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HEADER UNKNOWN FUNCTION 16-FEB-23 8CKP
TITLE X-RAY STRUCTURE OF THE CRYSTALLIZATION-PRONE FORM OF SUBFAMILY III
TITLE 2 HALOALKANE DEHALOGENASE DHMEA FROM HALOFERAX MEDITERRANEI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA FOLD HYDROLASE;
COMPND 3 CHAIN: D, F, G, H, I, J, A, B, C, E;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HALOFERAX MEDITERRANEI;
SOURCE 3 ORGANISM_TAXID: 2252;
SOURCE 4 GENE: MHPC;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HALOALKANE DEHALOGENASE-LIKE, HYDROLASE, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR M.MAREK,K.CHMELOVA,A.SCHENKMAYEROVA,T.CROLL,R.J.READ,K.DIEDERICHS
REVDAT 1 30-AUG-23 8CKP 0
JRNL AUTH K.CHMELOVA,T.GAO,M.POLAK,A.SCHENKMAYEROVA,T.I.CROLL,
JRNL AUTH 2 T.R.SHAIKH,J.SKARUPOVA,R.CHALOUPKOVA,K.DIEDERICHS,R.J.READ,
JRNL AUTH 3 J.DAMBORSKY,J.NOVACEK,M.MAREK
JRNL TITL MULTIMERIC STRUCTURE OF A SUBFAMILY III HALOALKANE
JRNL TITL 2 DEHALOGENASE-LIKE ENZYME SOLVED BY COMBINATION OF CRYO-EM
JRNL TITL 3 AND X-RAY CRYSTALLOGRAPHY.
JRNL REF PROTEIN SCI. E4751 2023
JRNL REFN ESSN 1469-896X
JRNL PMID 37574754
JRNL DOI 10.1002/PRO.4751
REMARK 2
REMARK 2 RESOLUTION. 3.31 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20.1-4487
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.31
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.47
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 63073
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.238
REMARK 3 R VALUE (WORKING SET) : 0.236
REMARK 3 FREE R VALUE : 0.275
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3153
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 49.4700 - 9.3800 0.99 2767 146 0.2119 0.2146
REMARK 3 2 9.3800 - 7.4500 1.00 2690 141 0.1790 0.2116
REMARK 3 3 7.4500 - 6.5200 1.00 2641 139 0.2187 0.2805
REMARK 3 4 6.5100 - 5.9200 1.00 2647 140 0.2198 0.2401
REMARK 3 5 5.9200 - 5.5000 1.00 2640 139 0.2338 0.2943
REMARK 3 6 5.5000 - 5.1700 1.00 2616 137 0.2218 0.2489
REMARK 3 7 5.1700 - 4.9100 1.00 2635 139 0.1948 0.2385
REMARK 3 8 4.9100 - 4.7000 1.00 2604 137 0.2229 0.2818
REMARK 3 9 4.7000 - 4.5200 1.00 2616 138 0.2222 0.2882
REMARK 3 10 4.5200 - 4.3600 1.00 2604 137 0.2231 0.2912
REMARK 3 11 4.3600 - 4.2300 1.00 2583 136 0.2253 0.2621
REMARK 3 12 4.2300 - 4.1100 1.00 2586 136 0.2455 0.3091
REMARK 3 13 4.1100 - 4.0000 1.00 2620 138 0.2632 0.3631
REMARK 3 14 4.0000 - 3.9000 1.00 2579 136 0.3159 0.3826
REMARK 3 15 3.9000 - 3.8100 1.00 2611 137 0.3055 0.3637
REMARK 3 16 3.8100 - 3.7300 1.00 2556 135 0.2900 0.3462
REMARK 3 17 3.7300 - 3.6600 1.00 2583 136 0.3563 0.4523
REMARK 3 18 3.6600 - 3.5900 1.00 2602 137 0.3471 0.3804
REMARK 3 19 3.5900 - 3.5200 1.00 2585 136 0.3558 0.4396
REMARK 3 20 3.5200 - 3.4600 1.00 2602 137 0.4108 0.4379
REMARK 3 21 3.4600 - 3.4100 1.00 2590 136 0.4162 0.4490
REMARK 3 22 3.4100 - 3.3600 0.99 2569 136 0.4662 0.5327
REMARK 3 23 3.3600 - 3.3100 0.93 2394 124 0.5441 0.5028
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) : 0.697
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 36.191
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 151.6
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 155.0
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 : 0.003 24550
REMARK 3 ANGLE : 0.692 33342
REMARK 3 CHIRALITY : 0.045 3439
REMARK 3 PLANARITY : 0.012 4420
REMARK 3 DIHEDRAL : 13.288 8833
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 8CKP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-FEB-23.
REMARK 100 THE DEPOSITION ID IS D_1292128694.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-MAY-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9999
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63328
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.306
REMARK 200 RESOLUTION RANGE LOW (A) : 49.470
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 70.30
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.7600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.31
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.42
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, MES/IMIDAZOLE BUFFER SYSTEM,
REMARK 280 AMINO ACIDS, PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 84.15500
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 84.15500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 86.38000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 144.95000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 86.38000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 144.95000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 84.15500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 86.38000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 144.95000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 84.15500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 86.38000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 144.95000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DECAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, F, G, H, I, J, A, B, C, 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 MET D 1
REMARK 465 SER D 2
REMARK 465 SER D 3
REMARK 465 ALA D 4
REMARK 465 SER D 5
REMARK 465 HIS D 308
REMARK 465 HIS D 309
REMARK 465 HIS D 310
REMARK 465 HIS D 311
REMARK 465 MET F 1
REMARK 465 ARG F 181
REMARK 465 TYR F 182
REMARK 465 ASP F 183
REMARK 465 LEU F 184
REMARK 465 PHE F 185
REMARK 465 THR F 186
REMARK 465 ARG F 187
REMARK 465 VAL F 188
REMARK 465 ILE F 189
REMARK 465 MET F 190
REMARK 465 PRO F 191
REMARK 465 MET F 192
REMARK 465 GLY F 193
REMARK 465 PHE F 194
REMARK 465 ALA F 195
REMARK 465 HIS F 309
REMARK 465 HIS F 310
REMARK 465 HIS F 311
REMARK 465 MET G 1
REMARK 465 SER G 2
REMARK 465 SER G 3
REMARK 465 ALA G 4
REMARK 465 SER G 5
REMARK 465 SER G 6
REMARK 465 ASN G 7
REMARK 465 ALA G 8
REMARK 465 HIS G 309
REMARK 465 HIS G 310
REMARK 465 HIS G 311
REMARK 465 MET H 1
REMARK 465 SER H 2
REMARK 465 SER H 3
REMARK 465 ALA H 4
REMARK 465 ARG H 181
REMARK 465 TYR H 182
REMARK 465 ASP H 183
REMARK 465 LEU H 184
REMARK 465 PHE H 185
REMARK 465 THR H 186
REMARK 465 ARG H 187
REMARK 465 VAL H 188
REMARK 465 ILE H 189
REMARK 465 MET H 190
REMARK 465 PRO H 191
REMARK 465 MET H 192
REMARK 465 GLY H 193
REMARK 465 HIS H 309
REMARK 465 HIS H 310
REMARK 465 HIS H 311
REMARK 465 MET I 1
REMARK 465 SER I 2
REMARK 465 SER I 3
REMARK 465 ALA I 4
REMARK 465 SER I 5
REMARK 465 SER I 6
REMARK 465 ASN I 7
REMARK 465 HIS I 308
REMARK 465 HIS I 309
REMARK 465 HIS I 310
REMARK 465 HIS I 311
REMARK 465 MET J 1
REMARK 465 SER J 2
REMARK 465 SER J 3
REMARK 465 ALA J 4
REMARK 465 SER J 5
REMARK 465 SER J 6
REMARK 465 ASN J 7
REMARK 465 ARG J 181
REMARK 465 TYR J 182
REMARK 465 ASP J 183
REMARK 465 LEU J 184
REMARK 465 PHE J 185
REMARK 465 THR J 186
REMARK 465 ARG J 187
REMARK 465 VAL J 188
REMARK 465 ILE J 189
REMARK 465 MET J 190
REMARK 465 PRO J 191
REMARK 465 MET J 192
REMARK 465 GLY J 193
REMARK 465 PHE J 194
REMARK 465 ALA J 195
REMARK 465 ASP J 196
REMARK 465 HIS J 310
REMARK 465 HIS J 311
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 SER A 3
REMARK 465 ALA A 4
REMARK 465 GLU A 180
REMARK 465 ARG A 181
REMARK 465 TYR A 182
REMARK 465 ASP A 183
REMARK 465 LEU A 184
REMARK 465 PHE A 185
REMARK 465 THR A 186
REMARK 465 ARG A 187
REMARK 465 VAL A 188
REMARK 465 ILE A 189
REMARK 465 MET A 190
REMARK 465 PRO A 191
REMARK 465 MET A 192
REMARK 465 GLY A 193
REMARK 465 PHE A 194
REMARK 465 ALA A 195
REMARK 465 ASP A 196
REMARK 465 ARG A 197
REMARK 465 HIS A 310
REMARK 465 HIS A 311
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 SER B 3
REMARK 465 ALA B 4
REMARK 465 SER B 5
REMARK 465 ARG B 181
REMARK 465 TYR B 182
REMARK 465 ASP B 183
REMARK 465 LEU B 184
REMARK 465 PHE B 185
REMARK 465 THR B 186
REMARK 465 ARG B 187
REMARK 465 VAL B 188
REMARK 465 ILE B 189
REMARK 465 MET B 190
REMARK 465 PRO B 191
REMARK 465 MET B 192
REMARK 465 GLY B 193
REMARK 465 PHE B 194
REMARK 465 ALA B 195
REMARK 465 ASP B 196
REMARK 465 HIS B 310
REMARK 465 HIS B 311
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 SER C 3
REMARK 465 ALA C 4
REMARK 465 HIS C 310
REMARK 465 HIS C 311
REMARK 465 MET E 1
REMARK 465 SER E 2
REMARK 465 SER E 3
REMARK 465 ALA E 4
REMARK 465 SER E 5
REMARK 465 HIS E 309
REMARK 465 HIS E 310
REMARK 465 HIS E 311
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 ARG D 197 CG CD NE CZ NH1 NH2
REMARK 470 ARG F 197 CG CD NE CZ NH1 NH2
REMARK 470 ARG G 197 CG CD NE CZ NH1 NH2
REMARK 470 ARG H 197 CG CD NE CZ NH1 NH2
REMARK 470 ARG I 197 CG CD NE CZ NH1 NH2
REMARK 470 ARG J 197 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 197 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 197 CG CD NE CZ NH1 NH2
REMARK 470 ARG E 197 CG CD NE CZ NH1 NH2
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 THR D 65 -178.21 -68.14
REMARK 500 GLU D 80 -21.43 -141.33
REMARK 500 ARG D 96 76.62 -104.10
REMARK 500 ASP D 129 -130.35 50.54
REMARK 500 HIS D 142 52.24 -118.69
REMARK 500 MET D 156 49.46 -146.49
REMARK 500 VAL D 188 -48.36 -134.43
REMARK 500 ARG F 25 0.30 -67.41
REMARK 500 TYR F 28 62.61 -118.71
REMARK 500 ARG F 78 -4.97 -59.38
REMARK 500 ARG F 96 72.66 -109.99
REMARK 500 TYR F 102 19.39 53.18
REMARK 500 ASP F 129 -131.03 53.49
REMARK 500 ASN F 153 72.84 33.87
REMARK 500 MET F 156 41.58 -148.46
REMARK 500 ARG F 176 99.14 -68.23
REMARK 500 ARG F 216 2.95 -65.46
REMARK 500 TYR G 28 64.59 -117.36
REMARK 500 ARG G 96 72.94 -111.19
REMARK 500 ASP G 129 -130.20 53.09
REMARK 500 ASN G 153 74.74 32.43
REMARK 500 MET G 156 44.37 -149.11
REMARK 500 VAL G 188 -50.74 -135.99
REMARK 500 ASN G 212 44.81 -83.70
REMARK 500 GLU H 19 18.44 -148.43
REMARK 500 TYR H 28 64.67 -114.37
REMARK 500 ARG H 96 71.91 -117.05
REMARK 500 TYR H 102 17.31 56.50
REMARK 500 ASP H 129 -127.93 52.03
REMARK 500 ASN H 153 70.77 35.14
REMARK 500 MET H 156 43.79 -145.82
REMARK 500 GLU I 18 0.87 -65.09
REMARK 500 ALA I 20 44.96 -102.64
REMARK 500 TYR I 28 62.27 -116.15
REMARK 500 ARG I 96 72.92 -114.14
REMARK 500 TYR I 102 18.04 56.81
REMARK 500 ASP I 129 -127.85 51.38
REMARK 500 SER I 137 10.00 -67.01
REMARK 500 ASN I 153 69.62 31.28
REMARK 500 MET I 156 39.28 -150.83
REMARK 500 ALA J 20 41.70 -78.20
REMARK 500 TYR J 28 61.55 -116.94
REMARK 500 PRO J 64 34.03 -99.66
REMARK 500 ARG J 96 72.21 -116.69
REMARK 500 TYR J 102 18.86 54.49
REMARK 500 ASP J 129 -128.45 52.81
REMARK 500 ASN J 153 74.74 29.96
REMARK 500 MET J 156 45.12 -151.98
REMARK 500 GLU A 19 -31.07 -131.86
REMARK 500 ALA A 20 7.90 -68.58
REMARK 500
REMARK 500 THIS ENTRY HAS 85 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASP G 21 TRP G 22 149.54
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG I 103 0.09 SIDE CHAIN
REMARK 500 ARG B 176 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 8CKP D 1 305 UNP I3R766 I3R766_HALMT 1 307
DBREF 8CKP F 1 305 UNP I3R766 I3R766_HALMT 1 307
DBREF 8CKP G 1 305 UNP I3R766 I3R766_HALMT 1 307
DBREF 8CKP H 1 305 UNP I3R766 I3R766_HALMT 1 307
DBREF 8CKP I 1 305 UNP I3R766 I3R766_HALMT 1 307
DBREF 8CKP J 1 305 UNP I3R766 I3R766_HALMT 1 307
DBREF 8CKP A 1 305 UNP I3R766 I3R766_HALMT 1 307
DBREF 8CKP B 1 305 UNP I3R766 I3R766_HALMT 1 307
DBREF 8CKP C 1 305 UNP I3R766 I3R766_HALMT 1 307
DBREF 8CKP E 1 305 UNP I3R766 I3R766_HALMT 1 307
SEQADV 8CKP D UNP I3R766 GLY 173 DELETION
SEQADV 8CKP D UNP I3R766 GLY 174 DELETION
SEQADV 8CKP HIS D 306 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS D 307 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS D 308 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS D 309 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS D 310 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS D 311 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP F UNP I3R766 GLY 173 DELETION
SEQADV 8CKP F UNP I3R766 GLY 174 DELETION
SEQADV 8CKP HIS F 306 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS F 307 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS F 308 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS F 309 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS F 310 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS F 311 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP G UNP I3R766 GLY 173 DELETION
SEQADV 8CKP G UNP I3R766 GLY 174 DELETION
SEQADV 8CKP HIS G 306 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS G 307 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS G 308 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS G 309 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS G 310 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS G 311 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP H UNP I3R766 GLY 173 DELETION
SEQADV 8CKP H UNP I3R766 GLY 174 DELETION
SEQADV 8CKP HIS H 306 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS H 307 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS H 308 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS H 309 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS H 310 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS H 311 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP I UNP I3R766 GLY 173 DELETION
SEQADV 8CKP I UNP I3R766 GLY 174 DELETION
SEQADV 8CKP HIS I 306 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS I 307 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS I 308 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS I 309 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS I 310 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS I 311 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP J UNP I3R766 GLY 173 DELETION
SEQADV 8CKP J UNP I3R766 GLY 174 DELETION
SEQADV 8CKP HIS J 306 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS J 307 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS J 308 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS J 309 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS J 310 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS J 311 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP A UNP I3R766 GLY 173 DELETION
SEQADV 8CKP A UNP I3R766 GLY 174 DELETION
SEQADV 8CKP HIS A 306 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS A 307 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS A 308 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS A 309 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS A 310 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS A 311 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP B UNP I3R766 GLY 173 DELETION
SEQADV 8CKP B UNP I3R766 GLY 174 DELETION
SEQADV 8CKP HIS B 306 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS B 307 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS B 308 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS B 309 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS B 310 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS B 311 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP C UNP I3R766 GLY 173 DELETION
SEQADV 8CKP C UNP I3R766 GLY 174 DELETION
SEQADV 8CKP HIS C 306 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS C 307 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS C 308 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS C 309 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS C 310 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS C 311 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP E UNP I3R766 GLY 173 DELETION
SEQADV 8CKP E UNP I3R766 GLY 174 DELETION
SEQADV 8CKP HIS E 306 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS E 307 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS E 308 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS E 309 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS E 310 UNP I3R766 EXPRESSION TAG
SEQADV 8CKP HIS E 311 UNP I3R766 EXPRESSION TAG
SEQRES 1 D 311 MET SER SER ALA SER SER ASN ALA ARG ASP GLU VAL ILE
SEQRES 2 D 311 ALA ALA ILE HIS GLU GLU ALA ASP TRP VAL ASP ARG THR
SEQRES 3 D 311 VAL TYR PRO PHE GLU SER ARG CYS ILE GLY LEU SER SER
SEQRES 4 D 311 GLY ALA VAL HIS TYR ILE ASP GLU GLY PRO ASP ASP GLY
SEQRES 5 D 311 GLY ARG GLU THR LEU LEU MET LEU HIS GLY ASN PRO THR
SEQRES 6 D 311 TRP SER PHE LEU TYR ARG HIS LEU VAL ARG ASP LEU ARG
SEQRES 7 D 311 ASP GLU TYR ARG CYS VAL ALA LEU ASP TYR LEU GLY PHE
SEQRES 8 D 311 GLY LEU SER GLU ARG PRO THR ASP PHE SER TYR ARG PRO
SEQRES 9 D 311 GLU ASP HIS ALA ASP VAL VAL GLU GLU PHE ILE ASP GLU
SEQRES 10 D 311 LEU GLY LEU GLU ASP VAL VAL LEU VAL GLY HIS ASP TRP
SEQRES 11 D 311 GLY GLY PRO ILE GLY PHE SER TYR ALA ILE ASP HIS PRO
SEQRES 12 D 311 GLU ASN VAL GLY GLY LEU VAL VAL MET ASN THR TRP MET
SEQRES 13 D 311 TRP PRO VAL SER ASP ASP LYS HIS PHE SER ARG PHE SER
SEQRES 14 D 311 LYS LEU LEU ARG ILE GLY ARG GLU LEU CYS GLU ARG TYR
SEQRES 15 D 311 ASP LEU PHE THR ARG VAL ILE MET PRO MET GLY PHE ALA
SEQRES 16 D 311 ASP ARG SER ARG PHE THR GLU SER ALA ARG GLU GLN TYR
SEQRES 17 D 311 ARG ALA ALA ASN ARG GLY ASP ARG THR GLY THR GLY ILE
SEQRES 18 D 311 PHE PRO GLN ALA ILE LEU GLY SER ARG ALA TRP LEU SER
SEQRES 19 D 311 SER LEU TRP GLU GLN ARG ASP ASN ILE ALA ASP ILE PRO
SEQRES 20 D 311 ALA ARG ILE ILE TRP GLY MET GLU ASP SER ALA PHE ARG
SEQRES 21 D 311 PRO ALA GLU LEU ARG THR PHE GLU ALA LEU PHE GLU ASP
SEQRES 22 D 311 SER SER THR VAL ARG LEU TYR GLY VAL GLY HIS TYR VAL
SEQRES 23 D 311 PRO GLU GLU PHE GLY SER ASP LEU VAL PRO LEU VAL ARG
SEQRES 24 D 311 GLU PHE LEU GLU GLU VAL HIS HIS HIS HIS HIS HIS
SEQRES 1 F 311 MET SER SER ALA SER SER ASN ALA ARG ASP GLU VAL ILE
SEQRES 2 F 311 ALA ALA ILE HIS GLU GLU ALA ASP TRP VAL ASP ARG THR
SEQRES 3 F 311 VAL TYR PRO PHE GLU SER ARG CYS ILE GLY LEU SER SER
SEQRES 4 F 311 GLY ALA VAL HIS TYR ILE ASP GLU GLY PRO ASP ASP GLY
SEQRES 5 F 311 GLY ARG GLU THR LEU LEU MET LEU HIS GLY ASN PRO THR
SEQRES 6 F 311 TRP SER PHE LEU TYR ARG HIS LEU VAL ARG ASP LEU ARG
SEQRES 7 F 311 ASP GLU TYR ARG CYS VAL ALA LEU ASP TYR LEU GLY PHE
SEQRES 8 F 311 GLY LEU SER GLU ARG PRO THR ASP PHE SER TYR ARG PRO
SEQRES 9 F 311 GLU ASP HIS ALA ASP VAL VAL GLU GLU PHE ILE ASP GLU
SEQRES 10 F 311 LEU GLY LEU GLU ASP VAL VAL LEU VAL GLY HIS ASP TRP
SEQRES 11 F 311 GLY GLY PRO ILE GLY PHE SER TYR ALA ILE ASP HIS PRO
SEQRES 12 F 311 GLU ASN VAL GLY GLY LEU VAL VAL MET ASN THR TRP MET
SEQRES 13 F 311 TRP PRO VAL SER ASP ASP LYS HIS PHE SER ARG PHE SER
SEQRES 14 F 311 LYS LEU LEU ARG ILE GLY ARG GLU LEU CYS GLU ARG TYR
SEQRES 15 F 311 ASP LEU PHE THR ARG VAL ILE MET PRO MET GLY PHE ALA
SEQRES 16 F 311 ASP ARG SER ARG PHE THR GLU SER ALA ARG GLU GLN TYR
SEQRES 17 F 311 ARG ALA ALA ASN ARG GLY ASP ARG THR GLY THR GLY ILE
SEQRES 18 F 311 PHE PRO GLN ALA ILE LEU GLY SER ARG ALA TRP LEU SER
SEQRES 19 F 311 SER LEU TRP GLU GLN ARG ASP ASN ILE ALA ASP ILE PRO
SEQRES 20 F 311 ALA ARG ILE ILE TRP GLY MET GLU ASP SER ALA PHE ARG
SEQRES 21 F 311 PRO ALA GLU LEU ARG THR PHE GLU ALA LEU PHE GLU ASP
SEQRES 22 F 311 SER SER THR VAL ARG LEU TYR GLY VAL GLY HIS TYR VAL
SEQRES 23 F 311 PRO GLU GLU PHE GLY SER ASP LEU VAL PRO LEU VAL ARG
SEQRES 24 F 311 GLU PHE LEU GLU GLU VAL HIS HIS HIS HIS HIS HIS
SEQRES 1 G 311 MET SER SER ALA SER SER ASN ALA ARG ASP GLU VAL ILE
SEQRES 2 G 311 ALA ALA ILE HIS GLU GLU ALA ASP TRP VAL ASP ARG THR
SEQRES 3 G 311 VAL TYR PRO PHE GLU SER ARG CYS ILE GLY LEU SER SER
SEQRES 4 G 311 GLY ALA VAL HIS TYR ILE ASP GLU GLY PRO ASP ASP GLY
SEQRES 5 G 311 GLY ARG GLU THR LEU LEU MET LEU HIS GLY ASN PRO THR
SEQRES 6 G 311 TRP SER PHE LEU TYR ARG HIS LEU VAL ARG ASP LEU ARG
SEQRES 7 G 311 ASP GLU TYR ARG CYS VAL ALA LEU ASP TYR LEU GLY PHE
SEQRES 8 G 311 GLY LEU SER GLU ARG PRO THR ASP PHE SER TYR ARG PRO
SEQRES 9 G 311 GLU ASP HIS ALA ASP VAL VAL GLU GLU PHE ILE ASP GLU
SEQRES 10 G 311 LEU GLY LEU GLU ASP VAL VAL LEU VAL GLY HIS ASP TRP
SEQRES 11 G 311 GLY GLY PRO ILE GLY PHE SER TYR ALA ILE ASP HIS PRO
SEQRES 12 G 311 GLU ASN VAL GLY GLY LEU VAL VAL MET ASN THR TRP MET
SEQRES 13 G 311 TRP PRO VAL SER ASP ASP LYS HIS PHE SER ARG PHE SER
SEQRES 14 G 311 LYS LEU LEU ARG ILE GLY ARG GLU LEU CYS GLU ARG TYR
SEQRES 15 G 311 ASP LEU PHE THR ARG VAL ILE MET PRO MET GLY PHE ALA
SEQRES 16 G 311 ASP ARG SER ARG PHE THR GLU SER ALA ARG GLU GLN TYR
SEQRES 17 G 311 ARG ALA ALA ASN ARG GLY ASP ARG THR GLY THR GLY ILE
SEQRES 18 G 311 PHE PRO GLN ALA ILE LEU GLY SER ARG ALA TRP LEU SER
SEQRES 19 G 311 SER LEU TRP GLU GLN ARG ASP ASN ILE ALA ASP ILE PRO
SEQRES 20 G 311 ALA ARG ILE ILE TRP GLY MET GLU ASP SER ALA PHE ARG
SEQRES 21 G 311 PRO ALA GLU LEU ARG THR PHE GLU ALA LEU PHE GLU ASP
SEQRES 22 G 311 SER SER THR VAL ARG LEU TYR GLY VAL GLY HIS TYR VAL
SEQRES 23 G 311 PRO GLU GLU PHE GLY SER ASP LEU VAL PRO LEU VAL ARG
SEQRES 24 G 311 GLU PHE LEU GLU GLU VAL HIS HIS HIS HIS HIS HIS
SEQRES 1 H 311 MET SER SER ALA SER SER ASN ALA ARG ASP GLU VAL ILE
SEQRES 2 H 311 ALA ALA ILE HIS GLU GLU ALA ASP TRP VAL ASP ARG THR
SEQRES 3 H 311 VAL TYR PRO PHE GLU SER ARG CYS ILE GLY LEU SER SER
SEQRES 4 H 311 GLY ALA VAL HIS TYR ILE ASP GLU GLY PRO ASP ASP GLY
SEQRES 5 H 311 GLY ARG GLU THR LEU LEU MET LEU HIS GLY ASN PRO THR
SEQRES 6 H 311 TRP SER PHE LEU TYR ARG HIS LEU VAL ARG ASP LEU ARG
SEQRES 7 H 311 ASP GLU TYR ARG CYS VAL ALA LEU ASP TYR LEU GLY PHE
SEQRES 8 H 311 GLY LEU SER GLU ARG PRO THR ASP PHE SER TYR ARG PRO
SEQRES 9 H 311 GLU ASP HIS ALA ASP VAL VAL GLU GLU PHE ILE ASP GLU
SEQRES 10 H 311 LEU GLY LEU GLU ASP VAL VAL LEU VAL GLY HIS ASP TRP
SEQRES 11 H 311 GLY GLY PRO ILE GLY PHE SER TYR ALA ILE ASP HIS PRO
SEQRES 12 H 311 GLU ASN VAL GLY GLY LEU VAL VAL MET ASN THR TRP MET
SEQRES 13 H 311 TRP PRO VAL SER ASP ASP LYS HIS PHE SER ARG PHE SER
SEQRES 14 H 311 LYS LEU LEU ARG ILE GLY ARG GLU LEU CYS GLU ARG TYR
SEQRES 15 H 311 ASP LEU PHE THR ARG VAL ILE MET PRO MET GLY PHE ALA
SEQRES 16 H 311 ASP ARG SER ARG PHE THR GLU SER ALA ARG GLU GLN TYR
SEQRES 17 H 311 ARG ALA ALA ASN ARG GLY ASP ARG THR GLY THR GLY ILE
SEQRES 18 H 311 PHE PRO GLN ALA ILE LEU GLY SER ARG ALA TRP LEU SER
SEQRES 19 H 311 SER LEU TRP GLU GLN ARG ASP ASN ILE ALA ASP ILE PRO
SEQRES 20 H 311 ALA ARG ILE ILE TRP GLY MET GLU ASP SER ALA PHE ARG
SEQRES 21 H 311 PRO ALA GLU LEU ARG THR PHE GLU ALA LEU PHE GLU ASP
SEQRES 22 H 311 SER SER THR VAL ARG LEU TYR GLY VAL GLY HIS TYR VAL
SEQRES 23 H 311 PRO GLU GLU PHE GLY SER ASP LEU VAL PRO LEU VAL ARG
SEQRES 24 H 311 GLU PHE LEU GLU GLU VAL HIS HIS HIS HIS HIS HIS
SEQRES 1 I 311 MET SER SER ALA SER SER ASN ALA ARG ASP GLU VAL ILE
SEQRES 2 I 311 ALA ALA ILE HIS GLU GLU ALA ASP TRP VAL ASP ARG THR
SEQRES 3 I 311 VAL TYR PRO PHE GLU SER ARG CYS ILE GLY LEU SER SER
SEQRES 4 I 311 GLY ALA VAL HIS TYR ILE ASP GLU GLY PRO ASP ASP GLY
SEQRES 5 I 311 GLY ARG GLU THR LEU LEU MET LEU HIS GLY ASN PRO THR
SEQRES 6 I 311 TRP SER PHE LEU TYR ARG HIS LEU VAL ARG ASP LEU ARG
SEQRES 7 I 311 ASP GLU TYR ARG CYS VAL ALA LEU ASP TYR LEU GLY PHE
SEQRES 8 I 311 GLY LEU SER GLU ARG PRO THR ASP PHE SER TYR ARG PRO
SEQRES 9 I 311 GLU ASP HIS ALA ASP VAL VAL GLU GLU PHE ILE ASP GLU
SEQRES 10 I 311 LEU GLY LEU GLU ASP VAL VAL LEU VAL GLY HIS ASP TRP
SEQRES 11 I 311 GLY GLY PRO ILE GLY PHE SER TYR ALA ILE ASP HIS PRO
SEQRES 12 I 311 GLU ASN VAL GLY GLY LEU VAL VAL MET ASN THR TRP MET
SEQRES 13 I 311 TRP PRO VAL SER ASP ASP LYS HIS PHE SER ARG PHE SER
SEQRES 14 I 311 LYS LEU LEU ARG ILE GLY ARG GLU LEU CYS GLU ARG TYR
SEQRES 15 I 311 ASP LEU PHE THR ARG VAL ILE MET PRO MET GLY PHE ALA
SEQRES 16 I 311 ASP ARG SER ARG PHE THR GLU SER ALA ARG GLU GLN TYR
SEQRES 17 I 311 ARG ALA ALA ASN ARG GLY ASP ARG THR GLY THR GLY ILE
SEQRES 18 I 311 PHE PRO GLN ALA ILE LEU GLY SER ARG ALA TRP LEU SER
SEQRES 19 I 311 SER LEU TRP GLU GLN ARG ASP ASN ILE ALA ASP ILE PRO
SEQRES 20 I 311 ALA ARG ILE ILE TRP GLY MET GLU ASP SER ALA PHE ARG
SEQRES 21 I 311 PRO ALA GLU LEU ARG THR PHE GLU ALA LEU PHE GLU ASP
SEQRES 22 I 311 SER SER THR VAL ARG LEU TYR GLY VAL GLY HIS TYR VAL
SEQRES 23 I 311 PRO GLU GLU PHE GLY SER ASP LEU VAL PRO LEU VAL ARG
SEQRES 24 I 311 GLU PHE LEU GLU GLU VAL HIS HIS HIS HIS HIS HIS
SEQRES 1 J 311 MET SER SER ALA SER SER ASN ALA ARG ASP GLU VAL ILE
SEQRES 2 J 311 ALA ALA ILE HIS GLU GLU ALA ASP TRP VAL ASP ARG THR
SEQRES 3 J 311 VAL TYR PRO PHE GLU SER ARG CYS ILE GLY LEU SER SER
SEQRES 4 J 311 GLY ALA VAL HIS TYR ILE ASP GLU GLY PRO ASP ASP GLY
SEQRES 5 J 311 GLY ARG GLU THR LEU LEU MET LEU HIS GLY ASN PRO THR
SEQRES 6 J 311 TRP SER PHE LEU TYR ARG HIS LEU VAL ARG ASP LEU ARG
SEQRES 7 J 311 ASP GLU TYR ARG CYS VAL ALA LEU ASP TYR LEU GLY PHE
SEQRES 8 J 311 GLY LEU SER GLU ARG PRO THR ASP PHE SER TYR ARG PRO
SEQRES 9 J 311 GLU ASP HIS ALA ASP VAL VAL GLU GLU PHE ILE ASP GLU
SEQRES 10 J 311 LEU GLY LEU GLU ASP VAL VAL LEU VAL GLY HIS ASP TRP
SEQRES 11 J 311 GLY GLY PRO ILE GLY PHE SER TYR ALA ILE ASP HIS PRO
SEQRES 12 J 311 GLU ASN VAL GLY GLY LEU VAL VAL MET ASN THR TRP MET
SEQRES 13 J 311 TRP PRO VAL SER ASP ASP LYS HIS PHE SER ARG PHE SER
SEQRES 14 J 311 LYS LEU LEU ARG ILE GLY ARG GLU LEU CYS GLU ARG TYR
SEQRES 15 J 311 ASP LEU PHE THR ARG VAL ILE MET PRO MET GLY PHE ALA
SEQRES 16 J 311 ASP ARG SER ARG PHE THR GLU SER ALA ARG GLU GLN TYR
SEQRES 17 J 311 ARG ALA ALA ASN ARG GLY ASP ARG THR GLY THR GLY ILE
SEQRES 18 J 311 PHE PRO GLN ALA ILE LEU GLY SER ARG ALA TRP LEU SER
SEQRES 19 J 311 SER LEU TRP GLU GLN ARG ASP ASN ILE ALA ASP ILE PRO
SEQRES 20 J 311 ALA ARG ILE ILE TRP GLY MET GLU ASP SER ALA PHE ARG
SEQRES 21 J 311 PRO ALA GLU LEU ARG THR PHE GLU ALA LEU PHE GLU ASP
SEQRES 22 J 311 SER SER THR VAL ARG LEU TYR GLY VAL GLY HIS TYR VAL
SEQRES 23 J 311 PRO GLU GLU PHE GLY SER ASP LEU VAL PRO LEU VAL ARG
SEQRES 24 J 311 GLU PHE LEU GLU GLU VAL HIS HIS HIS HIS HIS HIS
SEQRES 1 A 311 MET SER SER ALA SER SER ASN ALA ARG ASP GLU VAL ILE
SEQRES 2 A 311 ALA ALA ILE HIS GLU GLU ALA ASP TRP VAL ASP ARG THR
SEQRES 3 A 311 VAL TYR PRO PHE GLU SER ARG CYS ILE GLY LEU SER SER
SEQRES 4 A 311 GLY ALA VAL HIS TYR ILE ASP GLU GLY PRO ASP ASP GLY
SEQRES 5 A 311 GLY ARG GLU THR LEU LEU MET LEU HIS GLY ASN PRO THR
SEQRES 6 A 311 TRP SER PHE LEU TYR ARG HIS LEU VAL ARG ASP LEU ARG
SEQRES 7 A 311 ASP GLU TYR ARG CYS VAL ALA LEU ASP TYR LEU GLY PHE
SEQRES 8 A 311 GLY LEU SER GLU ARG PRO THR ASP PHE SER TYR ARG PRO
SEQRES 9 A 311 GLU ASP HIS ALA ASP VAL VAL GLU GLU PHE ILE ASP GLU
SEQRES 10 A 311 LEU GLY LEU GLU ASP VAL VAL LEU VAL GLY HIS ASP TRP
SEQRES 11 A 311 GLY GLY PRO ILE GLY PHE SER TYR ALA ILE ASP HIS PRO
SEQRES 12 A 311 GLU ASN VAL GLY GLY LEU VAL VAL MET ASN THR TRP MET
SEQRES 13 A 311 TRP PRO VAL SER ASP ASP LYS HIS PHE SER ARG PHE SER
SEQRES 14 A 311 LYS LEU LEU ARG ILE GLY ARG GLU LEU CYS GLU ARG TYR
SEQRES 15 A 311 ASP LEU PHE THR ARG VAL ILE MET PRO MET GLY PHE ALA
SEQRES 16 A 311 ASP ARG SER ARG PHE THR GLU SER ALA ARG GLU GLN TYR
SEQRES 17 A 311 ARG ALA ALA ASN ARG GLY ASP ARG THR GLY THR GLY ILE
SEQRES 18 A 311 PHE PRO GLN ALA ILE LEU GLY SER ARG ALA TRP LEU SER
SEQRES 19 A 311 SER LEU TRP GLU GLN ARG ASP ASN ILE ALA ASP ILE PRO
SEQRES 20 A 311 ALA ARG ILE ILE TRP GLY MET GLU ASP SER ALA PHE ARG
SEQRES 21 A 311 PRO ALA GLU LEU ARG THR PHE GLU ALA LEU PHE GLU ASP
SEQRES 22 A 311 SER SER THR VAL ARG LEU TYR GLY VAL GLY HIS TYR VAL
SEQRES 23 A 311 PRO GLU GLU PHE GLY SER ASP LEU VAL PRO LEU VAL ARG
SEQRES 24 A 311 GLU PHE LEU GLU GLU VAL HIS HIS HIS HIS HIS HIS
SEQRES 1 B 311 MET SER SER ALA SER SER ASN ALA ARG ASP GLU VAL ILE
SEQRES 2 B 311 ALA ALA ILE HIS GLU GLU ALA ASP TRP VAL ASP ARG THR
SEQRES 3 B 311 VAL TYR PRO PHE GLU SER ARG CYS ILE GLY LEU SER SER
SEQRES 4 B 311 GLY ALA VAL HIS TYR ILE ASP GLU GLY PRO ASP ASP GLY
SEQRES 5 B 311 GLY ARG GLU THR LEU LEU MET LEU HIS GLY ASN PRO THR
SEQRES 6 B 311 TRP SER PHE LEU TYR ARG HIS LEU VAL ARG ASP LEU ARG
SEQRES 7 B 311 ASP GLU TYR ARG CYS VAL ALA LEU ASP TYR LEU GLY PHE
SEQRES 8 B 311 GLY LEU SER GLU ARG PRO THR ASP PHE SER TYR ARG PRO
SEQRES 9 B 311 GLU ASP HIS ALA ASP VAL VAL GLU GLU PHE ILE ASP GLU
SEQRES 10 B 311 LEU GLY LEU GLU ASP VAL VAL LEU VAL GLY HIS ASP TRP
SEQRES 11 B 311 GLY GLY PRO ILE GLY PHE SER TYR ALA ILE ASP HIS PRO
SEQRES 12 B 311 GLU ASN VAL GLY GLY LEU VAL VAL MET ASN THR TRP MET
SEQRES 13 B 311 TRP PRO VAL SER ASP ASP LYS HIS PHE SER ARG PHE SER
SEQRES 14 B 311 LYS LEU LEU ARG ILE GLY ARG GLU LEU CYS GLU ARG TYR
SEQRES 15 B 311 ASP LEU PHE THR ARG VAL ILE MET PRO MET GLY PHE ALA
SEQRES 16 B 311 ASP ARG SER ARG PHE THR GLU SER ALA ARG GLU GLN TYR
SEQRES 17 B 311 ARG ALA ALA ASN ARG GLY ASP ARG THR GLY THR GLY ILE
SEQRES 18 B 311 PHE PRO GLN ALA ILE LEU GLY SER ARG ALA TRP LEU SER
SEQRES 19 B 311 SER LEU TRP GLU GLN ARG ASP ASN ILE ALA ASP ILE PRO
SEQRES 20 B 311 ALA ARG ILE ILE TRP GLY MET GLU ASP SER ALA PHE ARG
SEQRES 21 B 311 PRO ALA GLU LEU ARG THR PHE GLU ALA LEU PHE GLU ASP
SEQRES 22 B 311 SER SER THR VAL ARG LEU TYR GLY VAL GLY HIS TYR VAL
SEQRES 23 B 311 PRO GLU GLU PHE GLY SER ASP LEU VAL PRO LEU VAL ARG
SEQRES 24 B 311 GLU PHE LEU GLU GLU VAL HIS HIS HIS HIS HIS HIS
SEQRES 1 C 311 MET SER SER ALA SER SER ASN ALA ARG ASP GLU VAL ILE
SEQRES 2 C 311 ALA ALA ILE HIS GLU GLU ALA ASP TRP VAL ASP ARG THR
SEQRES 3 C 311 VAL TYR PRO PHE GLU SER ARG CYS ILE GLY LEU SER SER
SEQRES 4 C 311 GLY ALA VAL HIS TYR ILE ASP GLU GLY PRO ASP ASP GLY
SEQRES 5 C 311 GLY ARG GLU THR LEU LEU MET LEU HIS GLY ASN PRO THR
SEQRES 6 C 311 TRP SER PHE LEU TYR ARG HIS LEU VAL ARG ASP LEU ARG
SEQRES 7 C 311 ASP GLU TYR ARG CYS VAL ALA LEU ASP TYR LEU GLY PHE
SEQRES 8 C 311 GLY LEU SER GLU ARG PRO THR ASP PHE SER TYR ARG PRO
SEQRES 9 C 311 GLU ASP HIS ALA ASP VAL VAL GLU GLU PHE ILE ASP GLU
SEQRES 10 C 311 LEU GLY LEU GLU ASP VAL VAL LEU VAL GLY HIS ASP TRP
SEQRES 11 C 311 GLY GLY PRO ILE GLY PHE SER TYR ALA ILE ASP HIS PRO
SEQRES 12 C 311 GLU ASN VAL GLY GLY LEU VAL VAL MET ASN THR TRP MET
SEQRES 13 C 311 TRP PRO VAL SER ASP ASP LYS HIS PHE SER ARG PHE SER
SEQRES 14 C 311 LYS LEU LEU ARG ILE GLY ARG GLU LEU CYS GLU ARG TYR
SEQRES 15 C 311 ASP LEU PHE THR ARG VAL ILE MET PRO MET GLY PHE ALA
SEQRES 16 C 311 ASP ARG SER ARG PHE THR GLU SER ALA ARG GLU GLN TYR
SEQRES 17 C 311 ARG ALA ALA ASN ARG GLY ASP ARG THR GLY THR GLY ILE
SEQRES 18 C 311 PHE PRO GLN ALA ILE LEU GLY SER ARG ALA TRP LEU SER
SEQRES 19 C 311 SER LEU TRP GLU GLN ARG ASP ASN ILE ALA ASP ILE PRO
SEQRES 20 C 311 ALA ARG ILE ILE TRP GLY MET GLU ASP SER ALA PHE ARG
SEQRES 21 C 311 PRO ALA GLU LEU ARG THR PHE GLU ALA LEU PHE GLU ASP
SEQRES 22 C 311 SER SER THR VAL ARG LEU TYR GLY VAL GLY HIS TYR VAL
SEQRES 23 C 311 PRO GLU GLU PHE GLY SER ASP LEU VAL PRO LEU VAL ARG
SEQRES 24 C 311 GLU PHE LEU GLU GLU VAL HIS HIS HIS HIS HIS HIS
SEQRES 1 E 311 MET SER SER ALA SER SER ASN ALA ARG ASP GLU VAL ILE
SEQRES 2 E 311 ALA ALA ILE HIS GLU GLU ALA ASP TRP VAL ASP ARG THR
SEQRES 3 E 311 VAL TYR PRO PHE GLU SER ARG CYS ILE GLY LEU SER SER
SEQRES 4 E 311 GLY ALA VAL HIS TYR ILE ASP GLU GLY PRO ASP ASP GLY
SEQRES 5 E 311 GLY ARG GLU THR LEU LEU MET LEU HIS GLY ASN PRO THR
SEQRES 6 E 311 TRP SER PHE LEU TYR ARG HIS LEU VAL ARG ASP LEU ARG
SEQRES 7 E 311 ASP GLU TYR ARG CYS VAL ALA LEU ASP TYR LEU GLY PHE
SEQRES 8 E 311 GLY LEU SER GLU ARG PRO THR ASP PHE SER TYR ARG PRO
SEQRES 9 E 311 GLU ASP HIS ALA ASP VAL VAL GLU GLU PHE ILE ASP GLU
SEQRES 10 E 311 LEU GLY LEU GLU ASP VAL VAL LEU VAL GLY HIS ASP TRP
SEQRES 11 E 311 GLY GLY PRO ILE GLY PHE SER TYR ALA ILE ASP HIS PRO
SEQRES 12 E 311 GLU ASN VAL GLY GLY LEU VAL VAL MET ASN THR TRP MET
SEQRES 13 E 311 TRP PRO VAL SER ASP ASP LYS HIS PHE SER ARG PHE SER
SEQRES 14 E 311 LYS LEU LEU ARG ILE GLY ARG GLU LEU CYS GLU ARG TYR
SEQRES 15 E 311 ASP LEU PHE THR ARG VAL ILE MET PRO MET GLY PHE ALA
SEQRES 16 E 311 ASP ARG SER ARG PHE THR GLU SER ALA ARG GLU GLN TYR
SEQRES 17 E 311 ARG ALA ALA ASN ARG GLY ASP ARG THR GLY THR GLY ILE
SEQRES 18 E 311 PHE PRO GLN ALA ILE LEU GLY SER ARG ALA TRP LEU SER
SEQRES 19 E 311 SER LEU TRP GLU GLN ARG ASP ASN ILE ALA ASP ILE PRO
SEQRES 20 E 311 ALA ARG ILE ILE TRP GLY MET GLU ASP SER ALA PHE ARG
SEQRES 21 E 311 PRO ALA GLU LEU ARG THR PHE GLU ALA LEU PHE GLU ASP
SEQRES 22 E 311 SER SER THR VAL ARG LEU TYR GLY VAL GLY HIS TYR VAL
SEQRES 23 E 311 PRO GLU GLU PHE GLY SER ASP LEU VAL PRO LEU VAL ARG
SEQRES 24 E 311 GLU PHE LEU GLU GLU VAL HIS HIS HIS HIS HIS HIS
HET CL F1001 1
HETNAM CL CHLORIDE ION
FORMUL 11 CL CL 1-
FORMUL 12 HOH *(H2 O)
HELIX 1 AA1 SER D 6 ILE D 16 1 11
HELIX 2 AA2 TRP D 66 LEU D 69 5 4
HELIX 3 AA3 TYR D 70 ARG D 78 1 9
HELIX 4 AA4 ARG D 103 GLY D 119 1 17
HELIX 5 AA5 TRP D 130 ILE D 140 1 11
HELIX 6 AA6 HIS D 142 GLU D 144 5 3
HELIX 7 AA7 ASP D 162 GLY D 175 1 14
HELIX 8 AA8 GLY D 175 ASP D 183 1 9
HELIX 9 AA9 ASP D 183 VAL D 188 1 6
HELIX 10 AB1 VAL D 188 GLY D 193 1 6
HELIX 11 AB2 ASP D 196 PHE D 200 5 5
HELIX 12 AB3 THR D 201 ASN D 212 1 12
HELIX 13 AB4 ARG D 216 SER D 229 1 14
HELIX 14 AB5 SER D 229 GLU D 238 1 10
HELIX 15 AB6 GLN D 239 ILE D 243 5 5
HELIX 16 AB7 ARG D 260 PHE D 271 1 12
HELIX 17 AB8 TYR D 285 PHE D 290 1 6
HELIX 18 AB9 GLY D 291 ASP D 293 5 3
HELIX 19 AC1 LEU D 294 HIS D 306 1 13
HELIX 20 AC2 SER F 3 GLU F 19 1 17
HELIX 21 AC3 ALA F 20 VAL F 23 5 4
HELIX 22 AC4 TRP F 66 LEU F 69 5 4
HELIX 23 AC5 TYR F 70 ARG F 78 1 9
HELIX 24 AC6 ARG F 103 GLY F 119 1 17
HELIX 25 AC7 TRP F 130 HIS F 142 1 13
HELIX 26 AC8 ASP F 162 LEU F 171 1 10
HELIX 27 AC9 THR F 201 ARG F 213 1 13
HELIX 28 AD1 ARG F 216 SER F 229 1 14
HELIX 29 AD2 SER F 229 GLU F 238 1 10
HELIX 30 AD3 GLN F 239 ILE F 243 5 5
HELIX 31 AD4 ARG F 260 PHE F 271 1 12
HELIX 32 AD5 TYR F 285 PHE F 290 1 6
HELIX 33 AD6 GLY F 291 ASP F 293 5 3
HELIX 34 AD7 LEU F 294 HIS F 306 1 13
HELIX 35 AD8 ASP G 10 GLU G 19 1 10
HELIX 36 AD9 TRP G 66 LEU G 69 5 4
HELIX 37 AE1 TYR G 70 ARG G 78 1 9
HELIX 38 AE2 ARG G 103 GLY G 119 1 17
HELIX 39 AE3 TRP G 130 ILE G 140 1 11
HELIX 40 AE4 HIS G 142 GLU G 144 5 3
HELIX 41 AE5 ASP G 162 ASP G 183 1 22
HELIX 42 AE6 ASP G 183 VAL G 188 1 6
HELIX 43 AE7 VAL G 188 GLY G 193 1 6
HELIX 44 AE8 ASP G 196 PHE G 200 5 5
HELIX 45 AE9 THR G 201 ASN G 212 1 12
HELIX 46 AF1 ARG G 216 SER G 229 1 14
HELIX 47 AF2 SER G 229 GLN G 239 1 11
HELIX 48 AF3 ARG G 240 ILE G 243 5 4
HELIX 49 AF4 ARG G 260 PHE G 271 1 12
HELIX 50 AF5 TYR G 285 PHE G 290 1 6
HELIX 51 AF6 GLY G 291 ASP G 293 5 3
HELIX 52 AF7 LEU G 294 HIS G 307 1 14
HELIX 53 AF8 SER H 6 GLU H 19 1 14
HELIX 54 AF9 TRP H 66 LEU H 69 5 4
HELIX 55 AG1 TYR H 70 ARG H 78 1 9
HELIX 56 AG2 ARG H 103 GLY H 119 1 17
HELIX 57 AG3 TRP H 130 HIS H 142 1 13
HELIX 58 AG4 ASP H 162 LEU H 171 1 10
HELIX 59 AG5 THR H 201 ASN H 212 1 12
HELIX 60 AG6 THR H 217 SER H 229 1 13
HELIX 61 AG7 SER H 229 GLU H 238 1 10
HELIX 62 AG8 GLN H 239 ILE H 243 5 5
HELIX 63 AG9 ARG H 260 PHE H 271 1 12
HELIX 64 AH1 TYR H 285 PHE H 290 1 6
HELIX 65 AH2 GLY H 291 ASP H 293 5 3
HELIX 66 AH3 LEU H 294 HIS H 306 1 13
HELIX 67 AH4 HIS H 307 HIS H 308 5 2
HELIX 68 AH5 ALA I 8 ALA I 8 5 1
HELIX 69 AH6 ARG I 9 GLU I 18 1 10
HELIX 70 AH7 TRP I 66 LEU I 69 5 4
HELIX 71 AH8 TYR I 70 ARG I 78 1 9
HELIX 72 AH9 ARG I 103 GLY I 119 1 17
HELIX 73 AI1 TRP I 130 ILE I 140 1 11
HELIX 74 AI2 HIS I 142 GLU I 144 5 3
HELIX 75 AI3 ASP I 162 GLY I 175 1 14
HELIX 76 AI4 GLY I 175 ASP I 183 1 9
HELIX 77 AI5 ASP I 183 VAL I 188 1 6
HELIX 78 AI6 MET I 190 PHE I 194 5 5
HELIX 79 AI7 ASP I 196 PHE I 200 5 5
HELIX 80 AI8 THR I 201 ASN I 212 1 12
HELIX 81 AI9 ARG I 216 SER I 229 1 14
HELIX 82 AJ1 SER I 229 GLU I 238 1 10
HELIX 83 AJ2 GLN I 239 ILE I 243 5 5
HELIX 84 AJ3 ARG I 260 PHE I 271 1 12
HELIX 85 AJ4 TYR I 285 PHE I 290 1 6
HELIX 86 AJ5 LEU I 294 HIS I 306 1 13
HELIX 87 AJ6 ARG J 9 ALA J 20 1 12
HELIX 88 AJ7 TRP J 66 LEU J 69 5 4
HELIX 89 AJ8 TYR J 70 ARG J 78 1 9
HELIX 90 AJ9 ARG J 103 GLY J 119 1 17
HELIX 91 AK1 TRP J 130 HIS J 142 1 13
HELIX 92 AK2 ASP J 162 LEU J 171 1 10
HELIX 93 AK3 THR J 201 ASN J 212 1 12
HELIX 94 AK4 ARG J 216 SER J 229 1 14
HELIX 95 AK5 SER J 229 GLU J 238 1 10
HELIX 96 AK6 GLN J 239 ILE J 243 5 5
HELIX 97 AK7 ARG J 260 PHE J 271 1 12
HELIX 98 AK8 TYR J 285 GLY J 291 1 7
HELIX 99 AK9 LEU J 294 HIS J 306 1 13
HELIX 100 AL1 HIS J 307 HIS J 309 5 3
HELIX 101 AL2 SER A 6 ALA A 20 1 15
HELIX 102 AL3 ASP A 21 VAL A 23 5 3
HELIX 103 AL4 TRP A 66 LEU A 69 5 4
HELIX 104 AL5 TYR A 70 ARG A 78 1 9
HELIX 105 AL6 ARG A 103 GLY A 119 1 17
HELIX 106 AL7 TRP A 130 HIS A 142 1 13
HELIX 107 AL8 ASP A 162 LEU A 171 1 10
HELIX 108 AL9 THR A 201 ARG A 213 1 13
HELIX 109 AM1 ARG A 216 SER A 229 1 14
HELIX 110 AM2 SER A 229 GLU A 238 1 10
HELIX 111 AM3 GLN A 239 ILE A 243 5 5
HELIX 112 AM4 ARG A 260 PHE A 271 1 12
HELIX 113 AM5 TYR A 285 PHE A 290 1 6
HELIX 114 AM6 GLY A 291 ASP A 293 5 3
HELIX 115 AM7 LEU A 294 HIS A 307 1 14
HELIX 116 AM8 ASN B 7 GLU B 19 1 13
HELIX 117 AM9 TRP B 66 LEU B 69 5 4
HELIX 118 AN1 TYR B 70 ARG B 78 1 9
HELIX 119 AN2 ARG B 103 GLY B 119 1 17
HELIX 120 AN3 TRP B 130 HIS B 142 1 13
HELIX 121 AN4 ASP B 162 LEU B 171 1 10
HELIX 122 AN5 THR B 201 ARG B 213 1 13
HELIX 123 AN6 ARG B 216 SER B 229 1 14
HELIX 124 AN7 SER B 229 GLU B 238 1 10
HELIX 125 AN8 GLN B 239 ILE B 243 5 5
HELIX 126 AN9 ARG B 260 PHE B 271 1 12
HELIX 127 AO1 TYR B 285 PHE B 290 1 6
HELIX 128 AO2 GLY B 291 ASP B 293 5 3
HELIX 129 AO3 LEU B 294 HIS B 306 1 13
HELIX 130 AO4 HIS B 307 HIS B 309 5 3
HELIX 131 AO5 SER C 6 ALA C 20 1 15
HELIX 132 AO6 ASP C 21 VAL C 23 5 3
HELIX 133 AO7 TRP C 66 LEU C 69 5 4
HELIX 134 AO8 TYR C 70 ARG C 78 1 9
HELIX 135 AO9 ARG C 103 GLY C 119 1 17
HELIX 136 AP1 TRP C 130 ILE C 140 1 11
HELIX 137 AP2 HIS C 142 GLU C 144 5 3
HELIX 138 AP3 ASP C 162 ASP C 183 1 22
HELIX 139 AP4 ASP C 183 VAL C 188 1 6
HELIX 140 AP5 MET C 190 PHE C 194 5 5
HELIX 141 AP6 THR C 201 ASN C 212 1 12
HELIX 142 AP7 ARG C 216 SER C 229 1 14
HELIX 143 AP8 SER C 229 GLU C 238 1 10
HELIX 144 AP9 GLN C 239 ILE C 243 5 5
HELIX 145 AQ1 ARG C 260 PHE C 271 1 12
HELIX 146 AQ2 TYR C 285 PHE C 290 1 6
HELIX 147 AQ3 ASP C 293 HIS C 307 1 15
HELIX 148 AQ4 ASN E 7 GLU E 19 1 13
HELIX 149 AQ5 ALA E 20 VAL E 23 5 4
HELIX 150 AQ6 TRP E 66 LEU E 69 5 4
HELIX 151 AQ7 TYR E 70 ARG E 78 1 9
HELIX 152 AQ8 ARG E 103 GLY E 119 1 17
HELIX 153 AQ9 TRP E 130 ILE E 140 1 11
HELIX 154 AR1 HIS E 142 GLU E 144 5 3
HELIX 155 AR2 ASP E 162 ASP E 183 1 22
HELIX 156 AR3 ASP E 183 VAL E 188 1 6
HELIX 157 AR4 VAL E 188 PHE E 194 1 7
HELIX 158 AR5 THR E 201 ASN E 212 1 12
HELIX 159 AR6 ARG E 216 SER E 229 1 14
HELIX 160 AR7 SER E 229 GLU E 238 1 10
HELIX 161 AR8 GLN E 239 ILE E 243 5 5
HELIX 162 AR9 ARG E 260 PHE E 271 1 12
HELIX 163 AS1 TYR E 285 PHE E 290 1 6
HELIX 164 AS2 GLY E 291 ASP E 293 5 3
HELIX 165 AS3 LEU E 294 VAL E 305 1 12
SHEET 1 AA1 8 ARG D 33 GLY D 36 0
SHEET 2 AA1 8 ALA D 41 GLU D 47 -1 O TYR D 44 N ARG D 33
SHEET 3 AA1 8 ARG D 82 LEU D 86 -1 O ALA D 85 N ILE D 45
SHEET 4 AA1 8 THR D 56 LEU D 60 1 N LEU D 57 O ARG D 82
SHEET 5 AA1 8 VAL D 123 HIS D 128 1 O VAL D 126 N LEU D 60
SHEET 6 AA1 8 VAL D 146 MET D 152 1 O GLY D 147 N VAL D 123
SHEET 7 AA1 8 ALA D 248 GLY D 253 1 O ILE D 251 N VAL D 151
SHEET 8 AA1 8 SER D 274 LEU D 279 1 O VAL D 277 N ILE D 250
SHEET 1 AA2 8 ARG F 33 GLY F 36 0
SHEET 2 AA2 8 ALA F 41 GLU F 47 -1 O TYR F 44 N ARG F 33
SHEET 3 AA2 8 ARG F 82 ASP F 87 -1 O ALA F 85 N ILE F 45
SHEET 4 AA2 8 THR F 56 LEU F 60 1 N LEU F 57 O ARG F 82
SHEET 5 AA2 8 VAL F 123 HIS F 128 1 O VAL F 126 N LEU F 60
SHEET 6 AA2 8 VAL F 146 MET F 152 1 O VAL F 150 N LEU F 125
SHEET 7 AA2 8 ALA F 248 GLY F 253 1 O ILE F 251 N VAL F 151
SHEET 8 AA2 8 SER F 274 LEU F 279 1 O VAL F 277 N ILE F 250
SHEET 1 AA3 8 ARG G 33 LEU G 37 0
SHEET 2 AA3 8 GLY G 40 GLU G 47 -1 O TYR G 44 N ARG G 33
SHEET 3 AA3 8 ARG G 82 ASP G 87 -1 O ALA G 85 N ILE G 45
SHEET 4 AA3 8 THR G 56 LEU G 60 1 N LEU G 57 O ARG G 82
SHEET 5 AA3 8 VAL G 123 HIS G 128 1 O VAL G 126 N LEU G 60
SHEET 6 AA3 8 VAL G 146 MET G 152 1 O VAL G 150 N GLY G 127
SHEET 7 AA3 8 ALA G 248 GLY G 253 1 O ILE G 251 N VAL G 151
SHEET 8 AA3 8 SER G 274 LEU G 279 1 O VAL G 277 N ILE G 250
SHEET 1 AA4 8 ARG H 33 LEU H 37 0
SHEET 2 AA4 8 GLY H 40 GLU H 47 -1 O TYR H 44 N ARG H 33
SHEET 3 AA4 8 ARG H 82 ASP H 87 -1 O CYS H 83 N GLU H 47
SHEET 4 AA4 8 THR H 56 LEU H 60 1 N LEU H 57 O ARG H 82
SHEET 5 AA4 8 VAL H 123 HIS H 128 1 O VAL H 126 N LEU H 60
SHEET 6 AA4 8 VAL H 146 MET H 152 1 O VAL H 150 N LEU H 125
SHEET 7 AA4 8 ALA H 248 GLY H 253 1 O ILE H 251 N VAL H 151
SHEET 8 AA4 8 SER H 274 LEU H 279 1 O VAL H 277 N ILE H 250
SHEET 1 AA5 8 ARG I 33 GLY I 36 0
SHEET 2 AA5 8 ALA I 41 GLU I 47 -1 O VAL I 42 N ILE I 35
SHEET 3 AA5 8 ARG I 82 LEU I 86 -1 O ALA I 85 N ILE I 45
SHEET 4 AA5 8 THR I 56 LEU I 60 1 N LEU I 57 O ARG I 82
SHEET 5 AA5 8 VAL I 123 HIS I 128 1 O VAL I 126 N LEU I 60
SHEET 6 AA5 8 VAL I 146 MET I 152 1 O VAL I 150 N LEU I 125
SHEET 7 AA5 8 ALA I 248 GLY I 253 1 O ILE I 251 N VAL I 151
SHEET 8 AA5 8 SER I 274 LEU I 279 1 O VAL I 277 N ILE I 250
SHEET 1 AA6 8 SER J 32 GLY J 36 0
SHEET 2 AA6 8 ALA J 41 GLU J 47 -1 O TYR J 44 N ARG J 33
SHEET 3 AA6 8 ARG J 82 LEU J 86 -1 O CYS J 83 N GLU J 47
SHEET 4 AA6 8 THR J 56 LEU J 60 1 N LEU J 57 O ARG J 82
SHEET 5 AA6 8 VAL J 123 HIS J 128 1 O VAL J 126 N LEU J 60
SHEET 6 AA6 8 VAL J 146 MET J 152 1 O GLY J 147 N VAL J 123
SHEET 7 AA6 8 ALA J 248 GLY J 253 1 O ILE J 251 N VAL J 151
SHEET 8 AA6 8 SER J 274 LEU J 279 1 O VAL J 277 N ILE J 250
SHEET 1 AA7 8 ARG A 33 LEU A 37 0
SHEET 2 AA7 8 GLY A 40 GLU A 47 -1 O TYR A 44 N ARG A 33
SHEET 3 AA7 8 ARG A 82 LEU A 86 -1 O ALA A 85 N ILE A 45
SHEET 4 AA7 8 THR A 56 LEU A 60 1 N LEU A 57 O VAL A 84
SHEET 5 AA7 8 VAL A 123 HIS A 128 1 O VAL A 126 N LEU A 60
SHEET 6 AA7 8 VAL A 146 MET A 152 1 O GLY A 148 N LEU A 125
SHEET 7 AA7 8 ALA A 248 GLY A 253 1 O ILE A 251 N VAL A 151
SHEET 8 AA7 8 SER A 274 LEU A 279 1 O VAL A 277 N ILE A 250
SHEET 1 AA8 8 SER B 32 LEU B 37 0
SHEET 2 AA8 8 GLY B 40 GLU B 47 -1 O TYR B 44 N ARG B 33
SHEET 3 AA8 8 ARG B 82 ASP B 87 -1 O CYS B 83 N GLU B 47
SHEET 4 AA8 8 THR B 56 LEU B 60 1 N LEU B 57 O VAL B 84
SHEET 5 AA8 8 VAL B 123 HIS B 128 1 O VAL B 126 N LEU B 60
SHEET 6 AA8 8 VAL B 146 MET B 152 1 O GLY B 147 N VAL B 123
SHEET 7 AA8 8 ALA B 248 GLY B 253 1 O ARG B 249 N VAL B 151
SHEET 8 AA8 8 SER B 274 LEU B 279 1 O VAL B 277 N ILE B 250
SHEET 1 AA9 8 SER C 32 GLY C 36 0
SHEET 2 AA9 8 ALA C 41 GLU C 47 -1 O TYR C 44 N ARG C 33
SHEET 3 AA9 8 ARG C 82 ASP C 87 -1 O CYS C 83 N GLU C 47
SHEET 4 AA9 8 THR C 56 LEU C 60 1 N LEU C 57 O ARG C 82
SHEET 5 AA9 8 VAL C 123 HIS C 128 1 O VAL C 126 N LEU C 60
SHEET 6 AA9 8 VAL C 146 MET C 152 1 O GLY C 147 N VAL C 123
SHEET 7 AA9 8 ALA C 248 GLY C 253 1 O ARG C 249 N LEU C 149
SHEET 8 AA9 8 SER C 274 LEU C 279 1 O VAL C 277 N ILE C 250
SHEET 1 AB1 8 ARG E 33 LEU E 37 0
SHEET 2 AB1 8 GLY E 40 GLU E 47 -1 O TYR E 44 N ARG E 33
SHEET 3 AB1 8 ARG E 82 LEU E 86 -1 O CYS E 83 N GLU E 47
SHEET 4 AB1 8 THR E 56 LEU E 60 1 N LEU E 57 O ARG E 82
SHEET 5 AB1 8 VAL E 123 HIS E 128 1 O VAL E 126 N LEU E 60
SHEET 6 AB1 8 VAL E 146 MET E 152 1 O VAL E 150 N GLY E 127
SHEET 7 AB1 8 ALA E 248 GLY E 253 1 O ARG E 249 N VAL E 151
SHEET 8 AB1 8 SER E 274 LEU E 279 1 O VAL E 277 N ILE E 250
CISPEP 1 ASN D 63 PRO D 64 0 -23.41
CISPEP 2 ASN F 63 PRO F 64 0 -5.36
CISPEP 3 ASN G 63 PRO G 64 0 -8.01
CISPEP 4 ASN H 63 PRO H 64 0 -1.49
CISPEP 5 ASN I 63 PRO I 64 0 -17.88
CISPEP 6 ASN J 63 PRO J 64 0 -1.79
CISPEP 7 ASN A 63 PRO A 64 0 -3.28
CISPEP 8 ASN B 63 PRO B 64 0 -8.65
CISPEP 9 ASN C 63 PRO C 64 0 -18.05
CISPEP 10 ASN E 63 PRO E 64 0 -26.25
CRYST1 172.760 289.900 168.310 90.00 90.00 90.00 C 2 2 21 80
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 0.005788 0.000000 0.000000 0.00000
SCALE2 0.000000 0.003449 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005941 0.00000
TER 2443 HIS D 307
TER 4793 HIS F 308
TER 7227 HIS G 308
TER 9576 HIS H 308
TER 12005 HIS I 307
TER 14320 HIS J 309
TER 16641 HIS A 309
TER 18970 HIS B 309
TER 21439 HIS C 309
TER 23892 HIS E 308
MASTER 502 0 1 165 80 0 0 623884 10 0 240
END |