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HEADER HYDROLASE 14-FEB-24 8S0G
TITLE CRYSTAL STRUCTURE OF RENILLA RENIFORMIS LUCIFERASE-GFP BRET COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GREEN FLUORESCENT PROTEIN;
COMPND 3 CHAIN: A, B, E, F, I, J;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: COELENTERAZINE H 2-MONOOXYGENASE;
COMPND 7 CHAIN: C, D, G, H, K, L;
COMPND 8 SYNONYM: RENILLA-LUCIFERIN 2-MONOOXYGENASE,RENILLA-TYPE LUCIFERASE;
COMPND 9 EC: 1.13.12.5;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RENILLA RENIFORMIS;
SOURCE 3 ORGANISM_COMMON: SEA PANSY;
SOURCE 4 ORGANISM_TAXID: 6136;
SOURCE 5 GENE: GFP;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: RENILLA RENIFORMIS;
SOURCE 10 ORGANISM_COMMON: SEA PANSY;
SOURCE 11 ORGANISM_TAXID: 6136;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS BIOLUMINESCENCE, LUCIFERASE, GREEN FLUORESCENT PROTEIN, BRET
KEYWDS 2 (BIOLUMINESCENCE RESONANCE ENERGY TRANSFER) COMPLEX, COELENTERAMIDE
KEYWDS 3 EMITTER, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.MAREK
REVDAT 1 03-SEP-25 8S0G 0
JRNL AUTH M.MAREK
JRNL TITL CRYSTAL STRUCTURE OF RENILLA LUCIFERASE VARIANT RLUC8
JRNL TITL 2 COMPLEXED WITH RENILLA GFP (MACROMOLECULAR BRET COMPLEX)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.38 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.14_3260
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) : 2.38
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.44
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 151773
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.223
REMARK 3 R VALUE (WORKING SET) : 0.220
REMARK 3 FREE R VALUE : 0.281
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.760
REMARK 3 FREE R VALUE TEST SET COUNT : 7219
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 48.4370 - 7.3810 0.99 4759 245 0.1781 0.2041
REMARK 3 2 7.3810 - 5.8618 1.00 4888 199 0.1964 0.2492
REMARK 3 3 5.8618 - 5.1218 1.00 4770 272 0.1743 0.2220
REMARK 3 4 5.1218 - 4.6539 1.00 4834 221 0.1554 0.2149
REMARK 3 5 4.6539 - 4.3205 0.99 4833 266 0.1585 0.1971
REMARK 3 6 4.3205 - 4.0659 1.00 4732 279 0.1693 0.2448
REMARK 3 7 4.0659 - 3.8624 1.00 4867 212 0.1761 0.2502
REMARK 3 8 3.8624 - 3.6943 0.99 4841 250 0.1932 0.2486
REMARK 3 9 3.6943 - 3.5522 1.00 4769 281 0.2201 0.3069
REMARK 3 10 3.5522 - 3.4296 1.00 4817 266 0.2239 0.3021
REMARK 3 11 3.4296 - 3.3224 1.00 4869 218 0.2245 0.3081
REMARK 3 12 3.3224 - 3.2275 1.00 4760 248 0.2330 0.3102
REMARK 3 13 3.2275 - 3.1425 1.00 4893 240 0.2530 0.3169
REMARK 3 14 3.1425 - 3.0659 1.00 4880 230 0.2550 0.3122
REMARK 3 15 3.0659 - 2.9962 1.00 4791 256 0.2661 0.3269
REMARK 3 16 2.9962 - 2.9324 1.00 4796 228 0.2715 0.3358
REMARK 3 17 2.9324 - 2.8738 1.00 4909 243 0.2902 0.3529
REMARK 3 18 2.8738 - 2.8195 1.00 4867 199 0.2968 0.3747
REMARK 3 19 2.8195 - 2.7692 1.00 4732 275 0.2908 0.4060
REMARK 3 20 2.7692 - 2.7223 1.00 4917 240 0.2842 0.3366
REMARK 3 21 2.7223 - 2.6783 1.00 4834 190 0.2964 0.3967
REMARK 3 22 2.6783 - 2.6371 1.00 4835 224 0.3242 0.4193
REMARK 3 23 2.6371 - 2.5984 1.00 4805 300 0.3260 0.4146
REMARK 3 24 2.5984 - 2.5618 1.00 4819 197 0.3208 0.3807
REMARK 3 25 2.5618 - 2.5271 1.00 4918 199 0.3271 0.4212
REMARK 3 26 2.5271 - 2.4943 1.00 4800 238 0.3321 0.3919
REMARK 3 27 2.4943 - 2.4631 1.00 4812 253 0.3256 0.3681
REMARK 3 28 2.4631 - 2.4335 1.00 4766 294 0.3331 0.3976
REMARK 3 29 2.4335 - 2.4052 1.00 4816 257 0.3443 0.3918
REMARK 3 30 2.4052 - 2.3782 0.94 4625 199 0.3726 0.4162
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) : 0.440
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 36.260
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) : 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 26801
REMARK 3 ANGLE : 0.684 36231
REMARK 3 CHIRALITY : 0.047 3867
REMARK 3 PLANARITY : 0.004 4632
REMARK 3 DIHEDRAL : 5.342 16796
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): -15.8244 27.5361 -23.4952
REMARK 3 T TENSOR
REMARK 3 T11: 0.3247 T22: 0.2495
REMARK 3 T33: 0.2382 T12: 0.0186
REMARK 3 T13: -0.0006 T23: 0.0117
REMARK 3 L TENSOR
REMARK 3 L11: 0.0907 L22: 0.0400
REMARK 3 L33: 0.1477 L12: 0.0145
REMARK 3 L13: -0.0138 L23: -0.0461
REMARK 3 S TENSOR
REMARK 3 S11: -0.0199 S12: 0.0028 S13: 0.0061
REMARK 3 S21: 0.0103 S22: -0.0145 S23: -0.0009
REMARK 3 S31: -0.0225 S32: -0.0176 S33: -0.0000
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 8S0G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-FEB-24.
REMARK 100 THE DEPOSITION ID IS D_1292136594.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-JUL-20
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
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) : 1
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 : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 152020
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.378
REMARK 200 RESOLUTION RANGE LOW (A) : 48.437
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.38
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.46
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 (%): 52.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM TARTRATE, PEG3350, PH 7.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 240.97400
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 120.48700
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J, K, L
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 MET C 1
REMARK 465 THR C 2
REMARK 465 SER C 3
REMARK 465 GLU C 310
REMARK 465 GLN C 311
REMARK 465 SER C 312
REMARK 465 GLY C 313
REMARK 465 LEU C 314
REMARK 465 GLU C 315
REMARK 465 VAL C 316
REMARK 465 LEU C 317
REMARK 465 PHE C 318
REMARK 465 GLN C 319
REMARK 465 MET D 1
REMARK 465 GLN D 311
REMARK 465 SER D 312
REMARK 465 GLY D 313
REMARK 465 LEU D 314
REMARK 465 GLU D 315
REMARK 465 VAL D 316
REMARK 465 LEU D 317
REMARK 465 PHE D 318
REMARK 465 GLN D 319
REMARK 465 MET E 1
REMARK 465 ASP E 2
REMARK 465 MET F 1
REMARK 465 ASP F 2
REMARK 465 LEU F 3
REMARK 465 MET G 1
REMARK 465 LEU G 314
REMARK 465 GLU G 315
REMARK 465 VAL G 316
REMARK 465 LEU G 317
REMARK 465 PHE G 318
REMARK 465 GLN G 319
REMARK 465 MET H 1
REMARK 465 GLU H 310
REMARK 465 GLN H 311
REMARK 465 SER H 312
REMARK 465 GLY H 313
REMARK 465 LEU H 314
REMARK 465 GLU H 315
REMARK 465 VAL H 316
REMARK 465 LEU H 317
REMARK 465 PHE H 318
REMARK 465 GLN H 319
REMARK 465 MET I 1
REMARK 465 ASP I 2
REMARK 465 LEU I 3
REMARK 465 ALA I 4
REMARK 465 LYS I 5
REMARK 465 MET J 1
REMARK 465 MET K 1
REMARK 465 ASN K 309
REMARK 465 GLU K 310
REMARK 465 GLN K 311
REMARK 465 SER K 312
REMARK 465 GLY K 313
REMARK 465 LEU K 314
REMARK 465 GLU K 315
REMARK 465 VAL K 316
REMARK 465 LEU K 317
REMARK 465 PHE K 318
REMARK 465 GLN K 319
REMARK 465 MET L 1
REMARK 465 GLU L 310
REMARK 465 GLN L 311
REMARK 465 SER L 312
REMARK 465 GLY L 313
REMARK 465 LEU L 314
REMARK 465 GLU L 315
REMARK 465 VAL L 316
REMARK 465 LEU L 317
REMARK 465 PHE L 318
REMARK 465 GLN L 319
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 CRO A 67 CG1
REMARK 470 CRO B 67 CG1
REMARK 470 CRO E 67 CG1
REMARK 470 CRO F 67 CG1
REMARK 470 CRO I 67 CG1
REMARK 470 CRO J 67 CG1
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 OG1 CRO J 67 NE2 GLN J 213 1.30
REMARK 500 OE1 GLU A 159 O HOH A 301 1.97
REMARK 500 O SER L 168 N GLU L 170 2.14
REMARK 500 OD1 ASP K 148 CG ASN K 241 2.15
REMARK 500 OG SER E 182 O LYS E 184 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 LYS L 41 CB LYS L 41 CG -0.165
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 LYS C 271 CD - CE - NZ ANGL. DEV. = -23.5 DEGREES
REMARK 500 ASP F 138 CB - CA - C ANGL. DEV. = -13.8 DEGREES
REMARK 500 ASN G 309 N - CA - CB ANGL. DEV. = 12.5 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 PRO A 55 35.60 -87.72
REMARK 500 VAL A 153 -114.20 52.91
REMARK 500 VAL A 204 99.60 -67.92
REMARK 500 ASP A 205 -32.26 -177.05
REMARK 500 GLU A 228 -66.31 -21.54
REMARK 500 ASP B 2 105.06 -55.80
REMARK 500 LEU B 3 30.73 -78.56
REMARK 500 LEU B 6 7.64 -63.42
REMARK 500 VAL B 153 -103.14 54.22
REMARK 500 ASP B 205 -85.47 51.07
REMARK 500 THR B 206 -20.20 112.96
REMARK 500 SER B 208 166.90 89.44
REMARK 500 VAL C 5 -84.41 -68.16
REMARK 500 TYR C 6 156.72 70.52
REMARK 500 PRO C 8 -164.78 -72.73
REMARK 500 GLU C 9 -92.96 -137.99
REMARK 500 LYS C 12 57.35 -94.28
REMARK 500 LEU C 30 -126.93 56.79
REMARK 500 SER C 32 -155.18 -146.34
REMARK 500 GLU C 40 -51.11 67.62
REMARK 500 ALA C 54 -5.50 69.21
REMARK 500 THR C 55 -165.11 -113.45
REMARK 500 ASP C 120 -113.58 58.93
REMARK 500 THR C 184 -53.98 -121.64
REMARK 500 PHE C 261 -64.81 -127.13
REMARK 500 ALA C 270 -18.86 -48.41
REMARK 500 LYS C 272 1.49 -67.72
REMARK 500 LEU C 284 -115.76 -104.49
REMARK 500 LEU D 30 -123.12 53.74
REMARK 500 SER D 32 -150.37 -142.37
REMARK 500 GLU D 40 -59.77 66.64
REMARK 500 ALA D 54 -13.86 71.71
REMARK 500 THR D 55 -158.84 -115.04
REMARK 500 SER D 56 -161.29 -161.24
REMARK 500 ASP D 120 -135.98 58.97
REMARK 500 ASP D 148 171.70 61.17
REMARK 500 ASP D 158 78.25 -69.41
REMARK 500 LYS D 167 1.37 -67.17
REMARK 500 THR D 184 -57.64 -123.80
REMARK 500 ALA D 246 30.84 -99.09
REMARK 500 SER D 247 57.90 -106.02
REMARK 500 LEU D 284 -117.59 -104.01
REMARK 500 ALA D 291 58.53 -140.29
REMARK 500 VAL E 153 -99.15 53.69
REMARK 500 LEU E 191 -91.61 -79.91
REMARK 500 ASN E 203 26.37 -67.82
REMARK 500 VAL E 204 84.78 -62.31
REMARK 500 SER E 208 -157.55 46.79
REMARK 500 GLU E 228 -95.79 -4.99
REMARK 500 LYS F 5 85.29 -33.00
REMARK 500
REMARK 500 THIS ENTRY HAS 143 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 ALA E 207 SER E 208 144.13
REMARK 500 SER G 312 GLY G 313 128.04
REMARK 500 GLU L 40 LYS L 41 -140.81
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH C 446 DISTANCE = 5.93 ANGSTROMS
REMARK 525 HOH C 447 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH F 320 DISTANCE = 6.13 ANGSTROMS
REMARK 525 HOH G 454 DISTANCE = 7.60 ANGSTROMS
REMARK 525 HOH G 455 DISTANCE = 8.01 ANGSTROMS
REMARK 525 HOH G 456 DISTANCE = 10.58 ANGSTROMS
REMARK 525 HOH K 417 DISTANCE = 6.10 ANGSTROMS
REMARK 525 HOH K 418 DISTANCE = 7.29 ANGSTROMS
DBREF 8S0G A 1 232 UNP Q963I9 Q963I9_RENRE 1 233
DBREF 8S0G B 1 232 UNP Q963I9 Q963I9_RENRE 1 233
DBREF 8S0G C 1 311 UNP P27652 LUCI_RENRE 1 311
DBREF 8S0G D 1 311 UNP P27652 LUCI_RENRE 1 311
DBREF 8S0G E 1 232 UNP Q963I9 Q963I9_RENRE 1 233
DBREF 8S0G F 1 232 UNP Q963I9 Q963I9_RENRE 1 233
DBREF 8S0G G 1 311 UNP P27652 LUCI_RENRE 1 311
DBREF 8S0G H 1 311 UNP P27652 LUCI_RENRE 1 311
DBREF 8S0G I 1 232 UNP Q963I9 Q963I9_RENRE 1 233
DBREF 8S0G J 1 232 UNP Q963I9 Q963I9_RENRE 1 233
DBREF 8S0G K 1 311 UNP P27652 LUCI_RENRE 1 311
DBREF 8S0G L 1 311 UNP P27652 LUCI_RENRE 1 311
SEQADV 8S0G CRO A 67 UNP Q963I9 SER 66 CHROMOPHORE
SEQADV 8S0G CRO A 67 UNP Q963I9 TYR 67 CHROMOPHORE
SEQADV 8S0G CRO A 67 UNP Q963I9 GLY 68 CHROMOPHORE
SEQADV 8S0G CRO B 67 UNP Q963I9 SER 66 CHROMOPHORE
SEQADV 8S0G CRO B 67 UNP Q963I9 TYR 67 CHROMOPHORE
SEQADV 8S0G CRO B 67 UNP Q963I9 GLY 68 CHROMOPHORE
SEQADV 8S0G THR C 55 UNP P27652 ALA 55 ENGINEERED MUTATION
SEQADV 8S0G ALA C 124 UNP P27652 CYS 124 ENGINEERED MUTATION
SEQADV 8S0G ALA C 130 UNP P27652 SER 130 ENGINEERED MUTATION
SEQADV 8S0G ARG C 136 UNP P27652 LYS 136 ENGINEERED MUTATION
SEQADV 8S0G MET C 143 UNP P27652 ALA 143 ENGINEERED MUTATION
SEQADV 8S0G VAL C 185 UNP P27652 MET 185 ENGINEERED MUTATION
SEQADV 8S0G LEU C 253 UNP P27652 MET 253 ENGINEERED MUTATION
SEQADV 8S0G LEU C 287 UNP P27652 SER 287 ENGINEERED MUTATION
SEQADV 8S0G SER C 312 UNP P27652 EXPRESSION TAG
SEQADV 8S0G GLY C 313 UNP P27652 EXPRESSION TAG
SEQADV 8S0G LEU C 314 UNP P27652 EXPRESSION TAG
SEQADV 8S0G GLU C 315 UNP P27652 EXPRESSION TAG
SEQADV 8S0G VAL C 316 UNP P27652 EXPRESSION TAG
SEQADV 8S0G LEU C 317 UNP P27652 EXPRESSION TAG
SEQADV 8S0G PHE C 318 UNP P27652 EXPRESSION TAG
SEQADV 8S0G GLN C 319 UNP P27652 EXPRESSION TAG
SEQADV 8S0G THR D 55 UNP P27652 ALA 55 ENGINEERED MUTATION
SEQADV 8S0G ALA D 124 UNP P27652 CYS 124 ENGINEERED MUTATION
SEQADV 8S0G ALA D 130 UNP P27652 SER 130 ENGINEERED MUTATION
SEQADV 8S0G ARG D 136 UNP P27652 LYS 136 ENGINEERED MUTATION
SEQADV 8S0G MET D 143 UNP P27652 ALA 143 ENGINEERED MUTATION
SEQADV 8S0G VAL D 185 UNP P27652 MET 185 ENGINEERED MUTATION
SEQADV 8S0G LEU D 253 UNP P27652 MET 253 ENGINEERED MUTATION
SEQADV 8S0G LEU D 287 UNP P27652 SER 287 ENGINEERED MUTATION
SEQADV 8S0G SER D 312 UNP P27652 EXPRESSION TAG
SEQADV 8S0G GLY D 313 UNP P27652 EXPRESSION TAG
SEQADV 8S0G LEU D 314 UNP P27652 EXPRESSION TAG
SEQADV 8S0G GLU D 315 UNP P27652 EXPRESSION TAG
SEQADV 8S0G VAL D 316 UNP P27652 EXPRESSION TAG
SEQADV 8S0G LEU D 317 UNP P27652 EXPRESSION TAG
SEQADV 8S0G PHE D 318 UNP P27652 EXPRESSION TAG
SEQADV 8S0G GLN D 319 UNP P27652 EXPRESSION TAG
SEQADV 8S0G CRO E 67 UNP Q963I9 SER 66 CHROMOPHORE
SEQADV 8S0G CRO E 67 UNP Q963I9 TYR 67 CHROMOPHORE
SEQADV 8S0G CRO E 67 UNP Q963I9 GLY 68 CHROMOPHORE
SEQADV 8S0G CRO F 67 UNP Q963I9 SER 66 CHROMOPHORE
SEQADV 8S0G CRO F 67 UNP Q963I9 TYR 67 CHROMOPHORE
SEQADV 8S0G CRO F 67 UNP Q963I9 GLY 68 CHROMOPHORE
SEQADV 8S0G THR G 55 UNP P27652 ALA 55 ENGINEERED MUTATION
SEQADV 8S0G ALA G 124 UNP P27652 CYS 124 ENGINEERED MUTATION
SEQADV 8S0G ALA G 130 UNP P27652 SER 130 ENGINEERED MUTATION
SEQADV 8S0G ARG G 136 UNP P27652 LYS 136 ENGINEERED MUTATION
SEQADV 8S0G MET G 143 UNP P27652 ALA 143 ENGINEERED MUTATION
SEQADV 8S0G VAL G 185 UNP P27652 MET 185 ENGINEERED MUTATION
SEQADV 8S0G LEU G 253 UNP P27652 MET 253 ENGINEERED MUTATION
SEQADV 8S0G LEU G 287 UNP P27652 SER 287 ENGINEERED MUTATION
SEQADV 8S0G SER G 312 UNP P27652 EXPRESSION TAG
SEQADV 8S0G GLY G 313 UNP P27652 EXPRESSION TAG
SEQADV 8S0G LEU G 314 UNP P27652 EXPRESSION TAG
SEQADV 8S0G GLU G 315 UNP P27652 EXPRESSION TAG
SEQADV 8S0G VAL G 316 UNP P27652 EXPRESSION TAG
SEQADV 8S0G LEU G 317 UNP P27652 EXPRESSION TAG
SEQADV 8S0G PHE G 318 UNP P27652 EXPRESSION TAG
SEQADV 8S0G GLN G 319 UNP P27652 EXPRESSION TAG
SEQADV 8S0G THR H 55 UNP P27652 ALA 55 ENGINEERED MUTATION
SEQADV 8S0G ALA H 124 UNP P27652 CYS 124 ENGINEERED MUTATION
SEQADV 8S0G ALA H 130 UNP P27652 SER 130 ENGINEERED MUTATION
SEQADV 8S0G ARG H 136 UNP P27652 LYS 136 ENGINEERED MUTATION
SEQADV 8S0G MET H 143 UNP P27652 ALA 143 ENGINEERED MUTATION
SEQADV 8S0G VAL H 185 UNP P27652 MET 185 ENGINEERED MUTATION
SEQADV 8S0G LEU H 253 UNP P27652 MET 253 ENGINEERED MUTATION
SEQADV 8S0G LEU H 287 UNP P27652 SER 287 ENGINEERED MUTATION
SEQADV 8S0G SER H 312 UNP P27652 EXPRESSION TAG
SEQADV 8S0G GLY H 313 UNP P27652 EXPRESSION TAG
SEQADV 8S0G LEU H 314 UNP P27652 EXPRESSION TAG
SEQADV 8S0G GLU H 315 UNP P27652 EXPRESSION TAG
SEQADV 8S0G VAL H 316 UNP P27652 EXPRESSION TAG
SEQADV 8S0G LEU H 317 UNP P27652 EXPRESSION TAG
SEQADV 8S0G PHE H 318 UNP P27652 EXPRESSION TAG
SEQADV 8S0G GLN H 319 UNP P27652 EXPRESSION TAG
SEQADV 8S0G CRO I 67 UNP Q963I9 SER 66 CHROMOPHORE
SEQADV 8S0G CRO I 67 UNP Q963I9 TYR 67 CHROMOPHORE
SEQADV 8S0G CRO I 67 UNP Q963I9 GLY 68 CHROMOPHORE
SEQADV 8S0G CRO J 67 UNP Q963I9 SER 66 CHROMOPHORE
SEQADV 8S0G CRO J 67 UNP Q963I9 TYR 67 CHROMOPHORE
SEQADV 8S0G CRO J 67 UNP Q963I9 GLY 68 CHROMOPHORE
SEQADV 8S0G THR K 55 UNP P27652 ALA 55 ENGINEERED MUTATION
SEQADV 8S0G ALA K 124 UNP P27652 CYS 124 ENGINEERED MUTATION
SEQADV 8S0G ALA K 130 UNP P27652 SER 130 ENGINEERED MUTATION
SEQADV 8S0G ARG K 136 UNP P27652 LYS 136 ENGINEERED MUTATION
SEQADV 8S0G MET K 143 UNP P27652 ALA 143 ENGINEERED MUTATION
SEQADV 8S0G VAL K 185 UNP P27652 MET 185 ENGINEERED MUTATION
SEQADV 8S0G LEU K 253 UNP P27652 MET 253 ENGINEERED MUTATION
SEQADV 8S0G LEU K 287 UNP P27652 SER 287 ENGINEERED MUTATION
SEQADV 8S0G SER K 312 UNP P27652 EXPRESSION TAG
SEQADV 8S0G GLY K 313 UNP P27652 EXPRESSION TAG
SEQADV 8S0G LEU K 314 UNP P27652 EXPRESSION TAG
SEQADV 8S0G GLU K 315 UNP P27652 EXPRESSION TAG
SEQADV 8S0G VAL K 316 UNP P27652 EXPRESSION TAG
SEQADV 8S0G LEU K 317 UNP P27652 EXPRESSION TAG
SEQADV 8S0G PHE K 318 UNP P27652 EXPRESSION TAG
SEQADV 8S0G GLN K 319 UNP P27652 EXPRESSION TAG
SEQADV 8S0G THR L 55 UNP P27652 ALA 55 ENGINEERED MUTATION
SEQADV 8S0G ALA L 124 UNP P27652 CYS 124 ENGINEERED MUTATION
SEQADV 8S0G ALA L 130 UNP P27652 SER 130 ENGINEERED MUTATION
SEQADV 8S0G ARG L 136 UNP P27652 LYS 136 ENGINEERED MUTATION
SEQADV 8S0G MET L 143 UNP P27652 ALA 143 ENGINEERED MUTATION
SEQADV 8S0G VAL L 185 UNP P27652 MET 185 ENGINEERED MUTATION
SEQADV 8S0G LEU L 253 UNP P27652 MET 253 ENGINEERED MUTATION
SEQADV 8S0G LEU L 287 UNP P27652 SER 287 ENGINEERED MUTATION
SEQADV 8S0G SER L 312 UNP P27652 EXPRESSION TAG
SEQADV 8S0G GLY L 313 UNP P27652 EXPRESSION TAG
SEQADV 8S0G LEU L 314 UNP P27652 EXPRESSION TAG
SEQADV 8S0G GLU L 315 UNP P27652 EXPRESSION TAG
SEQADV 8S0G VAL L 316 UNP P27652 EXPRESSION TAG
SEQADV 8S0G LEU L 317 UNP P27652 EXPRESSION TAG
SEQADV 8S0G PHE L 318 UNP P27652 EXPRESSION TAG
SEQADV 8S0G GLN L 319 UNP P27652 EXPRESSION TAG
SEQRES 1 A 231 MET ASP LEU ALA LYS LEU GLY LEU LYS GLU VAL MET PRO
SEQRES 2 A 231 THR LYS ILE ASN LEU GLU GLY LEU VAL GLY ASP HIS ALA
SEQRES 3 A 231 PHE SER MET GLU GLY VAL GLY GLU GLY ASN ILE LEU GLU
SEQRES 4 A 231 GLY THR GLN GLU VAL LYS ILE SER VAL THR LYS GLY ALA
SEQRES 5 A 231 PRO LEU PRO PHE ALA PHE ASP ILE VAL SER VAL ALA PHE
SEQRES 6 A 231 CRO ASN ARG ALA TYR THR GLY TYR PRO GLU GLU ILE SER
SEQRES 7 A 231 ASP TYR PHE LEU GLN SER PHE PRO GLU GLY PHE THR TYR
SEQRES 8 A 231 GLU ARG ASN ILE ARG TYR GLN ASP GLY GLY THR ALA ILE
SEQRES 9 A 231 VAL LYS SER ASP ILE SER LEU GLU ASP GLY LYS PHE ILE
SEQRES 10 A 231 VAL ASN VAL ASP PHE LYS ALA LYS ASP LEU ARG ARG MET
SEQRES 11 A 231 GLY PRO VAL MET GLN GLN ASP ILE VAL GLY MET GLN PRO
SEQRES 12 A 231 SER TYR GLU SER MET TYR THR ASN VAL THR SER VAL ILE
SEQRES 13 A 231 GLY GLU CYS ILE ILE ALA PHE LYS LEU GLN THR GLY LYS
SEQRES 14 A 231 HIS PHE THR TYR HIS MET ARG THR VAL TYR LYS SER LYS
SEQRES 15 A 231 LYS PRO VAL GLU THR MET PRO LEU TYR HIS PHE ILE GLN
SEQRES 16 A 231 HIS ARG LEU VAL LYS THR ASN VAL ASP THR ALA SER GLY
SEQRES 17 A 231 TYR VAL VAL GLN HIS GLU THR ALA ILE ALA ALA HIS SER
SEQRES 18 A 231 THR ILE LYS LYS ILE GLU GLY SER LEU PRO
SEQRES 1 B 231 MET ASP LEU ALA LYS LEU GLY LEU LYS GLU VAL MET PRO
SEQRES 2 B 231 THR LYS ILE ASN LEU GLU GLY LEU VAL GLY ASP HIS ALA
SEQRES 3 B 231 PHE SER MET GLU GLY VAL GLY GLU GLY ASN ILE LEU GLU
SEQRES 4 B 231 GLY THR GLN GLU VAL LYS ILE SER VAL THR LYS GLY ALA
SEQRES 5 B 231 PRO LEU PRO PHE ALA PHE ASP ILE VAL SER VAL ALA PHE
SEQRES 6 B 231 CRO ASN ARG ALA TYR THR GLY TYR PRO GLU GLU ILE SER
SEQRES 7 B 231 ASP TYR PHE LEU GLN SER PHE PRO GLU GLY PHE THR TYR
SEQRES 8 B 231 GLU ARG ASN ILE ARG TYR GLN ASP GLY GLY THR ALA ILE
SEQRES 9 B 231 VAL LYS SER ASP ILE SER LEU GLU ASP GLY LYS PHE ILE
SEQRES 10 B 231 VAL ASN VAL ASP PHE LYS ALA LYS ASP LEU ARG ARG MET
SEQRES 11 B 231 GLY PRO VAL MET GLN GLN ASP ILE VAL GLY MET GLN PRO
SEQRES 12 B 231 SER TYR GLU SER MET TYR THR ASN VAL THR SER VAL ILE
SEQRES 13 B 231 GLY GLU CYS ILE ILE ALA PHE LYS LEU GLN THR GLY LYS
SEQRES 14 B 231 HIS PHE THR TYR HIS MET ARG THR VAL TYR LYS SER LYS
SEQRES 15 B 231 LYS PRO VAL GLU THR MET PRO LEU TYR HIS PHE ILE GLN
SEQRES 16 B 231 HIS ARG LEU VAL LYS THR ASN VAL ASP THR ALA SER GLY
SEQRES 17 B 231 TYR VAL VAL GLN HIS GLU THR ALA ILE ALA ALA HIS SER
SEQRES 18 B 231 THR ILE LYS LYS ILE GLU GLY SER LEU PRO
SEQRES 1 C 319 MET THR SER LYS VAL TYR ASP PRO GLU GLN ARG LYS ARG
SEQRES 2 C 319 MET ILE THR GLY PRO GLN TRP TRP ALA ARG CYS LYS GLN
SEQRES 3 C 319 MET ASN VAL LEU ASP SER PHE ILE ASN TYR TYR ASP SER
SEQRES 4 C 319 GLU LYS HIS ALA GLU ASN ALA VAL ILE PHE LEU HIS GLY
SEQRES 5 C 319 ASN ALA THR SER SER TYR LEU TRP ARG HIS VAL VAL PRO
SEQRES 6 C 319 HIS ILE GLU PRO VAL ALA ARG CYS ILE ILE PRO ASP LEU
SEQRES 7 C 319 ILE GLY MET GLY LYS SER GLY LYS SER GLY ASN GLY SER
SEQRES 8 C 319 TYR ARG LEU LEU ASP HIS TYR LYS TYR LEU THR ALA TRP
SEQRES 9 C 319 PHE GLU LEU LEU ASN LEU PRO LYS LYS ILE ILE PHE VAL
SEQRES 10 C 319 GLY HIS ASP TRP GLY ALA ALA LEU ALA PHE HIS TYR ALA
SEQRES 11 C 319 TYR GLU HIS GLN ASP ARG ILE LYS ALA ILE VAL HIS MET
SEQRES 12 C 319 GLU SER VAL VAL ASP VAL ILE GLU SER TRP ASP GLU TRP
SEQRES 13 C 319 PRO ASP ILE GLU GLU ASP ILE ALA LEU ILE LYS SER GLU
SEQRES 14 C 319 GLU GLY GLU LYS MET VAL LEU GLU ASN ASN PHE PHE VAL
SEQRES 15 C 319 GLU THR VAL LEU PRO SER LYS ILE MET ARG LYS LEU GLU
SEQRES 16 C 319 PRO GLU GLU PHE ALA ALA TYR LEU GLU PRO PHE LYS GLU
SEQRES 17 C 319 LYS GLY GLU VAL ARG ARG PRO THR LEU SER TRP PRO ARG
SEQRES 18 C 319 GLU ILE PRO LEU VAL LYS GLY GLY LYS PRO ASP VAL VAL
SEQRES 19 C 319 GLN ILE VAL ARG ASN TYR ASN ALA TYR LEU ARG ALA SER
SEQRES 20 C 319 ASP ASP LEU PRO LYS LEU PHE ILE GLU SER ASP PRO GLY
SEQRES 21 C 319 PHE PHE SER ASN ALA ILE VAL GLU GLY ALA LYS LYS PHE
SEQRES 22 C 319 PRO ASN THR GLU PHE VAL LYS VAL LYS GLY LEU HIS PHE
SEQRES 23 C 319 LEU GLN GLU ASP ALA PRO ASP GLU MET GLY LYS TYR ILE
SEQRES 24 C 319 LYS SER PHE VAL GLU ARG VAL LEU LYS ASN GLU GLN SER
SEQRES 25 C 319 GLY LEU GLU VAL LEU PHE GLN
SEQRES 1 D 319 MET THR SER LYS VAL TYR ASP PRO GLU GLN ARG LYS ARG
SEQRES 2 D 319 MET ILE THR GLY PRO GLN TRP TRP ALA ARG CYS LYS GLN
SEQRES 3 D 319 MET ASN VAL LEU ASP SER PHE ILE ASN TYR TYR ASP SER
SEQRES 4 D 319 GLU LYS HIS ALA GLU ASN ALA VAL ILE PHE LEU HIS GLY
SEQRES 5 D 319 ASN ALA THR SER SER TYR LEU TRP ARG HIS VAL VAL PRO
SEQRES 6 D 319 HIS ILE GLU PRO VAL ALA ARG CYS ILE ILE PRO ASP LEU
SEQRES 7 D 319 ILE GLY MET GLY LYS SER GLY LYS SER GLY ASN GLY SER
SEQRES 8 D 319 TYR ARG LEU LEU ASP HIS TYR LYS TYR LEU THR ALA TRP
SEQRES 9 D 319 PHE GLU LEU LEU ASN LEU PRO LYS LYS ILE ILE PHE VAL
SEQRES 10 D 319 GLY HIS ASP TRP GLY ALA ALA LEU ALA PHE HIS TYR ALA
SEQRES 11 D 319 TYR GLU HIS GLN ASP ARG ILE LYS ALA ILE VAL HIS MET
SEQRES 12 D 319 GLU SER VAL VAL ASP VAL ILE GLU SER TRP ASP GLU TRP
SEQRES 13 D 319 PRO ASP ILE GLU GLU ASP ILE ALA LEU ILE LYS SER GLU
SEQRES 14 D 319 GLU GLY GLU LYS MET VAL LEU GLU ASN ASN PHE PHE VAL
SEQRES 15 D 319 GLU THR VAL LEU PRO SER LYS ILE MET ARG LYS LEU GLU
SEQRES 16 D 319 PRO GLU GLU PHE ALA ALA TYR LEU GLU PRO PHE LYS GLU
SEQRES 17 D 319 LYS GLY GLU VAL ARG ARG PRO THR LEU SER TRP PRO ARG
SEQRES 18 D 319 GLU ILE PRO LEU VAL LYS GLY GLY LYS PRO ASP VAL VAL
SEQRES 19 D 319 GLN ILE VAL ARG ASN TYR ASN ALA TYR LEU ARG ALA SER
SEQRES 20 D 319 ASP ASP LEU PRO LYS LEU PHE ILE GLU SER ASP PRO GLY
SEQRES 21 D 319 PHE PHE SER ASN ALA ILE VAL GLU GLY ALA LYS LYS PHE
SEQRES 22 D 319 PRO ASN THR GLU PHE VAL LYS VAL LYS GLY LEU HIS PHE
SEQRES 23 D 319 LEU GLN GLU ASP ALA PRO ASP GLU MET GLY LYS TYR ILE
SEQRES 24 D 319 LYS SER PHE VAL GLU ARG VAL LEU LYS ASN GLU GLN SER
SEQRES 25 D 319 GLY LEU GLU VAL LEU PHE GLN
SEQRES 1 E 231 MET ASP LEU ALA LYS LEU GLY LEU LYS GLU VAL MET PRO
SEQRES 2 E 231 THR LYS ILE ASN LEU GLU GLY LEU VAL GLY ASP HIS ALA
SEQRES 3 E 231 PHE SER MET GLU GLY VAL GLY GLU GLY ASN ILE LEU GLU
SEQRES 4 E 231 GLY THR GLN GLU VAL LYS ILE SER VAL THR LYS GLY ALA
SEQRES 5 E 231 PRO LEU PRO PHE ALA PHE ASP ILE VAL SER VAL ALA PHE
SEQRES 6 E 231 CRO ASN ARG ALA TYR THR GLY TYR PRO GLU GLU ILE SER
SEQRES 7 E 231 ASP TYR PHE LEU GLN SER PHE PRO GLU GLY PHE THR TYR
SEQRES 8 E 231 GLU ARG ASN ILE ARG TYR GLN ASP GLY GLY THR ALA ILE
SEQRES 9 E 231 VAL LYS SER ASP ILE SER LEU GLU ASP GLY LYS PHE ILE
SEQRES 10 E 231 VAL ASN VAL ASP PHE LYS ALA LYS ASP LEU ARG ARG MET
SEQRES 11 E 231 GLY PRO VAL MET GLN GLN ASP ILE VAL GLY MET GLN PRO
SEQRES 12 E 231 SER TYR GLU SER MET TYR THR ASN VAL THR SER VAL ILE
SEQRES 13 E 231 GLY GLU CYS ILE ILE ALA PHE LYS LEU GLN THR GLY LYS
SEQRES 14 E 231 HIS PHE THR TYR HIS MET ARG THR VAL TYR LYS SER LYS
SEQRES 15 E 231 LYS PRO VAL GLU THR MET PRO LEU TYR HIS PHE ILE GLN
SEQRES 16 E 231 HIS ARG LEU VAL LYS THR ASN VAL ASP THR ALA SER GLY
SEQRES 17 E 231 TYR VAL VAL GLN HIS GLU THR ALA ILE ALA ALA HIS SER
SEQRES 18 E 231 THR ILE LYS LYS ILE GLU GLY SER LEU PRO
SEQRES 1 F 231 MET ASP LEU ALA LYS LEU GLY LEU LYS GLU VAL MET PRO
SEQRES 2 F 231 THR LYS ILE ASN LEU GLU GLY LEU VAL GLY ASP HIS ALA
SEQRES 3 F 231 PHE SER MET GLU GLY VAL GLY GLU GLY ASN ILE LEU GLU
SEQRES 4 F 231 GLY THR GLN GLU VAL LYS ILE SER VAL THR LYS GLY ALA
SEQRES 5 F 231 PRO LEU PRO PHE ALA PHE ASP ILE VAL SER VAL ALA PHE
SEQRES 6 F 231 CRO ASN ARG ALA TYR THR GLY TYR PRO GLU GLU ILE SER
SEQRES 7 F 231 ASP TYR PHE LEU GLN SER PHE PRO GLU GLY PHE THR TYR
SEQRES 8 F 231 GLU ARG ASN ILE ARG TYR GLN ASP GLY GLY THR ALA ILE
SEQRES 9 F 231 VAL LYS SER ASP ILE SER LEU GLU ASP GLY LYS PHE ILE
SEQRES 10 F 231 VAL ASN VAL ASP PHE LYS ALA LYS ASP LEU ARG ARG MET
SEQRES 11 F 231 GLY PRO VAL MET GLN GLN ASP ILE VAL GLY MET GLN PRO
SEQRES 12 F 231 SER TYR GLU SER MET TYR THR ASN VAL THR SER VAL ILE
SEQRES 13 F 231 GLY GLU CYS ILE ILE ALA PHE LYS LEU GLN THR GLY LYS
SEQRES 14 F 231 HIS PHE THR TYR HIS MET ARG THR VAL TYR LYS SER LYS
SEQRES 15 F 231 LYS PRO VAL GLU THR MET PRO LEU TYR HIS PHE ILE GLN
SEQRES 16 F 231 HIS ARG LEU VAL LYS THR ASN VAL ASP THR ALA SER GLY
SEQRES 17 F 231 TYR VAL VAL GLN HIS GLU THR ALA ILE ALA ALA HIS SER
SEQRES 18 F 231 THR ILE LYS LYS ILE GLU GLY SER LEU PRO
SEQRES 1 G 319 MET THR SER LYS VAL TYR ASP PRO GLU GLN ARG LYS ARG
SEQRES 2 G 319 MET ILE THR GLY PRO GLN TRP TRP ALA ARG CYS LYS GLN
SEQRES 3 G 319 MET ASN VAL LEU ASP SER PHE ILE ASN TYR TYR ASP SER
SEQRES 4 G 319 GLU LYS HIS ALA GLU ASN ALA VAL ILE PHE LEU HIS GLY
SEQRES 5 G 319 ASN ALA THR SER SER TYR LEU TRP ARG HIS VAL VAL PRO
SEQRES 6 G 319 HIS ILE GLU PRO VAL ALA ARG CYS ILE ILE PRO ASP LEU
SEQRES 7 G 319 ILE GLY MET GLY LYS SER GLY LYS SER GLY ASN GLY SER
SEQRES 8 G 319 TYR ARG LEU LEU ASP HIS TYR LYS TYR LEU THR ALA TRP
SEQRES 9 G 319 PHE GLU LEU LEU ASN LEU PRO LYS LYS ILE ILE PHE VAL
SEQRES 10 G 319 GLY HIS ASP TRP GLY ALA ALA LEU ALA PHE HIS TYR ALA
SEQRES 11 G 319 TYR GLU HIS GLN ASP ARG ILE LYS ALA ILE VAL HIS MET
SEQRES 12 G 319 GLU SER VAL VAL ASP VAL ILE GLU SER TRP ASP GLU TRP
SEQRES 13 G 319 PRO ASP ILE GLU GLU ASP ILE ALA LEU ILE LYS SER GLU
SEQRES 14 G 319 GLU GLY GLU LYS MET VAL LEU GLU ASN ASN PHE PHE VAL
SEQRES 15 G 319 GLU THR VAL LEU PRO SER LYS ILE MET ARG LYS LEU GLU
SEQRES 16 G 319 PRO GLU GLU PHE ALA ALA TYR LEU GLU PRO PHE LYS GLU
SEQRES 17 G 319 LYS GLY GLU VAL ARG ARG PRO THR LEU SER TRP PRO ARG
SEQRES 18 G 319 GLU ILE PRO LEU VAL LYS GLY GLY LYS PRO ASP VAL VAL
SEQRES 19 G 319 GLN ILE VAL ARG ASN TYR ASN ALA TYR LEU ARG ALA SER
SEQRES 20 G 319 ASP ASP LEU PRO LYS LEU PHE ILE GLU SER ASP PRO GLY
SEQRES 21 G 319 PHE PHE SER ASN ALA ILE VAL GLU GLY ALA LYS LYS PHE
SEQRES 22 G 319 PRO ASN THR GLU PHE VAL LYS VAL LYS GLY LEU HIS PHE
SEQRES 23 G 319 LEU GLN GLU ASP ALA PRO ASP GLU MET GLY LYS TYR ILE
SEQRES 24 G 319 LYS SER PHE VAL GLU ARG VAL LEU LYS ASN GLU GLN SER
SEQRES 25 G 319 GLY LEU GLU VAL LEU PHE GLN
SEQRES 1 H 319 MET THR SER LYS VAL TYR ASP PRO GLU GLN ARG LYS ARG
SEQRES 2 H 319 MET ILE THR GLY PRO GLN TRP TRP ALA ARG CYS LYS GLN
SEQRES 3 H 319 MET ASN VAL LEU ASP SER PHE ILE ASN TYR TYR ASP SER
SEQRES 4 H 319 GLU LYS HIS ALA GLU ASN ALA VAL ILE PHE LEU HIS GLY
SEQRES 5 H 319 ASN ALA THR SER SER TYR LEU TRP ARG HIS VAL VAL PRO
SEQRES 6 H 319 HIS ILE GLU PRO VAL ALA ARG CYS ILE ILE PRO ASP LEU
SEQRES 7 H 319 ILE GLY MET GLY LYS SER GLY LYS SER GLY ASN GLY SER
SEQRES 8 H 319 TYR ARG LEU LEU ASP HIS TYR LYS TYR LEU THR ALA TRP
SEQRES 9 H 319 PHE GLU LEU LEU ASN LEU PRO LYS LYS ILE ILE PHE VAL
SEQRES 10 H 319 GLY HIS ASP TRP GLY ALA ALA LEU ALA PHE HIS TYR ALA
SEQRES 11 H 319 TYR GLU HIS GLN ASP ARG ILE LYS ALA ILE VAL HIS MET
SEQRES 12 H 319 GLU SER VAL VAL ASP VAL ILE GLU SER TRP ASP GLU TRP
SEQRES 13 H 319 PRO ASP ILE GLU GLU ASP ILE ALA LEU ILE LYS SER GLU
SEQRES 14 H 319 GLU GLY GLU LYS MET VAL LEU GLU ASN ASN PHE PHE VAL
SEQRES 15 H 319 GLU THR VAL LEU PRO SER LYS ILE MET ARG LYS LEU GLU
SEQRES 16 H 319 PRO GLU GLU PHE ALA ALA TYR LEU GLU PRO PHE LYS GLU
SEQRES 17 H 319 LYS GLY GLU VAL ARG ARG PRO THR LEU SER TRP PRO ARG
SEQRES 18 H 319 GLU ILE PRO LEU VAL LYS GLY GLY LYS PRO ASP VAL VAL
SEQRES 19 H 319 GLN ILE VAL ARG ASN TYR ASN ALA TYR LEU ARG ALA SER
SEQRES 20 H 319 ASP ASP LEU PRO LYS LEU PHE ILE GLU SER ASP PRO GLY
SEQRES 21 H 319 PHE PHE SER ASN ALA ILE VAL GLU GLY ALA LYS LYS PHE
SEQRES 22 H 319 PRO ASN THR GLU PHE VAL LYS VAL LYS GLY LEU HIS PHE
SEQRES 23 H 319 LEU GLN GLU ASP ALA PRO ASP GLU MET GLY LYS TYR ILE
SEQRES 24 H 319 LYS SER PHE VAL GLU ARG VAL LEU LYS ASN GLU GLN SER
SEQRES 25 H 319 GLY LEU GLU VAL LEU PHE GLN
SEQRES 1 I 231 MET ASP LEU ALA LYS LEU GLY LEU LYS GLU VAL MET PRO
SEQRES 2 I 231 THR LYS ILE ASN LEU GLU GLY LEU VAL GLY ASP HIS ALA
SEQRES 3 I 231 PHE SER MET GLU GLY VAL GLY GLU GLY ASN ILE LEU GLU
SEQRES 4 I 231 GLY THR GLN GLU VAL LYS ILE SER VAL THR LYS GLY ALA
SEQRES 5 I 231 PRO LEU PRO PHE ALA PHE ASP ILE VAL SER VAL ALA PHE
SEQRES 6 I 231 CRO ASN ARG ALA TYR THR GLY TYR PRO GLU GLU ILE SER
SEQRES 7 I 231 ASP TYR PHE LEU GLN SER PHE PRO GLU GLY PHE THR TYR
SEQRES 8 I 231 GLU ARG ASN ILE ARG TYR GLN ASP GLY GLY THR ALA ILE
SEQRES 9 I 231 VAL LYS SER ASP ILE SER LEU GLU ASP GLY LYS PHE ILE
SEQRES 10 I 231 VAL ASN VAL ASP PHE LYS ALA LYS ASP LEU ARG ARG MET
SEQRES 11 I 231 GLY PRO VAL MET GLN GLN ASP ILE VAL GLY MET GLN PRO
SEQRES 12 I 231 SER TYR GLU SER MET TYR THR ASN VAL THR SER VAL ILE
SEQRES 13 I 231 GLY GLU CYS ILE ILE ALA PHE LYS LEU GLN THR GLY LYS
SEQRES 14 I 231 HIS PHE THR TYR HIS MET ARG THR VAL TYR LYS SER LYS
SEQRES 15 I 231 LYS PRO VAL GLU THR MET PRO LEU TYR HIS PHE ILE GLN
SEQRES 16 I 231 HIS ARG LEU VAL LYS THR ASN VAL ASP THR ALA SER GLY
SEQRES 17 I 231 TYR VAL VAL GLN HIS GLU THR ALA ILE ALA ALA HIS SER
SEQRES 18 I 231 THR ILE LYS LYS ILE GLU GLY SER LEU PRO
SEQRES 1 J 231 MET ASP LEU ALA LYS LEU GLY LEU LYS GLU VAL MET PRO
SEQRES 2 J 231 THR LYS ILE ASN LEU GLU GLY LEU VAL GLY ASP HIS ALA
SEQRES 3 J 231 PHE SER MET GLU GLY VAL GLY GLU GLY ASN ILE LEU GLU
SEQRES 4 J 231 GLY THR GLN GLU VAL LYS ILE SER VAL THR LYS GLY ALA
SEQRES 5 J 231 PRO LEU PRO PHE ALA PHE ASP ILE VAL SER VAL ALA PHE
SEQRES 6 J 231 CRO ASN ARG ALA TYR THR GLY TYR PRO GLU GLU ILE SER
SEQRES 7 J 231 ASP TYR PHE LEU GLN SER PHE PRO GLU GLY PHE THR TYR
SEQRES 8 J 231 GLU ARG ASN ILE ARG TYR GLN ASP GLY GLY THR ALA ILE
SEQRES 9 J 231 VAL LYS SER ASP ILE SER LEU GLU ASP GLY LYS PHE ILE
SEQRES 10 J 231 VAL ASN VAL ASP PHE LYS ALA LYS ASP LEU ARG ARG MET
SEQRES 11 J 231 GLY PRO VAL MET GLN GLN ASP ILE VAL GLY MET GLN PRO
SEQRES 12 J 231 SER TYR GLU SER MET TYR THR ASN VAL THR SER VAL ILE
SEQRES 13 J 231 GLY GLU CYS ILE ILE ALA PHE LYS LEU GLN THR GLY LYS
SEQRES 14 J 231 HIS PHE THR TYR HIS MET ARG THR VAL TYR LYS SER LYS
SEQRES 15 J 231 LYS PRO VAL GLU THR MET PRO LEU TYR HIS PHE ILE GLN
SEQRES 16 J 231 HIS ARG LEU VAL LYS THR ASN VAL ASP THR ALA SER GLY
SEQRES 17 J 231 TYR VAL VAL GLN HIS GLU THR ALA ILE ALA ALA HIS SER
SEQRES 18 J 231 THR ILE LYS LYS ILE GLU GLY SER LEU PRO
SEQRES 1 K 319 MET THR SER LYS VAL TYR ASP PRO GLU GLN ARG LYS ARG
SEQRES 2 K 319 MET ILE THR GLY PRO GLN TRP TRP ALA ARG CYS LYS GLN
SEQRES 3 K 319 MET ASN VAL LEU ASP SER PHE ILE ASN TYR TYR ASP SER
SEQRES 4 K 319 GLU LYS HIS ALA GLU ASN ALA VAL ILE PHE LEU HIS GLY
SEQRES 5 K 319 ASN ALA THR SER SER TYR LEU TRP ARG HIS VAL VAL PRO
SEQRES 6 K 319 HIS ILE GLU PRO VAL ALA ARG CYS ILE ILE PRO ASP LEU
SEQRES 7 K 319 ILE GLY MET GLY LYS SER GLY LYS SER GLY ASN GLY SER
SEQRES 8 K 319 TYR ARG LEU LEU ASP HIS TYR LYS TYR LEU THR ALA TRP
SEQRES 9 K 319 PHE GLU LEU LEU ASN LEU PRO LYS LYS ILE ILE PHE VAL
SEQRES 10 K 319 GLY HIS ASP TRP GLY ALA ALA LEU ALA PHE HIS TYR ALA
SEQRES 11 K 319 TYR GLU HIS GLN ASP ARG ILE LYS ALA ILE VAL HIS MET
SEQRES 12 K 319 GLU SER VAL VAL ASP VAL ILE GLU SER TRP ASP GLU TRP
SEQRES 13 K 319 PRO ASP ILE GLU GLU ASP ILE ALA LEU ILE LYS SER GLU
SEQRES 14 K 319 GLU GLY GLU LYS MET VAL LEU GLU ASN ASN PHE PHE VAL
SEQRES 15 K 319 GLU THR VAL LEU PRO SER LYS ILE MET ARG LYS LEU GLU
SEQRES 16 K 319 PRO GLU GLU PHE ALA ALA TYR LEU GLU PRO PHE LYS GLU
SEQRES 17 K 319 LYS GLY GLU VAL ARG ARG PRO THR LEU SER TRP PRO ARG
SEQRES 18 K 319 GLU ILE PRO LEU VAL LYS GLY GLY LYS PRO ASP VAL VAL
SEQRES 19 K 319 GLN ILE VAL ARG ASN TYR ASN ALA TYR LEU ARG ALA SER
SEQRES 20 K 319 ASP ASP LEU PRO LYS LEU PHE ILE GLU SER ASP PRO GLY
SEQRES 21 K 319 PHE PHE SER ASN ALA ILE VAL GLU GLY ALA LYS LYS PHE
SEQRES 22 K 319 PRO ASN THR GLU PHE VAL LYS VAL LYS GLY LEU HIS PHE
SEQRES 23 K 319 LEU GLN GLU ASP ALA PRO ASP GLU MET GLY LYS TYR ILE
SEQRES 24 K 319 LYS SER PHE VAL GLU ARG VAL LEU LYS ASN GLU GLN SER
SEQRES 25 K 319 GLY LEU GLU VAL LEU PHE GLN
SEQRES 1 L 319 MET THR SER LYS VAL TYR ASP PRO GLU GLN ARG LYS ARG
SEQRES 2 L 319 MET ILE THR GLY PRO GLN TRP TRP ALA ARG CYS LYS GLN
SEQRES 3 L 319 MET ASN VAL LEU ASP SER PHE ILE ASN TYR TYR ASP SER
SEQRES 4 L 319 GLU LYS HIS ALA GLU ASN ALA VAL ILE PHE LEU HIS GLY
SEQRES 5 L 319 ASN ALA THR SER SER TYR LEU TRP ARG HIS VAL VAL PRO
SEQRES 6 L 319 HIS ILE GLU PRO VAL ALA ARG CYS ILE ILE PRO ASP LEU
SEQRES 7 L 319 ILE GLY MET GLY LYS SER GLY LYS SER GLY ASN GLY SER
SEQRES 8 L 319 TYR ARG LEU LEU ASP HIS TYR LYS TYR LEU THR ALA TRP
SEQRES 9 L 319 PHE GLU LEU LEU ASN LEU PRO LYS LYS ILE ILE PHE VAL
SEQRES 10 L 319 GLY HIS ASP TRP GLY ALA ALA LEU ALA PHE HIS TYR ALA
SEQRES 11 L 319 TYR GLU HIS GLN ASP ARG ILE LYS ALA ILE VAL HIS MET
SEQRES 12 L 319 GLU SER VAL VAL ASP VAL ILE GLU SER TRP ASP GLU TRP
SEQRES 13 L 319 PRO ASP ILE GLU GLU ASP ILE ALA LEU ILE LYS SER GLU
SEQRES 14 L 319 GLU GLY GLU LYS MET VAL LEU GLU ASN ASN PHE PHE VAL
SEQRES 15 L 319 GLU THR VAL LEU PRO SER LYS ILE MET ARG LYS LEU GLU
SEQRES 16 L 319 PRO GLU GLU PHE ALA ALA TYR LEU GLU PRO PHE LYS GLU
SEQRES 17 L 319 LYS GLY GLU VAL ARG ARG PRO THR LEU SER TRP PRO ARG
SEQRES 18 L 319 GLU ILE PRO LEU VAL LYS GLY GLY LYS PRO ASP VAL VAL
SEQRES 19 L 319 GLN ILE VAL ARG ASN TYR ASN ALA TYR LEU ARG ALA SER
SEQRES 20 L 319 ASP ASP LEU PRO LYS LEU PHE ILE GLU SER ASP PRO GLY
SEQRES 21 L 319 PHE PHE SER ASN ALA ILE VAL GLU GLY ALA LYS LYS PHE
SEQRES 22 L 319 PRO ASN THR GLU PHE VAL LYS VAL LYS GLY LEU HIS PHE
SEQRES 23 L 319 LEU GLN GLU ASP ALA PRO ASP GLU MET GLY LYS TYR ILE
SEQRES 24 L 319 LYS SER PHE VAL GLU ARG VAL LEU LYS ASN GLU GLN SER
SEQRES 25 L 319 GLY LEU GLU VAL LEU PHE GLN
MODRES 8S0G CRO A 67 SER CHROMOPHORE
MODRES 8S0G CRO A 67 TYR CHROMOPHORE
MODRES 8S0G CRO A 67 GLY CHROMOPHORE
MODRES 8S0G CRO B 67 SER CHROMOPHORE
MODRES 8S0G CRO B 67 TYR CHROMOPHORE
MODRES 8S0G CRO B 67 GLY CHROMOPHORE
MODRES 8S0G CRO E 67 SER CHROMOPHORE
MODRES 8S0G CRO E 67 TYR CHROMOPHORE
MODRES 8S0G CRO E 67 GLY CHROMOPHORE
MODRES 8S0G CRO F 67 SER CHROMOPHORE
MODRES 8S0G CRO F 67 TYR CHROMOPHORE
MODRES 8S0G CRO F 67 GLY CHROMOPHORE
MODRES 8S0G CRO I 67 SER CHROMOPHORE
MODRES 8S0G CRO I 67 TYR CHROMOPHORE
MODRES 8S0G CRO I 67 GLY CHROMOPHORE
MODRES 8S0G CRO J 67 SER CHROMOPHORE
MODRES 8S0G CRO J 67 TYR CHROMOPHORE
MODRES 8S0G CRO J 67 GLY CHROMOPHORE
HET CRO A 67 21
HET CRO B 67 21
HET CRO E 67 21
HET CRO F 67 21
HET CRO I 67 21
HET CRO J 67 21
HET CEI L 401 31
HETNAM CRO {2-[(1R,2R)-1-AMINO-2-HYDROXYPROPYL]-4-(4-
HETNAM 2 CRO HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-
HETNAM 3 CRO YL}ACETIC ACID
HETNAM CEI N-[3-BENZYL-5-(4-HYDROXYPHENYL)PYRAZIN-2-YL]-2-(4-
HETNAM 2 CEI HYDROXYPHENYL)ACETAMIDE
HETSYN CRO PEPTIDE DERIVED CHROMOPHORE
HETSYN CEI COELENTERAMIDE
FORMUL 1 CRO 6(C15 H17 N3 O5)
FORMUL 13 CEI C25 H21 N3 O3
FORMUL 14 HOH *371(H2 O)
HELIX 1 AA1 ASP A 2 GLY A 7 5 6
HELIX 2 AA2 ALA A 57 SER A 62 5 6
HELIX 3 AA3 GLY A 132 GLN A 137 1 6
HELIX 4 AA4 ALA B 57 PHE B 65 5 9
HELIX 5 AA5 ASP B 80 SER B 85 1 6
HELIX 6 AA6 THR C 16 ALA C 22 1 7
HELIX 7 AA7 SER C 56 ARG C 61 5 6
HELIX 8 AA8 VAL C 63 ILE C 67 5 5
HELIX 9 AA9 ARG C 93 GLU C 106 1 14
HELIX 10 AB1 ASP C 120 HIS C 133 1 14
HELIX 11 AB2 ILE C 159 SER C 168 1 10
HELIX 12 AB3 GLU C 170 VAL C 175 1 6
HELIX 13 AB4 ASN C 179 THR C 184 1 6
HELIX 14 AB5 THR C 184 LYS C 189 1 6
HELIX 15 AB6 GLU C 195 GLU C 204 1 10
HELIX 16 AB7 PRO C 205 LYS C 207 5 3
HELIX 17 AB8 GLY C 210 VAL C 212 5 3
HELIX 18 AB9 ARG C 213 TRP C 219 1 7
HELIX 19 AC1 PRO C 220 ILE C 223 5 4
HELIX 20 AC2 LYS C 230 SER C 247 1 18
HELIX 21 AC3 PHE C 262 LYS C 272 1 11
HELIX 22 AC4 PHE C 286 ASP C 290 5 5
HELIX 23 AC5 ALA C 291 ASN C 309 1 19
HELIX 24 AC6 GLN D 10 MET D 14 5 5
HELIX 25 AC7 THR D 16 ALA D 22 1 7
HELIX 26 AC8 SER D 56 ARG D 61 5 6
HELIX 27 AC9 VAL D 63 GLU D 68 1 6
HELIX 28 AD1 ARG D 93 GLU D 106 1 14
HELIX 29 AD2 TRP D 121 HIS D 133 1 13
HELIX 30 AD3 ILE D 159 LYS D 167 1 9
HELIX 31 AD4 GLU D 169 LEU D 176 1 8
HELIX 32 AD5 ASN D 179 THR D 184 1 6
HELIX 33 AD6 THR D 184 LYS D 189 1 6
HELIX 34 AD7 GLU D 195 GLU D 204 1 10
HELIX 35 AD8 PRO D 205 LYS D 207 5 3
HELIX 36 AD9 GLY D 210 VAL D 212 5 3
HELIX 37 AE1 ARG D 213 TRP D 219 1 7
HELIX 38 AE2 PRO D 220 ILE D 223 5 4
HELIX 39 AE3 LYS D 230 ALA D 246 1 17
HELIX 40 AE4 PHE D 262 LYS D 272 1 11
HELIX 41 AE5 PHE D 286 ASP D 290 5 5
HELIX 42 AE6 ALA D 291 LEU D 307 1 17
HELIX 43 AE7 ALA E 57 SER E 62 5 6
HELIX 44 AE8 ASP E 80 SER E 85 1 6
HELIX 45 AE9 ALA F 57 PHE F 65 5 9
HELIX 46 AF1 ASP F 80 SER F 85 1 6
HELIX 47 AF2 GLY F 132 GLN F 137 1 6
HELIX 48 AF3 GLN G 10 MET G 14 5 5
HELIX 49 AF4 THR G 16 ARG G 23 1 8
HELIX 50 AF5 SER G 56 ARG G 61 5 6
HELIX 51 AF6 VAL G 63 ILE G 67 5 5
HELIX 52 AF7 ARG G 93 LEU G 107 1 15
HELIX 53 AF8 ASP G 120 HIS G 133 1 14
HELIX 54 AF9 ILE G 159 SER G 168 1 10
HELIX 55 AG1 GLU G 169 LEU G 176 1 8
HELIX 56 AG2 ASN G 179 THR G 184 1 6
HELIX 57 AG3 THR G 184 LYS G 189 1 6
HELIX 58 AG4 GLU G 195 GLU G 204 1 10
HELIX 59 AG5 PRO G 205 LYS G 207 5 3
HELIX 60 AG6 GLY G 210 VAL G 212 5 3
HELIX 61 AG7 ARG G 213 TRP G 219 1 7
HELIX 62 AG8 PRO G 220 ILE G 223 5 4
HELIX 63 AG9 LYS G 230 SER G 247 1 18
HELIX 64 AH1 PHE G 262 LYS G 272 1 11
HELIX 65 AH2 PHE G 286 ALA G 291 1 6
HELIX 66 AH3 ALA G 291 ASN G 309 1 19
HELIX 67 AH4 GLN H 10 MET H 14 5 5
HELIX 68 AH5 THR H 16 ALA H 22 1 7
HELIX 69 AH6 SER H 56 ARG H 61 5 6
HELIX 70 AH7 VAL H 63 ILE H 67 5 5
HELIX 71 AH8 ARG H 93 LEU H 107 1 15
HELIX 72 AH9 ASP H 120 HIS H 133 1 14
HELIX 73 AI1 ILE H 159 SER H 168 1 10
HELIX 74 AI2 GLU H 169 LEU H 176 1 8
HELIX 75 AI3 ASN H 179 THR H 184 1 6
HELIX 76 AI4 THR H 184 LYS H 189 1 6
HELIX 77 AI5 GLU H 195 GLU H 204 1 10
HELIX 78 AI6 PRO H 205 LYS H 207 5 3
HELIX 79 AI7 GLY H 210 VAL H 212 5 3
HELIX 80 AI8 ARG H 213 TRP H 219 1 7
HELIX 81 AI9 PRO H 220 ILE H 223 5 4
HELIX 82 AJ1 LYS H 230 SER H 247 1 18
HELIX 83 AJ2 PHE H 262 LYS H 272 1 11
HELIX 84 AJ3 PHE H 286 ASP H 290 5 5
HELIX 85 AJ4 ALA H 291 LYS H 308 1 18
HELIX 86 AJ5 ALA I 57 PHE I 65 5 9
HELIX 87 AJ6 ASP I 80 SER I 85 1 6
HELIX 88 AJ7 GLY I 132 GLN I 137 1 6
HELIX 89 AJ8 ALA J 57 SER J 62 5 6
HELIX 90 AJ9 ASP J 80 SER J 85 1 6
HELIX 91 AK1 THR K 16 ALA K 22 1 7
HELIX 92 AK2 SER K 56 ARG K 61 5 6
HELIX 93 AK3 VAL K 63 ILE K 67 5 5
HELIX 94 AK4 ARG K 93 LEU K 107 1 15
HELIX 95 AK5 ASP K 120 HIS K 133 1 14
HELIX 96 AK6 GLU K 161 LYS K 167 1 7
HELIX 97 AK7 GLU K 170 LEU K 176 1 7
HELIX 98 AK8 ASN K 179 THR K 184 1 6
HELIX 99 AK9 THR K 184 LYS K 189 1 6
HELIX 100 AL1 GLU K 195 GLU K 204 1 10
HELIX 101 AL2 PRO K 205 LYS K 207 5 3
HELIX 102 AL3 GLY K 210 ARG K 213 5 4
HELIX 103 AL4 ARG K 214 TRP K 219 1 6
HELIX 104 AL5 PRO K 220 ILE K 223 5 4
HELIX 105 AL6 LYS K 230 ALA K 246 1 17
HELIX 106 AL7 PHE K 262 LYS K 271 1 10
HELIX 107 AL8 PHE K 286 ASP K 290 5 5
HELIX 108 AL9 ALA K 291 VAL K 306 1 16
HELIX 109 AM1 GLN L 10 MET L 14 5 5
HELIX 110 AM2 THR L 16 ARG L 23 1 8
HELIX 111 AM3 SER L 56 ARG L 61 5 6
HELIX 112 AM4 VAL L 63 ILE L 67 5 5
HELIX 113 AM5 ARG L 93 LEU L 107 1 15
HELIX 114 AM6 TRP L 121 HIS L 133 1 13
HELIX 115 AM7 GLU L 161 LYS L 167 1 7
HELIX 116 AM8 GLU L 169 LEU L 176 1 8
HELIX 117 AM9 ASN L 179 THR L 184 1 6
HELIX 118 AN1 THR L 184 LYS L 189 1 6
HELIX 119 AN2 GLU L 195 GLU L 204 1 10
HELIX 120 AN3 PRO L 205 LYS L 207 5 3
HELIX 121 AN4 GLY L 210 VAL L 212 5 3
HELIX 122 AN5 ARG L 213 TRP L 219 1 7
HELIX 123 AN6 PRO L 220 ILE L 223 5 4
HELIX 124 AN7 LYS L 230 ARG L 245 1 16
HELIX 125 AN8 PHE L 262 LYS L 272 1 11
HELIX 126 AN9 PHE L 286 ASP L 290 5 5
HELIX 127 AO1 ALA L 291 ASN L 309 1 19
SHEET 1 AA113 ILE A 139 MET A 142 0
SHEET 2 AA113 SER A 155 LEU A 166 -1 O LYS A 165 N VAL A 140
SHEET 3 AA113 HIS A 171 SER A 182 -1 O PHE A 172 N PHE A 164
SHEET 4 AA113 PHE A 90 TYR A 98 -1 N ASN A 95 O ARG A 177
SHEET 5 AA113 THR A 103 LEU A 112 -1 O ALA A 104 N ILE A 96
SHEET 6 AA113 PHE A 117 LYS A 126 -1 O ILE A 118 N SER A 111
SHEET 7 AA113 THR A 14 VAL A 22 1 N LYS A 15 O VAL A 119
SHEET 8 AA113 HIS A 25 ASN A 36 -1 O PHE A 27 N GLY A 20
SHEET 9 AA113 THR A 41 LYS A 50 -1 O LYS A 50 N SER A 28
SHEET 10 AA113 VAL A 211 ALA A 220 -1 O GLN A 213 N VAL A 44
SHEET 11 AA113 HIS A 193 LYS A 201 -1 N GLN A 196 O ILE A 218
SHEET 12 AA113 SER A 145 ASN A 152 -1 N GLU A 147 O ILE A 195
SHEET 13 AA113 SER A 155 LEU A 166 -1 O SER A 155 N ASN A 152
SHEET 1 AA213 ILE B 139 MET B 142 0
SHEET 2 AA213 SER B 155 LEU B 166 -1 O LYS B 165 N VAL B 140
SHEET 3 AA213 HIS B 171 SER B 182 -1 O THR B 178 N GLY B 158
SHEET 4 AA213 PHE B 90 TYR B 98 -1 N ASN B 95 O ARG B 177
SHEET 5 AA213 THR B 103 GLU B 113 -1 O ILE B 110 N PHE B 90
SHEET 6 AA213 LYS B 116 LYS B 126 -1 O ILE B 118 N SER B 111
SHEET 7 AA213 VAL B 11 VAL B 22 1 N ASN B 17 O VAL B 121
SHEET 8 AA213 HIS B 25 ASN B 36 -1 O PHE B 27 N GLY B 20
SHEET 9 AA213 THR B 41 LYS B 50 -1 O LYS B 45 N VAL B 32
SHEET 10 AA213 VAL B 211 ALA B 220 -1 O VAL B 211 N ILE B 46
SHEET 11 AA213 HIS B 193 THR B 202 -1 N GLN B 196 O ILE B 218
SHEET 12 AA213 SER B 145 ASN B 152 -1 N MET B 149 O HIS B 193
SHEET 13 AA213 SER B 155 LEU B 166 -1 O SER B 155 N ASN B 152
SHEET 1 AA3 8 LYS C 25 VAL C 29 0
SHEET 2 AA3 8 SER C 32 ASP C 38 -1 O TYR C 36 N LYS C 25
SHEET 3 AA3 8 ARG C 72 PRO C 76 -1 O ILE C 75 N TYR C 37
SHEET 4 AA3 8 ALA C 46 LEU C 50 1 N VAL C 47 O ARG C 72
SHEET 5 AA3 8 ILE C 114 HIS C 119 1 O VAL C 117 N ILE C 48
SHEET 6 AA3 8 ILE C 137 MET C 143 1 O VAL C 141 N PHE C 116
SHEET 7 AA3 8 LYS C 252 PRO C 259 1 O LEU C 253 N ILE C 140
SHEET 8 AA3 8 THR C 276 GLY C 283 1 O VAL C 279 N PHE C 254
SHEET 1 AA4 8 LYS D 25 VAL D 29 0
SHEET 2 AA4 8 SER D 32 ASP D 38 -1 O TYR D 36 N LYS D 25
SHEET 3 AA4 8 ARG D 72 PRO D 76 -1 O ILE D 75 N TYR D 37
SHEET 4 AA4 8 ALA D 46 LEU D 50 1 N VAL D 47 O ARG D 72
SHEET 5 AA4 8 ILE D 114 HIS D 119 1 O VAL D 117 N LEU D 50
SHEET 6 AA4 8 ILE D 137 MET D 143 1 O VAL D 141 N PHE D 116
SHEET 7 AA4 8 LYS D 252 PRO D 259 1 O LEU D 253 N HIS D 142
SHEET 8 AA4 8 THR D 276 GLY D 283 1 O VAL D 279 N GLU D 256
SHEET 1 AA513 ILE E 139 MET E 142 0
SHEET 2 AA513 SER E 155 LEU E 166 -1 O LYS E 165 N GLY E 141
SHEET 3 AA513 HIS E 171 SER E 182 -1 O PHE E 172 N PHE E 164
SHEET 4 AA513 GLY E 89 TYR E 98 -1 N ASN E 95 O ARG E 177
SHEET 5 AA513 THR E 103 GLU E 113 -1 O VAL E 106 N ARG E 94
SHEET 6 AA513 LYS E 116 LYS E 126 -1 O ILE E 118 N SER E 111
SHEET 7 AA513 VAL E 11 VAL E 22 1 N ASN E 17 O VAL E 121
SHEET 8 AA513 HIS E 25 ASN E 36 -1 O MET E 29 N LEU E 18
SHEET 9 AA513 THR E 41 LYS E 50 -1 O LYS E 45 N VAL E 32
SHEET 10 AA513 VAL E 211 ALA E 220 -1 O VAL E 211 N ILE E 46
SHEET 11 AA513 TYR E 192 LYS E 201 -1 N GLN E 196 O ILE E 218
SHEET 12 AA513 SER E 145 ASN E 152 -1 N MET E 149 O HIS E 193
SHEET 13 AA513 SER E 155 LEU E 166 -1 O ILE E 157 N TYR E 150
SHEET 1 AA6 5 SER E 230 LEU E 231 0
SHEET 2 AA6 5 HIS F 193 THR F 202 -1 O LYS F 201 N LEU E 231
SHEET 3 AA6 5 SER F 145 ASN F 152 -1 N MET F 149 O HIS F 193
SHEET 4 AA6 5 SER F 155 LEU F 166 -1 O ILE F 157 N TYR F 150
SHEET 5 AA6 5 ILE F 139 MET F 142 -1 N VAL F 140 O LYS F 165
SHEET 1 AA712 SER E 230 LEU E 231 0
SHEET 2 AA712 HIS F 193 THR F 202 -1 O LYS F 201 N LEU E 231
SHEET 3 AA712 VAL F 211 ALA F 220 -1 O ILE F 218 N GLN F 196
SHEET 4 AA712 THR F 41 LYS F 50 -1 N ILE F 46 O VAL F 211
SHEET 5 AA712 HIS F 25 ASN F 36 -1 N VAL F 32 O LYS F 45
SHEET 6 AA712 VAL F 11 VAL F 22 -1 N LEU F 18 O MET F 29
SHEET 7 AA712 PHE F 117 LYS F 126 1 O VAL F 119 N ASN F 17
SHEET 8 AA712 THR F 103 SER F 111 -1 N SER F 111 O ILE F 118
SHEET 9 AA712 PHE F 90 TYR F 98 -1 N TYR F 92 O SER F 108
SHEET 10 AA712 HIS F 171 SER F 182 -1 O ARG F 177 N ASN F 95
SHEET 11 AA712 SER F 155 LEU F 166 -1 N PHE F 164 O PHE F 172
SHEET 12 AA712 ILE F 139 MET F 142 -1 N VAL F 140 O LYS F 165
SHEET 1 AA8 2 ASN G 28 VAL G 29 0
SHEET 2 AA8 2 SER G 32 PHE G 33 -1 O SER G 32 N VAL G 29
SHEET 1 AA9 7 TYR G 36 ASP G 38 0
SHEET 2 AA9 7 ARG G 72 PRO G 76 -1 O ILE G 75 N TYR G 37
SHEET 3 AA9 7 ALA G 46 LEU G 50 1 N VAL G 47 O ARG G 72
SHEET 4 AA9 7 ILE G 114 HIS G 119 1 O VAL G 117 N LEU G 50
SHEET 5 AA9 7 ILE G 137 MET G 143 1 O VAL G 141 N PHE G 116
SHEET 6 AA9 7 LYS G 252 PRO G 259 1 O LEU G 253 N HIS G 142
SHEET 7 AA9 7 THR G 276 GLY G 283 1 O VAL G 279 N GLU G 256
SHEET 1 AB1 8 LYS H 25 VAL H 29 0
SHEET 2 AB1 8 SER H 32 ASP H 38 -1 O TYR H 36 N LYS H 25
SHEET 3 AB1 8 ARG H 72 PRO H 76 -1 O ILE H 75 N TYR H 37
SHEET 4 AB1 8 ALA H 46 LEU H 50 1 N VAL H 47 O ILE H 74
SHEET 5 AB1 8 ILE H 114 HIS H 119 1 O ILE H 115 N ILE H 48
SHEET 6 AB1 8 ILE H 137 MET H 143 1 O VAL H 141 N GLY H 118
SHEET 7 AB1 8 LYS H 252 PRO H 259 1 O LEU H 253 N ILE H 140
SHEET 8 AB1 8 THR H 276 GLY H 283 1 O VAL H 279 N GLU H 256
SHEET 1 AB213 ILE I 139 MET I 142 0
SHEET 2 AB213 SER I 155 LEU I 166 -1 O LYS I 165 N GLY I 141
SHEET 3 AB213 HIS I 171 SER I 182 -1 O TYR I 180 N VAL I 156
SHEET 4 AB213 PHE I 90 TYR I 98 -1 N ASN I 95 O ARG I 177
SHEET 5 AB213 THR I 103 LEU I 112 -1 O VAL I 106 N ARG I 94
SHEET 6 AB213 PHE I 117 LYS I 126 -1 O ILE I 118 N SER I 111
SHEET 7 AB213 VAL I 11 VAL I 22 1 N ASN I 17 O VAL I 121
SHEET 8 AB213 HIS I 25 ASN I 36 -1 O PHE I 27 N GLY I 20
SHEET 9 AB213 THR I 41 LYS I 50 -1 O THR I 41 N ASN I 36
SHEET 10 AB213 VAL I 211 ALA I 220 -1 O VAL I 211 N ILE I 46
SHEET 11 AB213 TYR I 192 THR I 202 -1 N GLN I 196 O ILE I 218
SHEET 12 AB213 SER I 145 ASN I 152 -1 N MET I 149 O HIS I 193
SHEET 13 AB213 SER I 155 LEU I 166 -1 O SER I 155 N ASN I 152
SHEET 1 AB313 ILE J 139 MET J 142 0
SHEET 2 AB313 SER J 155 LEU J 166 -1 O LYS J 165 N GLY J 141
SHEET 3 AB313 HIS J 171 SER J 182 -1 O MET J 176 N CYS J 160
SHEET 4 AB313 PHE J 90 TYR J 98 -1 N ASN J 95 O ARG J 177
SHEET 5 AB313 THR J 103 GLU J 113 -1 O ALA J 104 N ILE J 96
SHEET 6 AB313 LYS J 116 LYS J 126 -1 O ILE J 118 N SER J 111
SHEET 7 AB313 VAL J 11 VAL J 22 1 N ASN J 17 O VAL J 121
SHEET 8 AB313 HIS J 25 ASN J 36 -1 O GLY J 33 N THR J 14
SHEET 9 AB313 THR J 41 LYS J 50 -1 O LYS J 45 N VAL J 32
SHEET 10 AB313 VAL J 211 ALA J 220 -1 O GLN J 213 N VAL J 44
SHEET 11 AB313 HIS J 193 LYS J 201 -1 N GLN J 196 O ILE J 218
SHEET 12 AB313 SER J 145 ASN J 152 -1 N MET J 149 O HIS J 193
SHEET 13 AB313 SER J 155 LEU J 166 -1 O ILE J 157 N TYR J 150
SHEET 1 AB4 8 LYS K 25 VAL K 29 0
SHEET 2 AB4 8 SER K 32 ASP K 38 -1 O TYR K 36 N LYS K 25
SHEET 3 AB4 8 ARG K 72 PRO K 76 -1 O ILE K 75 N TYR K 37
SHEET 4 AB4 8 ALA K 46 LEU K 50 1 N VAL K 47 O ARG K 72
SHEET 5 AB4 8 ILE K 114 HIS K 119 1 O ILE K 115 N ALA K 46
SHEET 6 AB4 8 ILE K 137 MET K 143 1 O VAL K 141 N PHE K 116
SHEET 7 AB4 8 LYS K 252 PRO K 259 1 O LEU K 253 N ILE K 140
SHEET 8 AB4 8 THR K 276 GLY K 283 1 O GLU K 277 N LYS K 252
SHEET 1 AB5 8 LYS L 25 VAL L 29 0
SHEET 2 AB5 8 SER L 32 ASP L 38 -1 O TYR L 36 N LYS L 25
SHEET 3 AB5 8 ARG L 72 PRO L 76 -1 O ILE L 75 N TYR L 37
SHEET 4 AB5 8 ALA L 46 LEU L 50 1 N VAL L 47 O ARG L 72
SHEET 5 AB5 8 ILE L 114 HIS L 119 1 O VAL L 117 N LEU L 50
SHEET 6 AB5 8 ILE L 137 MET L 143 1 O VAL L 141 N GLY L 118
SHEET 7 AB5 8 LYS L 252 PRO L 259 1 O LEU L 253 N ILE L 140
SHEET 8 AB5 8 THR L 276 GLY L 283 1 O VAL L 279 N GLU L 256
LINK C PHE A 65 N1 CRO A 67 1555 1555 1.43
LINK C3 CRO A 67 N ASN A 68 1555 1555 1.43
LINK C PHE B 65 N1 CRO B 67 1555 1555 1.43
LINK C3 CRO B 67 N ASN B 68 1555 1555 1.43
LINK C PHE E 65 N1 CRO E 67 1555 1555 1.43
LINK C3 CRO E 67 N ASN E 68 1555 1555 1.43
LINK C PHE F 65 N1 CRO F 67 1555 1555 1.50
LINK C3 CRO F 67 N ASN F 68 1555 1555 1.61
LINK C PHE I 65 N1 CRO I 67 1555 1555 1.43
LINK C3 CRO I 67 N ASN I 68 1555 1555 1.43
LINK C PHE J 65 N1 CRO J 67 1555 1555 1.43
LINK C3 CRO J 67 N ASN J 68 1555 1555 1.43
CISPEP 1 ALA A 52 PRO A 53 0 -1.31
CISPEP 2 PHE A 86 PRO A 87 0 15.13
CISPEP 3 LEU A 231 PRO A 232 0 -2.53
CISPEP 4 ALA B 4 LYS B 5 0 -20.56
CISPEP 5 ALA B 52 PRO B 53 0 -1.38
CISPEP 6 PHE B 86 PRO B 87 0 6.49
CISPEP 7 LEU B 231 PRO B 232 0 3.06
CISPEP 8 ASP C 258 PRO C 259 0 -7.31
CISPEP 9 ASP D 258 PRO D 259 0 3.70
CISPEP 10 ALA E 52 PRO E 53 0 -0.31
CISPEP 11 PHE E 86 PRO E 87 0 7.66
CISPEP 12 LEU E 231 PRO E 232 0 -11.46
CISPEP 13 ALA F 52 PRO F 53 0 -2.14
CISPEP 14 PHE F 86 PRO F 87 0 7.77
CISPEP 15 LEU F 231 PRO F 232 0 1.70
CISPEP 16 ASP G 258 PRO G 259 0 -0.92
CISPEP 17 ASP H 258 PRO H 259 0 0.43
CISPEP 18 ALA I 52 PRO I 53 0 -0.72
CISPEP 19 PHE I 86 PRO I 87 0 7.27
CISPEP 20 ALA J 52 PRO J 53 0 -2.08
CISPEP 21 PHE J 86 PRO J 87 0 2.99
CISPEP 22 LEU J 231 PRO J 232 0 4.72
CISPEP 23 ASP K 258 PRO K 259 0 -1.19
CISPEP 24 ASP L 258 PRO L 259 0 -2.40
CRYST1 96.875 96.875 361.461 90.00 90.00 120.00 P 32 18
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 0.010323 0.005960 0.000000 0.00000
SCALE2 0.000000 0.011919 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002767 0.00000
TER 1821 PRO A 232
TER 3650 PRO B 232
TER 6161 ASN C 309
TER 8694 GLU D 310
TER 10516 PRO E 232
TER 12321 PRO F 232
TER 14873 GLY G 313
TER 17397 ASN H 309
TER 19188 PRO I 232
TER 21009 PRO J 232
TER 23525 LYS K 308
TER 26049 ASN L 309
MASTER 493 0 7 127 131 0 0 626430 12 169 258
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