
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 103.80200
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 103.80200
REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 103.80200
REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 103.80200
REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 103.80200
REMARK 290 SMTRY1 18 0.000000 0.000000 1.000000 103.80200
REMARK 290 SMTRY2 18 -1.000000 0.000000 0.000000 103.80200
REMARK 290 SMTRY3 18 0.000000 -1.000000 0.000000 103.80200
REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 103.80200
REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 103.80200
REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 103.80200
REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 103.80200
REMARK 290 SMTRY2 20 1.000000 0.000000 0.000000 103.80200
REMARK 290 SMTRY3 20 0.000000 -1.000000 0.000000 103.80200
REMARK 290 SMTRY1 21 0.000000 1.000000 0.000000 103.80200
REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 103.80200
REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 103.80200
REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 103.80200
REMARK 290 SMTRY2 22 0.000000 0.000000 1.000000 103.80200
REMARK 290 SMTRY3 22 -1.000000 0.000000 0.000000 103.80200
REMARK 290 SMTRY1 23 0.000000 1.000000 0.000000 103.80200
REMARK 290 SMTRY2 23 0.000000 0.000000 -1.000000 103.80200
REMARK 290 SMTRY3 23 -1.000000 0.000000 0.000000 103.80200
REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 103.80200
REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 103.80200
REMARK 290 SMTRY3 24 1.000000 0.000000 0.000000 103.80200
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: PENTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 12720 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -63.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E
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 ASP A -8
REMARK 465 TYR A -7
REMARK 465 LYS A -6
REMARK 465 ASP A -5
REMARK 465 ASP A -4
REMARK 465 ASP A -3
REMARK 465 ASP A -2
REMARK 465 LYS A -1
REMARK 465 LEU A 0
REMARK 465 SER A 1
REMARK 465 ARG A 208
REMARK 465 ALA A 209
REMARK 465 GLY A 210
REMARK 465 ASN A 211
REMARK 465 GLY A 212
REMARK 465 PHE A 213
REMARK 465 PHE A 214
REMARK 465 ARG A 215
REMARK 465 ASN A 216
REMARK 465 LEU A 217
REMARK 465 PHE A 218
REMARK 465 ASP A 219
REMARK 465 SER A 220
REMARK 465 ARG A 221
REMARK 465 ASP B -8
REMARK 465 TYR B -7
REMARK 465 LYS B -6
REMARK 465 ASP B -5
REMARK 465 ASP B -4
REMARK 465 ASP B -3
REMARK 465 ASP B -2
REMARK 465 LYS B -1
REMARK 465 LEU B 0
REMARK 465 SER B 1
REMARK 465 ARG B 208
REMARK 465 ALA B 209
REMARK 465 GLY B 210
REMARK 465 ASN B 211
REMARK 465 GLY B 212
REMARK 465 PHE B 213
REMARK 465 PHE B 214
REMARK 465 ARG B 215
REMARK 465 ASN B 216
REMARK 465 LEU B 217
REMARK 465 PHE B 218
REMARK 465 ASP B 219
REMARK 465 SER B 220
REMARK 465 ARG B 221
REMARK 465 ASP C -8
REMARK 465 TYR C -7
REMARK 465 LYS C -6
REMARK 465 ASP C -5
REMARK 465 ASP C -4
REMARK 465 ASP C -3
REMARK 465 ASP C -2
REMARK 465 LYS C -1
REMARK 465 LEU C 0
REMARK 465 SER C 1
REMARK 465 SER C 189
REMARK 465 ARG C 208
REMARK 465 ALA C 209
REMARK 465 GLY C 210
REMARK 465 ASN C 211
REMARK 465 GLY C 212
REMARK 465 PHE C 213
REMARK 465 PHE C 214
REMARK 465 ARG C 215
REMARK 465 ASN C 216
REMARK 465 LEU C 217
REMARK 465 PHE C 218
REMARK 465 ASP C 219
REMARK 465 SER C 220
REMARK 465 ARG C 221
REMARK 465 ASP D -8
REMARK 465 TYR D -7
REMARK 465 LYS D -6
REMARK 465 ASP D -5
REMARK 465 ASP D -4
REMARK 465 ASP D -3
REMARK 465 ASP D -2
REMARK 465 LYS D -1
REMARK 465 LEU D 0
REMARK 465 SER D 1
REMARK 465 ARG D 208
REMARK 465 ALA D 209
REMARK 465 GLY D 210
REMARK 465 ASN D 211
REMARK 465 GLY D 212
REMARK 465 PHE D 213
REMARK 465 PHE D 214
REMARK 465 ARG D 215
REMARK 465 ASN D 216
REMARK 465 LEU D 217
REMARK 465 PHE D 218
REMARK 465 ASP D 219
REMARK 465 SER D 220
REMARK 465 ARG D 221
REMARK 465 ASP E -8
REMARK 465 TYR E -7
REMARK 465 LYS E -6
REMARK 465 ASP E -5
REMARK 465 ASP E -4
REMARK 465 ASP E -3
REMARK 465 ASP E -2
REMARK 465 LYS E -1
REMARK 465 LEU E 0
REMARK 465 SER E 1
REMARK 465 ARG E 207
REMARK 465 ARG E 208
REMARK 465 ALA E 209
REMARK 465 GLY E 210
REMARK 465 ASN E 211
REMARK 465 GLY E 212
REMARK 465 PHE E 213
REMARK 465 PHE E 214
REMARK 465 ARG E 215
REMARK 465 ASN E 216
REMARK 465 LEU E 217
REMARK 465 PHE E 218
REMARK 465 ASP E 219
REMARK 465 SER E 220
REMARK 465 ARG E 221
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 GLU A 2 CG CD OE1 OE2
REMARK 470 LYS A 10 CG CD CE NZ
REMARK 470 LYS A 13 CG CD CE NZ
REMARK 470 GLU A 23 CG CD OE1 OE2
REMARK 470 ARG A 26 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 27 CG CD OE1 NE2
REMARK 470 LYS A 76 CG CD CE NZ
REMARK 470 GLU A 135 CG CD OE1 OE2
REMARK 470 GLU A 136 CG CD OE1 OE2
REMARK 470 LYS A 157 CG CD CE NZ
REMARK 470 LYS A 203 CG CD CE NZ
REMARK 470 GLU B 2 CG CD OE1 OE2
REMARK 470 LYS B 10 CG CD CE NZ
REMARK 470 LYS B 13 CG CD CE NZ
REMARK 470 ARG B 26 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 30 CG CD OE1 OE2
REMARK 470 GLU B 135 CG CD OE1 OE2
REMARK 470 GLU B 136 CG CD OE1 OE2
REMARK 470 LYS B 157 CG CD CE NZ
REMARK 470 GLU C 2 CG CD OE1 OE2
REMARK 470 ARG C 6 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 26 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 157 CG CD CE NZ
REMARK 470 GLU D 2 CG CD OE1 OE2
REMARK 470 ARG D 6 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 10 CG CD CE NZ
REMARK 470 LYS D 13 CG CD CE NZ
REMARK 470 GLU D 23 CG CD OE1 OE2
REMARK 470 ARG D 26 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 135 CG CD OE1 OE2
REMARK 470 GLU D 136 CG CD OE1 OE2
REMARK 470 LYS D 157 CG CD CE NZ
REMARK 470 GLU E 2 CG CD OE1 OE2
REMARK 470 ARG E 6 CG CD NE CZ NH1 NH2
REMARK 470 LYS E 10 CG CD CE NZ
REMARK 470 LYS E 13 CG CD CE NZ
REMARK 470 GLU E 23 CG CD OE1 OE2
REMARK 470 HIS E 25 CG ND1 CD2 CE1 NE2
REMARK 470 ARG E 26 CG CD NE CZ NH1 NH2
REMARK 470 GLN E 27 CG CD OE1 NE2
REMARK 470 GLU E 30 CG CD OE1 OE2
REMARK 470 LYS E 76 CG CD CE NZ
REMARK 470 GLU E 135 CG CD OE1 OE2
REMARK 470 GLU E 136 CG CD OE1 OE2
REMARK 470 LYS E 157 CG CD CE NZ
REMARK 470 ASP E 161 CG OD1 OD2
REMARK 470 LYS E 203 CG CD CE NZ
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 NH1 ARG D 59 OD2 ASP D 159 2.18
REMARK 500 NH1 ARG C 59 OD2 ASP C 159 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 C 192 C - N - CA ANGL. DEV. = 9.4 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 A 39 133.84 -172.33
REMARK 500 TYR A 72 44.34 -140.90
REMARK 500 TYR B 72 46.88 -145.80
REMARK 500 GLN B 105 76.08 -102.03
REMARK 500 ASP B 133 30.21 -94.35
REMARK 500 LEU C 65 52.07 -115.26
REMARK 500 TYR C 72 49.47 -140.52
REMARK 500 ASP D 39 132.45 -170.38
REMARK 500 TYR D 72 51.27 -141.55
REMARK 500 ASP D 133 39.06 -94.96
REMARK 500 LEU E 65 54.91 -113.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 4P0 B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 4P0 D 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 4P0 E 301
DBREF 4ZJS A 1 30 UNP P02708 ACHA_HUMAN 21 50
DBREF 4ZJS A 31 60 UNP Q8WSF8 Q8WSF8_APLCA 48 77
DBREF 4ZJS A 61 81 UNP P02708 ACHA_HUMAN 106 126
DBREF 4ZJS A 82 219 UNP Q8WSF8 Q8WSF8_APLCA 99 236
DBREF 4ZJS B 1 30 UNP P02708 ACHA_HUMAN 21 50
DBREF 4ZJS B 31 60 UNP Q8WSF8 Q8WSF8_APLCA 48 77
DBREF 4ZJS B 61 81 UNP P02708 ACHA_HUMAN 106 126
DBREF 4ZJS B 82 219 UNP Q8WSF8 Q8WSF8_APLCA 99 236
DBREF 4ZJS C 1 30 UNP P02708 ACHA_HUMAN 21 50
DBREF 4ZJS C 31 60 UNP Q8WSF8 Q8WSF8_APLCA 48 77
DBREF 4ZJS C 61 81 UNP P02708 ACHA_HUMAN 106 126
DBREF 4ZJS C 82 219 UNP Q8WSF8 Q8WSF8_APLCA 99 236
DBREF 4ZJS D 1 30 UNP P02708 ACHA_HUMAN 21 50
DBREF 4ZJS D 31 60 UNP Q8WSF8 Q8WSF8_APLCA 48 77
DBREF 4ZJS D 61 81 UNP P02708 ACHA_HUMAN 106 126
DBREF 4ZJS D 82 219 UNP Q8WSF8 Q8WSF8_APLCA 99 236
DBREF 4ZJS E 1 30 UNP P02708 ACHA_HUMAN 21 50
DBREF 4ZJS E 31 60 UNP Q8WSF8 Q8WSF8_APLCA 48 77
DBREF 4ZJS E 61 81 UNP P02708 ACHA_HUMAN 106 126
DBREF 4ZJS E 82 219 UNP Q8WSF8 Q8WSF8_APLCA 99 236
SEQADV 4ZJS ASP A -8 UNP P02708 EXPRESSION TAG
SEQADV 4ZJS TYR A -7 UNP P02708 EXPRESSION TAG
SEQADV 4ZJS LYS A -6 UNP P02708 EXPRESSION TAG
SEQADV 4ZJS ASP A -5 UNP P02708 EXPRESSION TAG
SEQADV 4ZJS ASP A -4 UNP P02708 EXPRESSION TAG
SEQADV 4ZJS ASP A -3 UNP P02708 EXPRESSION TAG
SEQADV 4ZJS ASP A -2 UNP P02708 EXPRESSION TAG
SEQADV 4ZJS LYS A -1 UNP P02708 EXPRESSION TAG
SEQADV 4ZJS LEU A 0 UNP P02708 EXPRESSION TAG
SEQADV 4ZJS SER A 220 UNP Q8WSF8 CLONING ARTIFACT
SEQADV 4ZJS ARG A 221 UNP Q8WSF8 CLONING ARTIFACT
SEQADV 4ZJS ASP B -8 UNP P02708 EXPRESSION TAG
SEQADV 4ZJS TYR B -7 UNP P02708 EXPRESSION TAG
SEQADV 4ZJS LYS B -6 UNP P02708 EXPRESSION TAG
SEQADV 4ZJS ASP B -5 UNP P02708 EXPRESSION TAG
SEQADV 4ZJS ASP B -4 UNP P02708 EXPRESSION TAG
SEQADV 4ZJS ASP B -3 UNP P02708 EXPRESSION TAG
SEQADV 4ZJS ASP B -2 UNP P02708 EXPRESSION TAG
SEQADV 4ZJS LYS B -1 UNP P02708 EXPRESSION TAG
SEQADV 4ZJS LEU B 0 UNP P02708 EXPRESSION TAG
SEQADV 4ZJS SER B 220 UNP Q8WSF8 CLONING ARTIFACT
SEQADV 4ZJS ARG B 221 UNP Q8WSF8 CLONING ARTIFACT
SEQADV 4ZJS ASP C -8 UNP P02708 EXPRESSION TAG
SEQADV 4ZJS TYR C -7 UNP P02708 EXPRESSION TAG
SEQADV 4ZJS LYS C -6 UNP P02708 EXPRESSION TAG
SEQADV 4ZJS ASP C -5 UNP P02708 EXPRESSION TAG
SEQADV 4ZJS ASP C -4 UNP P02708 EXPRESSION TAG
SEQADV 4ZJS ASP C -3 UNP P02708 EXPRESSION TAG
SEQADV 4ZJS ASP C -2 UNP P02708 EXPRESSION TAG
SEQADV 4ZJS LYS C -1 UNP P02708 EXPRESSION TAG
SEQADV 4ZJS LEU C 0 UNP P02708 EXPRESSION TAG
SEQADV 4ZJS SER C 220 UNP Q8WSF8 CLONING ARTIFACT
SEQADV 4ZJS ARG C 221 UNP Q8WSF8 CLONING ARTIFACT
SEQADV 4ZJS ASP D -8 UNP P02708 EXPRESSION TAG
SEQADV 4ZJS TYR D -7 UNP P02708 EXPRESSION TAG
SEQADV 4ZJS LYS D -6 UNP P02708 EXPRESSION TAG
SEQADV 4ZJS ASP D -5 UNP P02708 EXPRESSION TAG
SEQADV 4ZJS ASP D -4 UNP P02708 EXPRESSION TAG
SEQADV 4ZJS ASP D -3 UNP P02708 EXPRESSION TAG
SEQADV 4ZJS ASP D -2 UNP P02708 EXPRESSION TAG
SEQADV 4ZJS LYS D -1 UNP P02708 EXPRESSION TAG
SEQADV 4ZJS LEU D 0 UNP P02708 EXPRESSION TAG
SEQADV 4ZJS SER D 220 UNP Q8WSF8 CLONING ARTIFACT
SEQADV 4ZJS ARG D 221 UNP Q8WSF8 CLONING ARTIFACT
SEQADV 4ZJS ASP E -8 UNP P02708 EXPRESSION TAG
SEQADV 4ZJS TYR E -7 UNP P02708 EXPRESSION TAG
SEQADV 4ZJS LYS E -6 UNP P02708 EXPRESSION TAG
SEQADV 4ZJS ASP E -5 UNP P02708 EXPRESSION TAG
SEQADV 4ZJS ASP E -4 UNP P02708 EXPRESSION TAG
SEQADV 4ZJS ASP E -3 UNP P02708 EXPRESSION TAG
SEQADV 4ZJS ASP E -2 UNP P02708 EXPRESSION TAG
SEQADV 4ZJS LYS E -1 UNP P02708 EXPRESSION TAG
SEQADV 4ZJS LEU E 0 UNP P02708 EXPRESSION TAG
SEQADV 4ZJS SER E 220 UNP Q8WSF8 CLONING ARTIFACT
SEQADV 4ZJS ARG E 221 UNP Q8WSF8 CLONING ARTIFACT
SEQRES 1 A 230 ASP TYR LYS ASP ASP ASP ASP LYS LEU SER GLU HIS GLU
SEQRES 2 A 230 THR ARG LEU VAL ALA LYS LEU PHE LYS ASP TYR SER SER
SEQRES 3 A 230 VAL VAL ARG PRO VAL GLU ASP HIS ARG GLN VAL VAL GLU
SEQRES 4 A 230 VAL THR LEU GLY PHE THR LEU GLN ASP ILE VAL LYS ALA
SEQRES 5 A 230 ASP SER SER THR ASN GLU VAL ASP LEU VAL TYR TYR GLU
SEQRES 6 A 230 GLN GLN ARG TRP VAL ASP TYR ASN LEU LYS TRP ASN PRO
SEQRES 7 A 230 ASP ASP TYR GLY GLY VAL LYS LYS ILE HIS ILE PRO ALA
SEQRES 8 A 230 ALA ASP ILE TRP THR PRO ASP ILE THR ALA TYR SER SER
SEQRES 9 A 230 THR ARG PRO VAL GLN VAL LEU SER PRO GLN ILE ALA VAL
SEQRES 10 A 230 VAL THR HIS ASP GLY SER VAL MET PHE ILE PRO ALA GLN
SEQRES 11 A 230 ARG LEU SER PHE MET CYS ASP PRO THR GLY VAL ASP SER
SEQRES 12 A 230 GLU GLU GLY ALA THR CYS ALA VAL LYS PHE GLY SER TRP
SEQRES 13 A 230 VAL TYR SER GLY PHE GLU ILE ASP LEU LYS THR ASP THR
SEQRES 14 A 230 ASP GLN VAL ASP LEU SER SER TYR TYR ALA SER SER LYS
SEQRES 15 A 230 TYR GLU ILE LEU SER ALA THR GLN THR ARG GLN VAL GLN
SEQRES 16 A 230 HIS TYR SER CYS CYS PRO GLU PRO TYR ILE ASP VAL ASN
SEQRES 17 A 230 LEU VAL VAL LYS PHE ARG GLU ARG ARG ALA GLY ASN GLY
SEQRES 18 A 230 PHE PHE ARG ASN LEU PHE ASP SER ARG
SEQRES 1 B 230 ASP TYR LYS ASP ASP ASP ASP LYS LEU SER GLU HIS GLU
SEQRES 2 B 230 THR ARG LEU VAL ALA LYS LEU PHE LYS ASP TYR SER SER
SEQRES 3 B 230 VAL VAL ARG PRO VAL GLU ASP HIS ARG GLN VAL VAL GLU
SEQRES 4 B 230 VAL THR LEU GLY PHE THR LEU GLN ASP ILE VAL LYS ALA
SEQRES 5 B 230 ASP SER SER THR ASN GLU VAL ASP LEU VAL TYR TYR GLU
SEQRES 6 B 230 GLN GLN ARG TRP VAL ASP TYR ASN LEU LYS TRP ASN PRO
SEQRES 7 B 230 ASP ASP TYR GLY GLY VAL LYS LYS ILE HIS ILE PRO ALA
SEQRES 8 B 230 ALA ASP ILE TRP THR PRO ASP ILE THR ALA TYR SER SER
SEQRES 9 B 230 THR ARG PRO VAL GLN VAL LEU SER PRO GLN ILE ALA VAL
SEQRES 10 B 230 VAL THR HIS ASP GLY SER VAL MET PHE ILE PRO ALA GLN
SEQRES 11 B 230 ARG LEU SER PHE MET CYS ASP PRO THR GLY VAL ASP SER
SEQRES 12 B 230 GLU GLU GLY ALA THR CYS ALA VAL LYS PHE GLY SER TRP
SEQRES 13 B 230 VAL TYR SER GLY PHE GLU ILE ASP LEU LYS THR ASP THR
SEQRES 14 B 230 ASP GLN VAL ASP LEU SER SER TYR TYR ALA SER SER LYS
SEQRES 15 B 230 TYR GLU ILE LEU SER ALA THR GLN THR ARG GLN VAL GLN
SEQRES 16 B 230 HIS TYR SER CYS CYS PRO GLU PRO TYR ILE ASP VAL ASN
SEQRES 17 B 230 LEU VAL VAL LYS PHE ARG GLU ARG ARG ALA GLY ASN GLY
SEQRES 18 B 230 PHE PHE ARG ASN LEU PHE ASP SER ARG
SEQRES 1 C 230 ASP TYR LYS ASP ASP ASP ASP LYS LEU SER GLU HIS GLU
SEQRES 2 C 230 THR ARG LEU VAL ALA LYS LEU PHE LYS ASP TYR SER SER
SEQRES 3 C 230 VAL VAL ARG PRO VAL GLU ASP HIS ARG GLN VAL VAL GLU
SEQRES 4 C 230 VAL THR LEU GLY PHE THR LEU GLN ASP ILE VAL LYS ALA
SEQRES 5 C 230 ASP SER SER THR ASN GLU VAL ASP LEU VAL TYR TYR GLU
SEQRES 6 C 230 GLN GLN ARG TRP VAL ASP TYR ASN LEU LYS TRP ASN PRO
SEQRES 7 C 230 ASP ASP TYR GLY GLY VAL LYS LYS ILE HIS ILE PRO ALA
SEQRES 8 C 230 ALA ASP ILE TRP THR PRO ASP ILE THR ALA TYR SER SER
SEQRES 9 C 230 THR ARG PRO VAL GLN VAL LEU SER PRO GLN ILE ALA VAL
SEQRES 10 C 230 VAL THR HIS ASP GLY SER VAL MET PHE ILE PRO ALA GLN
SEQRES 11 C 230 ARG LEU SER PHE MET CYS ASP PRO THR GLY VAL ASP SER
SEQRES 12 C 230 GLU GLU GLY ALA THR CYS ALA VAL LYS PHE GLY SER TRP
SEQRES 13 C 230 VAL TYR SER GLY PHE GLU ILE ASP LEU LYS THR ASP THR
SEQRES 14 C 230 ASP GLN VAL ASP LEU SER SER TYR TYR ALA SER SER LYS
SEQRES 15 C 230 TYR GLU ILE LEU SER ALA THR GLN THR ARG GLN VAL GLN
SEQRES 16 C 230 HIS TYR SER CYS CYS PRO GLU PRO TYR ILE ASP VAL ASN
SEQRES 17 C 230 LEU VAL VAL LYS PHE ARG GLU ARG ARG ALA GLY ASN GLY
SEQRES 18 C 230 PHE PHE ARG ASN LEU PHE ASP SER ARG
SEQRES 1 D 230 ASP TYR LYS ASP ASP ASP ASP LYS LEU SER GLU HIS GLU
SEQRES 2 D 230 THR ARG LEU VAL ALA LYS LEU PHE LYS ASP TYR SER SER
SEQRES 3 D 230 VAL VAL ARG PRO VAL GLU ASP HIS ARG GLN VAL VAL GLU
SEQRES 4 D 230 VAL THR LEU GLY PHE THR LEU GLN ASP ILE VAL LYS ALA
SEQRES 5 D 230 ASP SER SER THR ASN GLU VAL ASP LEU VAL TYR TYR GLU
SEQRES 6 D 230 GLN GLN ARG TRP VAL ASP TYR ASN LEU LYS TRP ASN PRO
SEQRES 7 D 230 ASP ASP TYR GLY GLY VAL LYS LYS ILE HIS ILE PRO ALA
SEQRES 8 D 230 ALA ASP ILE TRP THR PRO ASP ILE THR ALA TYR SER SER
SEQRES 9 D 230 THR ARG PRO VAL GLN VAL LEU SER PRO GLN ILE ALA VAL
SEQRES 10 D 230 VAL THR HIS ASP GLY SER VAL MET PHE ILE PRO ALA GLN
SEQRES 11 D 230 ARG LEU SER PHE MET CYS ASP PRO THR GLY VAL ASP SER
SEQRES 12 D 230 GLU GLU GLY ALA THR CYS ALA VAL LYS PHE GLY SER TRP
SEQRES 13 D 230 VAL TYR SER GLY PHE GLU ILE ASP LEU LYS THR ASP THR
SEQRES 14 D 230 ASP GLN VAL ASP LEU SER SER TYR TYR ALA SER SER LYS
SEQRES 15 D 230 TYR GLU ILE LEU SER ALA THR GLN THR ARG GLN VAL GLN
SEQRES 16 D 230 HIS TYR SER CYS CYS PRO GLU PRO TYR ILE ASP VAL ASN
SEQRES 17 D 230 LEU VAL VAL LYS PHE ARG GLU ARG ARG ALA GLY ASN GLY
SEQRES 18 D 230 PHE PHE ARG ASN LEU PHE ASP SER ARG
SEQRES 1 E 230 ASP TYR LYS ASP ASP ASP ASP LYS LEU SER GLU HIS GLU
SEQRES 2 E 230 THR ARG LEU VAL ALA LYS LEU PHE LYS ASP TYR SER SER
SEQRES 3 E 230 VAL VAL ARG PRO VAL GLU ASP HIS ARG GLN VAL VAL GLU
SEQRES 4 E 230 VAL THR LEU GLY PHE THR LEU GLN ASP ILE VAL LYS ALA
SEQRES 5 E 230 ASP SER SER THR ASN GLU VAL ASP LEU VAL TYR TYR GLU
SEQRES 6 E 230 GLN GLN ARG TRP VAL ASP TYR ASN LEU LYS TRP ASN PRO
SEQRES 7 E 230 ASP ASP TYR GLY GLY VAL LYS LYS ILE HIS ILE PRO ALA
SEQRES 8 E 230 ALA ASP ILE TRP THR PRO ASP ILE THR ALA TYR SER SER
SEQRES 9 E 230 THR ARG PRO VAL GLN VAL LEU SER PRO GLN ILE ALA VAL
SEQRES 10 E 230 VAL THR HIS ASP GLY SER VAL MET PHE ILE PRO ALA GLN
SEQRES 11 E 230 ARG LEU SER PHE MET CYS ASP PRO THR GLY VAL ASP SER
SEQRES 12 E 230 GLU GLU GLY ALA THR CYS ALA VAL LYS PHE GLY SER TRP
SEQRES 13 E 230 VAL TYR SER GLY PHE GLU ILE ASP LEU LYS THR ASP THR
SEQRES 14 E 230 ASP GLN VAL ASP LEU SER SER TYR TYR ALA SER SER LYS
SEQRES 15 E 230 TYR GLU ILE LEU SER ALA THR GLN THR ARG GLN VAL GLN
SEQRES 16 E 230 HIS TYR SER CYS CYS PRO GLU PRO TYR ILE ASP VAL ASN
SEQRES 17 E 230 LEU VAL VAL LYS PHE ARG GLU ARG ARG ALA GLY ASN GLY
SEQRES 18 E 230 PHE PHE ARG ASN LEU PHE ASP SER ARG
HET 4P0 B 301 12
HET 4P0 D 301 12
HET 4P0 E 301 12
HETNAM 4P0 1-[(1R,6R)-9-AZABICYCLO[4.2.1]NON-2-EN-2-YL]ETHANONE
FORMUL 6 4P0 3(C10 H15 N O)
FORMUL 9 HOH *181(H2 O)
HELIX 1 AA1 GLU A 2 PHE A 12 1 11
HELIX 2 AA2 ASN A 68 GLY A 73 5 6
HELIX 3 AA3 ALA A 83 ILE A 85 5 3
HELIX 4 AA4 HIS B 3 LYS B 13 1 11
HELIX 5 AA5 ASN B 68 GLY B 73 5 6
HELIX 6 AA6 ALA B 83 ILE B 85 5 3
HELIX 7 AA7 HIS C 3 LYS C 13 1 11
HELIX 8 AA8 ASN C 68 GLY C 73 5 6
HELIX 9 AA9 ALA C 83 ILE C 85 5 3
HELIX 10 AB1 HIS D 3 LYS D 13 1 11
HELIX 11 AB2 ASN D 68 GLY D 73 5 6
HELIX 12 AB3 ALA D 83 ILE D 85 5 3
HELIX 13 AB4 HIS E 3 LYS E 13 1 11
HELIX 14 AB5 ASN E 68 GLY E 73 5 6
HELIX 15 AB6 ALA E 83 ILE E 85 5 3
SHEET 1 AA1 6 LYS A 77 PRO A 81 0
SHEET 2 AA1 6 ILE A 106 THR A 110 -1 O ALA A 107 N ILE A 80
SHEET 3 AA1 6 ASP A 112 PHE A 117 -1 O MET A 116 N VAL A 108
SHEET 4 AA1 6 GLU A 49 LYS A 66 -1 N TRP A 60 O VAL A 115
SHEET 5 AA1 6 ALA A 120 MET A 126 -1 O GLN A 121 N TYR A 54
SHEET 6 AA1 6 GLN A 100 VAL A 101 -1 N GLN A 100 O ARG A 122
SHEET 1 AA2 6 LYS A 77 PRO A 81 0
SHEET 2 AA2 6 ILE A 106 THR A 110 -1 O ALA A 107 N ILE A 80
SHEET 3 AA2 6 ASP A 112 PHE A 117 -1 O MET A 116 N VAL A 108
SHEET 4 AA2 6 GLU A 49 LYS A 66 -1 N TRP A 60 O VAL A 115
SHEET 5 AA2 6 VAL A 29 ASP A 44 -1 N ASP A 39 O VAL A 53
SHEET 6 AA2 6 ILE A 154 LYS A 157 1 O LYS A 157 N LEU A 33
SHEET 1 AA3 4 ILE A 90 ALA A 92 0
SHEET 2 AA3 4 ALA A 138 SER A 146 -1 O GLY A 145 N THR A 91
SHEET 3 AA3 4 TYR A 195 GLU A 206 -1 O PHE A 204 N ALA A 138
SHEET 4 AA3 4 TYR A 174 GLN A 186 -1 N GLN A 186 O TYR A 195
SHEET 1 AA4 6 LYS B 77 PRO B 81 0
SHEET 2 AA4 6 ILE B 106 THR B 110 -1 O ALA B 107 N ILE B 80
SHEET 3 AA4 6 ASP B 112 PHE B 117 -1 O MET B 116 N VAL B 108
SHEET 4 AA4 6 GLU B 49 LYS B 66 -1 N TRP B 60 O VAL B 115
SHEET 5 AA4 6 ALA B 120 MET B 126 -1 O LEU B 123 N LEU B 52
SHEET 6 AA4 6 GLN B 100 VAL B 101 -1 N GLN B 100 O ARG B 122
SHEET 1 AA5 6 LYS B 77 PRO B 81 0
SHEET 2 AA5 6 ILE B 106 THR B 110 -1 O ALA B 107 N ILE B 80
SHEET 3 AA5 6 ASP B 112 PHE B 117 -1 O MET B 116 N VAL B 108
SHEET 4 AA5 6 GLU B 49 LYS B 66 -1 N TRP B 60 O VAL B 115
SHEET 5 AA5 6 VAL B 29 ASP B 44 -1 N ASP B 39 O VAL B 53
SHEET 6 AA5 6 ILE B 154 LYS B 157 1 O LYS B 157 N LEU B 33
SHEET 1 AA6 4 ILE B 90 ALA B 92 0
SHEET 2 AA6 4 ALA B 138 SER B 146 -1 O GLY B 145 N THR B 91
SHEET 3 AA6 4 TYR B 195 GLU B 206 -1 O PHE B 204 N ALA B 138
SHEET 4 AA6 4 TYR B 174 GLN B 186 -1 N GLN B 186 O TYR B 195
SHEET 1 AA7 6 LYS C 77 PRO C 81 0
SHEET 2 AA7 6 ILE C 106 THR C 110 -1 O ALA C 107 N ILE C 80
SHEET 3 AA7 6 SER C 114 PHE C 117 -1 O MET C 116 N VAL C 108
SHEET 4 AA7 6 GLU C 49 VAL C 61 -1 N TRP C 60 O VAL C 115
SHEET 5 AA7 6 ALA C 120 MET C 126 -1 O GLN C 121 N TYR C 54
SHEET 6 AA7 6 GLN C 100 VAL C 101 -1 N GLN C 100 O ARG C 122
SHEET 1 AA8 6 LYS C 77 PRO C 81 0
SHEET 2 AA8 6 ILE C 106 THR C 110 -1 O ALA C 107 N ILE C 80
SHEET 3 AA8 6 SER C 114 PHE C 117 -1 O MET C 116 N VAL C 108
SHEET 4 AA8 6 GLU C 49 VAL C 61 -1 N TRP C 60 O VAL C 115
SHEET 5 AA8 6 VAL C 29 ASP C 44 -1 N ASP C 44 O GLU C 49
SHEET 6 AA8 6 ILE C 154 LYS C 157 1 O ASP C 155 N VAL C 31
SHEET 1 AA9 4 ILE C 90 ALA C 92 0
SHEET 2 AA9 4 ALA C 138 SER C 146 -1 O GLY C 145 N THR C 91
SHEET 3 AA9 4 TYR C 195 GLU C 206 -1 O LEU C 200 N VAL C 142
SHEET 4 AA9 4 TYR C 174 GLN C 186 -1 N LEU C 177 O LYS C 203
SHEET 1 AB1 6 LYS D 77 PRO D 81 0
SHEET 2 AB1 6 ILE D 106 THR D 110 -1 O ALA D 107 N ILE D 80
SHEET 3 AB1 6 ASP D 112 PHE D 117 -1 O MET D 116 N VAL D 108
SHEET 4 AB1 6 GLU D 49 LYS D 66 -1 N TRP D 60 O VAL D 115
SHEET 5 AB1 6 ALA D 120 MET D 126 -1 O GLN D 121 N TYR D 54
SHEET 6 AB1 6 GLN D 100 VAL D 101 -1 N GLN D 100 O ARG D 122
SHEET 1 AB2 6 LYS D 77 PRO D 81 0
SHEET 2 AB2 6 ILE D 106 THR D 110 -1 O ALA D 107 N ILE D 80
SHEET 3 AB2 6 ASP D 112 PHE D 117 -1 O MET D 116 N VAL D 108
SHEET 4 AB2 6 GLU D 49 LYS D 66 -1 N TRP D 60 O VAL D 115
SHEET 5 AB2 6 VAL D 29 ASP D 44 -1 N LYS D 42 O ASP D 51
SHEET 6 AB2 6 ILE D 154 LYS D 157 1 O ASP D 155 N VAL D 31
SHEET 1 AB3 4 ILE D 90 ALA D 92 0
SHEET 2 AB3 4 ALA D 138 SER D 146 -1 O GLY D 145 N THR D 91
SHEET 3 AB3 4 CYS D 191 GLU D 206 -1 O VAL D 202 N CYS D 140
SHEET 4 AB3 4 TYR D 174 TYR D 188 -1 N GLU D 175 O ARG D 205
SHEET 1 AB4 6 LYS E 77 PRO E 81 0
SHEET 2 AB4 6 ILE E 106 THR E 110 -1 O ALA E 107 N ILE E 80
SHEET 3 AB4 6 ASP E 112 PHE E 117 -1 O SER E 114 N THR E 110
SHEET 4 AB4 6 GLU E 49 LYS E 66 -1 N TRP E 60 O VAL E 115
SHEET 5 AB4 6 ALA E 120 MET E 126 -1 O LEU E 123 N LEU E 52
SHEET 6 AB4 6 GLN E 100 VAL E 101 -1 N GLN E 100 O ARG E 122
SHEET 1 AB5 6 LYS E 77 PRO E 81 0
SHEET 2 AB5 6 ILE E 106 THR E 110 -1 O ALA E 107 N ILE E 80
SHEET 3 AB5 6 ASP E 112 PHE E 117 -1 O SER E 114 N THR E 110
SHEET 4 AB5 6 GLU E 49 LYS E 66 -1 N TRP E 60 O VAL E 115
SHEET 5 AB5 6 VAL E 29 ASP E 44 -1 N ASP E 44 O GLU E 49
SHEET 6 AB5 6 ILE E 154 LYS E 157 1 O LYS E 157 N LEU E 33
SHEET 1 AB6 4 ILE E 90 ALA E 92 0
SHEET 2 AB6 4 ALA E 138 SER E 146 -1 O GLY E 145 N THR E 91
SHEET 3 AB6 4 CYS E 191 ARG E 205 -1 O LEU E 200 N VAL E 142
SHEET 4 AB6 4 GLU E 175 TYR E 188 -1 N GLN E 184 O ASP E 197
SSBOND 1 CYS A 127 CYS A 140 1555 1555 2.02
SSBOND 2 CYS A 190 CYS A 191 1555 1555 2.05
SSBOND 3 CYS B 127 CYS B 140 1555 1555 2.03
SSBOND 4 CYS B 190 CYS B 191 1555 1555 2.06
SSBOND 5 CYS C 127 CYS C 140 1555 1555 2.02
SSBOND 6 CYS C 190 CYS C 191 1555 1555 2.05
SSBOND 7 CYS D 127 CYS D 140 1555 1555 2.02
SSBOND 8 CYS D 190 CYS D 191 1555 1555 2.07
SSBOND 9 CYS E 127 CYS E 140 1555 1555 2.02
SSBOND 10 CYS E 190 CYS E 191 1555 1555 2.06
SITE 1 AC1 4 TYR B 93 TRP B 147 HOH B 426 ILE C 118
SITE 1 AC2 6 ILE A 118 HOH A 320 TYR D 93 TRP D 147
SITE 2 AC2 6 CYS D 190 TYR D 195
SITE 1 AC3 6 ILE B 118 TYR E 93 TRP E 147 CYS E 190
SITE 2 AC3 6 CYS E 191 HOH E 427
CRYST1 207.604 207.604 207.604 90.00 90.00 90.00 I 2 3 120
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 0.004817 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004817 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004817 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
