| content |
HEADER HYDROLASE 13-FEB-24 8RZZ
TITLE CRYSTAL STRUCTURE OF RENILLA LUCIFERASE RLUC8-GFP BRET COMPLEX AT PH
TITLE 2 9.0 (SPACE GROUP P32)
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,
KEYWDS 2 COELENTERAMIDE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.MAREK,A.SMRCKOVA
REVDAT 1 03-SEP-25 8RZZ 0
JRNL AUTH M.MAREK,A.SMRCKOVA
JRNL TITL CRYSTAL STRUCTURE OF RENILLA LUCIFERASE RLUC8-GFP BRET
JRNL TITL 2 COMPLEX AT PH 9.0 (SPACE GROUP P32)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.30 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 : TWIN_LSQ_F
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.17
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 217.79
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 172762
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.249
REMARK 3 R VALUE (WORKING SET) : 0.227
REMARK 3 FREE R VALUE : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.910
REMARK 3 FREE R VALUE TEST SET COUNT : 8477
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 31.9520 - 6.2285 0.95 8208 452 0.2087 0.2325
REMARK 3 2 6.2285 - 4.9497 0.95 8198 421 0.2005 0.2265
REMARK 3 3 4.9497 - 4.3257 0.95 8182 448 0.1870 0.2105
REMARK 3 4 4.3257 - 3.9310 0.95 8171 420 0.2045 0.2456
REMARK 3 5 3.9310 - 3.6497 0.96 8258 380 0.2276 0.2453
REMARK 3 6 3.6497 - 3.4348 0.95 8239 449 0.2426 0.2598
REMARK 3 7 3.4348 - 3.2629 0.95 8150 405 0.2481 0.3041
REMARK 3 8 3.2629 - 3.1210 0.95 8243 434 0.2636 0.3015
REMARK 3 9 3.1210 - 3.0010 0.94 8156 494 0.2733 0.3141
REMARK 3 10 3.0010 - 2.8975 0.95 8189 413 0.2944 0.3353
REMARK 3 11 2.8975 - 2.8069 0.95 8205 428 0.3080 0.3591
REMARK 3 12 2.8069 - 2.7267 0.95 8221 414 0.3095 0.3500
REMARK 3 13 2.7267 - 2.6550 0.95 8182 434 0.3176 0.3902
REMARK 3 14 2.6550 - 2.5902 0.96 8257 376 0.3316 0.3722
REMARK 3 15 2.5902 - 2.5314 0.95 8203 428 0.3317 0.3712
REMARK 3 16 2.5314 - 2.4775 0.96 8361 348 0.3363 0.3892
REMARK 3 17 2.4775 - 2.4280 0.95 8183 458 0.3440 0.3630
REMARK 3 18 2.4280 - 2.3822 0.95 8176 404 0.3416 0.3898
REMARK 3 19 2.3822 - 2.3397 0.95 8127 456 0.3461 0.3839
REMARK 3 20 2.3397 - 2.3000 0.95 8273 414 0.3521 0.4086
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) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 41.340
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 : 0.002 27017
REMARK 3 ANGLE : 0.563 36523
REMARK 3 CHIRALITY : 0.045 3878
REMARK 3 PLANARITY : 0.004 4666
REMARK 3 DIHEDRAL : 4.589 18380
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 8RZZ 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_1292136554.
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 : 9
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 : 172869
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.299
REMARK 200 RESOLUTION RANGE LOW (A) : 49.172
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 10.40
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.42
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 (%): 53.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: T-MATE, BICINE, PEG SMEAR HIGH,
REMARK 280 ETHYLENE GLYCOL, PH 9, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 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 241.33067
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 120.66533
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8990 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -45.0 KCAL/MOL
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -59.0 KCAL/MOL
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40350 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 KCAL/MOL
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 ASP A 2
REMARK 465 MET B 1
REMARK 465 MET C 1
REMARK 465 ASN C 309
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 SER D 322
REMARK 465 GLY D 323
REMARK 465 LEU D 324
REMARK 465 GLU D 325
REMARK 465 VAL D 326
REMARK 465 LEU D 327
REMARK 465 PHE D 328
REMARK 465 GLN D 329
REMARK 465 MET F 1
REMARK 465 MET G 1
REMARK 465 ASN G 309
REMARK 465 GLU G 310
REMARK 465 GLN G 311
REMARK 465 SER G 312
REMARK 465 GLY G 313
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 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 SER L 322
REMARK 465 GLY L 323
REMARK 465 LEU L 324
REMARK 465 GLU L 325
REMARK 465 VAL L 326
REMARK 465 LEU L 327
REMARK 465 PHE L 328
REMARK 465 GLN L 329
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 66 CG1
REMARK 470 CRO B 66 CG1
REMARK 470 CRO E 66 CG1
REMARK 470 CRO F 66 CG1
REMARK 470 CRO I 66 CG1
REMARK 470 CRO J 66 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 O ILE I 226 OG SER I 229 2.11
REMARK 500 O ILE C 15 OH TYR C 58 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 ASP H 135 CA ASP H 135 CB 0.161
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 GLU D 320 C - N - CA ANGL. DEV. = 18.3 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 30.10 -85.05
REMARK 500 GLU A 112 -91.04 -124.25
REMARK 500 VAL A 152 -102.42 56.92
REMARK 500 GLU A 186 -75.78 -58.89
REMARK 500 LEU A 190 -95.86 -83.55
REMARK 500 THR A 205 -73.78 -44.17
REMARK 500 ALA A 206 -131.75 54.68
REMARK 500 ASP B 59 -8.49 -57.65
REMARK 500 GLN B 98 35.37 -70.23
REMARK 500 ASP B 113 -75.89 56.16
REMARK 500 VAL B 152 -107.74 54.49
REMARK 500 VAL B 185 133.16 47.73
REMARK 500 GLU B 186 -73.74 -69.32
REMARK 500 ASP B 204 21.32 -78.87
REMARK 500 ALA B 206 85.40 -59.51
REMARK 500 LEU B 230 -71.03 -64.69
REMARK 500 GLN C 10 -31.62 -133.70
REMARK 500 LEU C 30 -128.56 56.47
REMARK 500 GLU C 40 -54.75 67.66
REMARK 500 ALA C 54 6.76 59.62
REMARK 500 THR C 55 -169.56 -124.26
REMARK 500 PRO C 69 7.07 -69.23
REMARK 500 LEU C 107 46.55 -104.86
REMARK 500 PRO C 111 -178.84 -65.93
REMARK 500 ASP C 120 -133.57 59.50
REMARK 500 HIS C 133 59.65 -112.91
REMARK 500 VAL C 146 76.39 -116.44
REMARK 500 ASP C 148 -169.08 60.32
REMARK 500 SER C 152 -44.75 -135.06
REMARK 500 ASP C 158 62.39 -69.06
REMARK 500 GLU C 161 -46.32 66.36
REMARK 500 THR C 184 -56.83 -124.27
REMARK 500 LYS C 189 31.76 -86.35
REMARK 500 LEU C 284 -113.80 -105.75
REMARK 500 SER D 3 -74.38 -88.65
REMARK 500 LYS D 4 156.79 66.03
REMARK 500 LEU D 30 -128.93 59.03
REMARK 500 GLU D 40 -67.08 57.39
REMARK 500 ALA D 54 -0.87 69.04
REMARK 500 THR D 55 -162.72 -122.09
REMARK 500 ASP D 120 -134.50 59.60
REMARK 500 VAL D 146 71.32 -105.43
REMARK 500 ASP D 154 -84.40 -61.46
REMARK 500 GLU D 161 -45.41 66.42
REMARK 500 GLU D 169 -51.50 59.45
REMARK 500 LYS D 189 30.18 -86.87
REMARK 500 PHE D 261 -56.55 -126.02
REMARK 500 LEU D 284 -113.28 -103.24
REMARK 500 GLU D 320 59.64 -166.21
REMARK 500 GLU E 112 -110.29 -119.00
REMARK 500
REMARK 500 THIS ENTRY HAS 131 RAMACHANDRAN OUTLIERS.
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 F 443 DISTANCE = 5.94 ANGSTROMS
DBREF 8RZZ A 1 231 UNP Q963I9 Q963I9_RENRE 1 233
DBREF 8RZZ B 1 231 UNP Q963I9 Q963I9_RENRE 1 233
DBREF 8RZZ C 1 311 UNP P27652 LUCI_RENRE 1 311
DBREF 8RZZ D 1 321 UNP P27652 LUCI_RENRE 1 311
DBREF 8RZZ E 1 231 UNP Q963I9 Q963I9_RENRE 1 233
DBREF 8RZZ F 1 231 UNP Q963I9 Q963I9_RENRE 1 233
DBREF 8RZZ G 1 311 UNP P27652 LUCI_RENRE 1 311
DBREF 8RZZ H 1 311 UNP P27652 LUCI_RENRE 1 311
DBREF 8RZZ I 1 231 UNP Q963I9 Q963I9_RENRE 1 233
DBREF 8RZZ J 1 231 UNP Q963I9 Q963I9_RENRE 1 233
DBREF 8RZZ K 1 311 UNP P27652 LUCI_RENRE 1 311
DBREF 8RZZ L 1 321 UNP P27652 LUCI_RENRE 1 311
SEQADV 8RZZ CRO A 66 UNP Q963I9 SER 66 CHROMOPHORE
SEQADV 8RZZ CRO A 66 UNP Q963I9 TYR 67 CHROMOPHORE
SEQADV 8RZZ CRO A 66 UNP Q963I9 GLY 68 CHROMOPHORE
SEQADV 8RZZ CRO B 66 UNP Q963I9 SER 66 CHROMOPHORE
SEQADV 8RZZ CRO B 66 UNP Q963I9 TYR 67 CHROMOPHORE
SEQADV 8RZZ CRO B 66 UNP Q963I9 GLY 68 CHROMOPHORE
SEQADV 8RZZ THR C 55 UNP P27652 ALA 55 ENGINEERED MUTATION
SEQADV 8RZZ ALA C 124 UNP P27652 CYS 124 ENGINEERED MUTATION
SEQADV 8RZZ ALA C 130 UNP P27652 SER 130 ENGINEERED MUTATION
SEQADV 8RZZ ARG C 136 UNP P27652 LYS 136 ENGINEERED MUTATION
SEQADV 8RZZ MET C 143 UNP P27652 ALA 143 ENGINEERED MUTATION
SEQADV 8RZZ VAL C 185 UNP P27652 MET 185 ENGINEERED MUTATION
SEQADV 8RZZ LEU C 253 UNP P27652 MET 253 ENGINEERED MUTATION
SEQADV 8RZZ LEU C 287 UNP P27652 SER 287 ENGINEERED MUTATION
SEQADV 8RZZ SER C 312 UNP P27652 EXPRESSION TAG
SEQADV 8RZZ GLY C 313 UNP P27652 EXPRESSION TAG
SEQADV 8RZZ LEU C 314 UNP P27652 EXPRESSION TAG
SEQADV 8RZZ GLU C 315 UNP P27652 EXPRESSION TAG
SEQADV 8RZZ VAL C 316 UNP P27652 EXPRESSION TAG
SEQADV 8RZZ LEU C 317 UNP P27652 EXPRESSION TAG
SEQADV 8RZZ PHE C 318 UNP P27652 EXPRESSION TAG
SEQADV 8RZZ GLN C 319 UNP P27652 EXPRESSION TAG
SEQADV 8RZZ THR D 55 UNP P27652 ALA 55 ENGINEERED MUTATION
SEQADV 8RZZ ALA D 124 UNP P27652 CYS 124 ENGINEERED MUTATION
SEQADV 8RZZ ALA D 130 UNP P27652 SER 130 ENGINEERED MUTATION
SEQADV 8RZZ ARG D 136 UNP P27652 LYS 136 ENGINEERED MUTATION
SEQADV 8RZZ MET D 143 UNP P27652 ALA 143 ENGINEERED MUTATION
SEQADV 8RZZ VAL D 185 UNP P27652 MET 185 ENGINEERED MUTATION
SEQADV 8RZZ LEU D 253 UNP P27652 MET 253 ENGINEERED MUTATION
SEQADV 8RZZ LEU D 287 UNP P27652 SER 287 ENGINEERED MUTATION
SEQADV 8RZZ SER D 322 UNP P27652 EXPRESSION TAG
SEQADV 8RZZ GLY D 323 UNP P27652 EXPRESSION TAG
SEQADV 8RZZ LEU D 324 UNP P27652 EXPRESSION TAG
SEQADV 8RZZ GLU D 325 UNP P27652 EXPRESSION TAG
SEQADV 8RZZ VAL D 326 UNP P27652 EXPRESSION TAG
SEQADV 8RZZ LEU D 327 UNP P27652 EXPRESSION TAG
SEQADV 8RZZ PHE D 328 UNP P27652 EXPRESSION TAG
SEQADV 8RZZ GLN D 329 UNP P27652 EXPRESSION TAG
SEQADV 8RZZ CRO E 66 UNP Q963I9 SER 66 CHROMOPHORE
SEQADV 8RZZ CRO E 66 UNP Q963I9 TYR 67 CHROMOPHORE
SEQADV 8RZZ CRO E 66 UNP Q963I9 GLY 68 CHROMOPHORE
SEQADV 8RZZ CRO F 66 UNP Q963I9 SER 66 CHROMOPHORE
SEQADV 8RZZ CRO F 66 UNP Q963I9 TYR 67 CHROMOPHORE
SEQADV 8RZZ CRO F 66 UNP Q963I9 GLY 68 CHROMOPHORE
SEQADV 8RZZ THR G 55 UNP P27652 ALA 55 ENGINEERED MUTATION
SEQADV 8RZZ ALA G 124 UNP P27652 CYS 124 ENGINEERED MUTATION
SEQADV 8RZZ ALA G 130 UNP P27652 SER 130 ENGINEERED MUTATION
SEQADV 8RZZ ARG G 136 UNP P27652 LYS 136 ENGINEERED MUTATION
SEQADV 8RZZ MET G 143 UNP P27652 ALA 143 ENGINEERED MUTATION
SEQADV 8RZZ VAL G 185 UNP P27652 MET 185 ENGINEERED MUTATION
SEQADV 8RZZ LEU G 253 UNP P27652 MET 253 ENGINEERED MUTATION
SEQADV 8RZZ LEU G 287 UNP P27652 SER 287 ENGINEERED MUTATION
SEQADV 8RZZ SER G 312 UNP P27652 EXPRESSION TAG
SEQADV 8RZZ GLY G 313 UNP P27652 EXPRESSION TAG
SEQADV 8RZZ LEU G 314 UNP P27652 EXPRESSION TAG
SEQADV 8RZZ GLU G 315 UNP P27652 EXPRESSION TAG
SEQADV 8RZZ VAL G 316 UNP P27652 EXPRESSION TAG
SEQADV 8RZZ LEU G 317 UNP P27652 EXPRESSION TAG
SEQADV 8RZZ PHE G 318 UNP P27652 EXPRESSION TAG
SEQADV 8RZZ GLN G 319 UNP P27652 EXPRESSION TAG
SEQADV 8RZZ THR H 55 UNP P27652 ALA 55 ENGINEERED MUTATION
SEQADV 8RZZ ALA H 124 UNP P27652 CYS 124 ENGINEERED MUTATION
SEQADV 8RZZ ALA H 130 UNP P27652 SER 130 ENGINEERED MUTATION
SEQADV 8RZZ ARG H 136 UNP P27652 LYS 136 ENGINEERED MUTATION
SEQADV 8RZZ MET H 143 UNP P27652 ALA 143 ENGINEERED MUTATION
SEQADV 8RZZ VAL H 185 UNP P27652 MET 185 ENGINEERED MUTATION
SEQADV 8RZZ LEU H 253 UNP P27652 MET 253 ENGINEERED MUTATION
SEQADV 8RZZ LEU H 287 UNP P27652 SER 287 ENGINEERED MUTATION
SEQADV 8RZZ SER H 312 UNP P27652 EXPRESSION TAG
SEQADV 8RZZ GLY H 313 UNP P27652 EXPRESSION TAG
SEQADV 8RZZ LEU H 314 UNP P27652 EXPRESSION TAG
SEQADV 8RZZ GLU H 315 UNP P27652 EXPRESSION TAG
SEQADV 8RZZ VAL H 316 UNP P27652 EXPRESSION TAG
SEQADV 8RZZ LEU H 317 UNP P27652 EXPRESSION TAG
SEQADV 8RZZ PHE H 318 UNP P27652 EXPRESSION TAG
SEQADV 8RZZ GLN H 319 UNP P27652 EXPRESSION TAG
SEQADV 8RZZ CRO I 66 UNP Q963I9 SER 66 CHROMOPHORE
SEQADV 8RZZ CRO I 66 UNP Q963I9 TYR 67 CHROMOPHORE
SEQADV 8RZZ CRO I 66 UNP Q963I9 GLY 68 CHROMOPHORE
SEQADV 8RZZ CRO J 66 UNP Q963I9 SER 66 CHROMOPHORE
SEQADV 8RZZ CRO J 66 UNP Q963I9 TYR 67 CHROMOPHORE
SEQADV 8RZZ CRO J 66 UNP Q963I9 GLY 68 CHROMOPHORE
SEQADV 8RZZ THR K 55 UNP P27652 ALA 55 ENGINEERED MUTATION
SEQADV 8RZZ ALA K 124 UNP P27652 CYS 124 ENGINEERED MUTATION
SEQADV 8RZZ ALA K 130 UNP P27652 SER 130 ENGINEERED MUTATION
SEQADV 8RZZ ARG K 136 UNP P27652 LYS 136 ENGINEERED MUTATION
SEQADV 8RZZ MET K 143 UNP P27652 ALA 143 ENGINEERED MUTATION
SEQADV 8RZZ VAL K 185 UNP P27652 MET 185 ENGINEERED MUTATION
SEQADV 8RZZ LEU K 253 UNP P27652 MET 253 ENGINEERED MUTATION
SEQADV 8RZZ LEU K 287 UNP P27652 SER 287 ENGINEERED MUTATION
SEQADV 8RZZ SER K 312 UNP P27652 EXPRESSION TAG
SEQADV 8RZZ GLY K 313 UNP P27652 EXPRESSION TAG
SEQADV 8RZZ LEU K 314 UNP P27652 EXPRESSION TAG
SEQADV 8RZZ GLU K 315 UNP P27652 EXPRESSION TAG
SEQADV 8RZZ VAL K 316 UNP P27652 EXPRESSION TAG
SEQADV 8RZZ LEU K 317 UNP P27652 EXPRESSION TAG
SEQADV 8RZZ PHE K 318 UNP P27652 EXPRESSION TAG
SEQADV 8RZZ GLN K 319 UNP P27652 EXPRESSION TAG
SEQADV 8RZZ THR L 55 UNP P27652 ALA 55 ENGINEERED MUTATION
SEQADV 8RZZ ALA L 124 UNP P27652 CYS 124 ENGINEERED MUTATION
SEQADV 8RZZ ALA L 130 UNP P27652 SER 130 ENGINEERED MUTATION
SEQADV 8RZZ ARG L 136 UNP P27652 LYS 136 ENGINEERED MUTATION
SEQADV 8RZZ MET L 143 UNP P27652 ALA 143 ENGINEERED MUTATION
SEQADV 8RZZ VAL L 185 UNP P27652 MET 185 ENGINEERED MUTATION
SEQADV 8RZZ LEU L 253 UNP P27652 MET 253 ENGINEERED MUTATION
SEQADV 8RZZ LEU L 287 UNP P27652 SER 287 ENGINEERED MUTATION
SEQADV 8RZZ SER L 322 UNP P27652 EXPRESSION TAG
SEQADV 8RZZ GLY L 323 UNP P27652 EXPRESSION TAG
SEQADV 8RZZ LEU L 324 UNP P27652 EXPRESSION TAG
SEQADV 8RZZ GLU L 325 UNP P27652 EXPRESSION TAG
SEQADV 8RZZ VAL L 326 UNP P27652 EXPRESSION TAG
SEQADV 8RZZ LEU L 327 UNP P27652 EXPRESSION TAG
SEQADV 8RZZ PHE L 328 UNP P27652 EXPRESSION TAG
SEQADV 8RZZ GLN L 329 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 8RZZ CRO A 66 SER CHROMOPHORE
MODRES 8RZZ CRO A 66 TYR CHROMOPHORE
MODRES 8RZZ CRO A 66 GLY CHROMOPHORE
MODRES 8RZZ CRO B 66 SER CHROMOPHORE
MODRES 8RZZ CRO B 66 TYR CHROMOPHORE
MODRES 8RZZ CRO B 66 GLY CHROMOPHORE
MODRES 8RZZ CRO E 66 SER CHROMOPHORE
MODRES 8RZZ CRO E 66 TYR CHROMOPHORE
MODRES 8RZZ CRO E 66 GLY CHROMOPHORE
MODRES 8RZZ CRO F 66 SER CHROMOPHORE
MODRES 8RZZ CRO F 66 TYR CHROMOPHORE
MODRES 8RZZ CRO F 66 GLY CHROMOPHORE
MODRES 8RZZ CRO I 66 SER CHROMOPHORE
MODRES 8RZZ CRO I 66 TYR CHROMOPHORE
MODRES 8RZZ CRO I 66 GLY CHROMOPHORE
MODRES 8RZZ CRO J 66 SER CHROMOPHORE
MODRES 8RZZ CRO J 66 TYR CHROMOPHORE
MODRES 8RZZ CRO J 66 GLY CHROMOPHORE
HET CRO A 66 21
HET CRO B 66 21
HET CRO E 66 21
HET CRO F 66 21
HET CRO I 66 21
HET CRO J 66 21
HET CEI D 401 31
HET CEI G 401 31
HET CEI H 401 31
HET CEI K 401 31
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 5(C25 H21 N3 O3)
FORMUL 18 HOH *647(H2 O)
HELIX 1 AA1 LEU A 3 GLY A 7 5 5
HELIX 2 AA2 ALA A 57 SER A 62 5 6
HELIX 3 AA3 ASP A 79 SER A 84 1 6
HELIX 4 AA4 ALA B 57 SER B 62 5 6
HELIX 5 AA5 ASP B 79 SER B 84 1 6
HELIX 6 AA6 GLN C 10 MET C 14 5 5
HELIX 7 AA7 THR C 16 ALA C 22 1 7
HELIX 8 AA8 SER C 56 ARG C 61 5 6
HELIX 9 AA9 VAL C 63 ILE C 67 5 5
HELIX 10 AB1 ARG C 93 LEU C 107 1 15
HELIX 11 AB2 ASP C 120 HIS C 133 1 14
HELIX 12 AB3 GLU C 161 SER C 168 1 8
HELIX 13 AB4 GLU C 169 LEU C 176 1 8
HELIX 14 AB5 ASN C 179 THR C 184 1 6
HELIX 15 AB6 THR C 184 LYS C 189 1 6
HELIX 16 AB7 GLU C 195 GLU C 204 1 10
HELIX 17 AB8 PRO C 205 LYS C 207 5 3
HELIX 18 AB9 GLY C 210 VAL C 212 5 3
HELIX 19 AC1 ARG C 213 TRP C 219 1 7
HELIX 20 AC2 PRO C 220 ILE C 223 5 4
HELIX 21 AC3 LYS C 230 ARG C 245 1 16
HELIX 22 AC4 PHE C 262 LYS C 271 1 10
HELIX 23 AC5 ALA C 291 LYS C 308 1 18
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 ILE D 67 5 5
HELIX 28 AD1 ARG D 93 GLU D 106 1 14
HELIX 29 AD2 ASP D 120 HIS D 133 1 14
HELIX 30 AD3 GLU D 161 SER D 168 1 8
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 GLU D 222 1 10
HELIX 38 AE2 LYS D 230 ALA D 246 1 17
HELIX 39 AE3 PHE D 262 LYS D 272 1 11
HELIX 40 AE4 PHE D 286 ASP D 290 5 5
HELIX 41 AE5 ALA D 291 LYS D 308 1 18
HELIX 42 AE6 ALA E 57 SER E 62 5 6
HELIX 43 AE7 ASP E 79 SER E 84 1 6
HELIX 44 AE8 GLY E 131 GLN E 136 1 6
HELIX 45 AE9 ASP F 2 GLY F 7 5 6
HELIX 46 AF1 ALA F 57 SER F 62 5 6
HELIX 47 AF2 PHE F 81 PHE F 85 5 5
HELIX 48 AF3 GLN G 10 MET G 14 5 5
HELIX 49 AF4 THR G 16 ALA G 22 1 7
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 GLU G 106 1 14
HELIX 53 AF8 ASP G 120 HIS G 133 1 14
HELIX 54 AF9 ILE G 159 LYS G 167 1 9
HELIX 55 AG1 GLU G 169 VAL G 175 1 7
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 ALA G 246 1 17
HELIX 64 AH1 PHE G 262 LYS G 271 1 10
HELIX 65 AH2 PHE G 286 ASP G 290 5 5
HELIX 66 AH3 ALA G 291 LEU G 307 1 17
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 108 1 16
HELIX 72 AH9 ASP H 120 HIS H 133 1 14
HELIX 73 AI1 GLU H 161 LYS H 167 1 7
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 GLU H 222 1 10
HELIX 81 AI9 LYS H 230 ALA H 246 1 17
HELIX 82 AJ1 PHE H 262 LYS H 271 1 10
HELIX 83 AJ2 PHE H 286 ASP H 290 5 5
HELIX 84 AJ3 ALA H 291 LEU H 307 1 17
HELIX 85 AJ4 ALA I 57 SER I 62 5 6
HELIX 86 AJ5 ALA J 57 SER J 62 5 6
HELIX 87 AJ6 THR K 16 ALA K 22 1 7
HELIX 88 AJ7 SER K 56 ARG K 61 5 6
HELIX 89 AJ8 VAL K 63 ILE K 67 5 5
HELIX 90 AJ9 ARG K 93 GLU K 106 1 14
HELIX 91 AK1 ASP K 120 HIS K 133 1 14
HELIX 92 AK2 GLU K 161 LYS K 167 1 7
HELIX 93 AK3 GLU K 169 LEU K 176 1 8
HELIX 94 AK4 ASN K 179 THR K 184 1 6
HELIX 95 AK5 THR K 184 LYS K 189 1 6
HELIX 96 AK6 GLU K 195 GLU K 204 1 10
HELIX 97 AK7 PRO K 205 LYS K 207 5 3
HELIX 98 AK8 GLY K 210 VAL K 212 5 3
HELIX 99 AK9 ARG K 213 TRP K 219 1 7
HELIX 100 AL1 PRO K 220 ILE K 223 5 4
HELIX 101 AL2 LYS K 230 ALA K 246 1 17
HELIX 102 AL3 PHE K 262 LYS K 272 1 11
HELIX 103 AL4 PHE K 286 ASP K 290 5 5
HELIX 104 AL5 ALA K 291 LEU K 307 1 17
HELIX 105 AL6 GLN L 10 MET L 14 5 5
HELIX 106 AL7 THR L 16 ALA L 22 1 7
HELIX 107 AL8 SER L 56 ARG L 61 5 6
HELIX 108 AL9 VAL L 63 ILE L 67 5 5
HELIX 109 AM1 ARG L 93 GLU L 106 1 14
HELIX 110 AM2 ASP L 120 HIS L 133 1 14
HELIX 111 AM3 GLU L 161 LYS L 167 1 7
HELIX 112 AM4 GLU L 169 VAL L 175 1 7
HELIX 113 AM5 ASN L 179 THR L 184 1 6
HELIX 114 AM6 THR L 184 LYS L 189 1 6
HELIX 115 AM7 GLU L 195 GLU L 204 1 10
HELIX 116 AM8 PRO L 205 LYS L 207 5 3
HELIX 117 AM9 GLY L 210 VAL L 212 5 3
HELIX 118 AN1 ARG L 213 TRP L 219 1 7
HELIX 119 AN2 PRO L 220 ILE L 223 5 4
HELIX 120 AN3 LYS L 230 ALA L 246 1 17
HELIX 121 AN4 PHE L 262 LYS L 271 1 10
HELIX 122 AN5 ALA L 291 GLU L 320 1 20
SHEET 1 AA113 ILE A 138 MET A 141 0
SHEET 2 AA113 SER A 154 LEU A 165 -1 O LYS A 164 N VAL A 139
SHEET 3 AA113 HIS A 170 SER A 181 -1 O TYR A 179 N VAL A 155
SHEET 4 AA113 PHE A 89 TYR A 97 -1 N ASN A 94 O ARG A 176
SHEET 5 AA113 THR A 102 LEU A 111 -1 O ALA A 103 N ILE A 95
SHEET 6 AA113 PHE A 116 LYS A 125 -1 O ILE A 117 N SER A 110
SHEET 7 AA113 VAL A 11 VAL A 22 1 N ASN A 17 O VAL A 120
SHEET 8 AA113 HIS A 25 ASN A 36 -1 O GLY A 35 N MET A 12
SHEET 9 AA113 THR A 41 LYS A 50 -1 O LYS A 45 N VAL A 32
SHEET 10 AA113 VAL A 210 ALA A 219 -1 O GLN A 212 N VAL A 44
SHEET 11 AA113 TYR A 191 THR A 201 -1 N PHE A 193 O ALA A 219
SHEET 12 AA113 SER A 144 ASN A 151 -1 N MET A 148 O HIS A 192
SHEET 13 AA113 SER A 154 LEU A 165 -1 O GLU A 158 N SER A 147
SHEET 1 AA213 ILE B 138 MET B 141 0
SHEET 2 AA213 SER B 154 LEU B 165 -1 O LYS B 164 N VAL B 139
SHEET 3 AA213 HIS B 170 SER B 181 -1 O TYR B 179 N VAL B 155
SHEET 4 AA213 PHE B 89 TYR B 97 -1 N ASN B 94 O ARG B 176
SHEET 5 AA213 THR B 102 GLU B 112 -1 O ALA B 103 N ILE B 95
SHEET 6 AA213 LYS B 115 LYS B 125 -1 O LYS B 115 N GLU B 112
SHEET 7 AA213 VAL B 11 VAL B 22 1 N PRO B 13 O PHE B 116
SHEET 8 AA213 HIS B 25 ASN B 36 -1 O GLY B 35 N MET B 12
SHEET 9 AA213 THR B 41 LYS B 50 -1 O SER B 47 N GLU B 30
SHEET 10 AA213 VAL B 210 ALA B 219 -1 O VAL B 210 N ILE B 46
SHEET 11 AA213 HIS B 192 LYS B 200 -1 N GLN B 195 O ILE B 217
SHEET 12 AA213 SER B 144 ASN B 151 -1 N MET B 148 O HIS B 192
SHEET 13 AA213 SER B 154 LEU B 165 -1 O SER B 154 N ASN B 151
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 LEU C 50
SHEET 6 AA3 8 ILE C 137 MET C 143 1 O LYS C 138 N ILE C 114
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 GLU C 256
SHEET 1 AA4 2 ASN D 28 VAL D 29 0
SHEET 2 AA4 2 SER D 32 PHE D 33 -1 O SER D 32 N VAL D 29
SHEET 1 AA5 7 TYR D 36 ASP D 38 0
SHEET 2 AA5 7 ARG D 72 PRO D 76 -1 O ILE D 75 N TYR D 37
SHEET 3 AA5 7 ALA D 46 LEU D 50 1 N VAL D 47 O ARG D 72
SHEET 4 AA5 7 ILE D 114 HIS D 119 1 O ILE D 115 N ILE D 48
SHEET 5 AA5 7 ILE D 137 MET D 143 1 O VAL D 141 N PHE D 116
SHEET 6 AA5 7 LYS D 252 PRO D 259 1 O LEU D 253 N ILE D 140
SHEET 7 AA5 7 THR D 276 GLY D 283 1 O VAL D 279 N GLU D 256
SHEET 1 AA613 ILE E 138 MET E 141 0
SHEET 2 AA613 SER E 154 LEU E 165 -1 O LYS E 164 N VAL E 139
SHEET 3 AA613 HIS E 170 SER E 181 -1 O PHE E 171 N PHE E 163
SHEET 4 AA613 PHE E 89 TYR E 97 -1 N ASN E 94 O ARG E 176
SHEET 5 AA613 THR E 102 LEU E 111 -1 O VAL E 105 N ARG E 93
SHEET 6 AA613 PHE E 116 LYS E 125 -1 O LYS E 125 N THR E 102
SHEET 7 AA613 VAL E 11 VAL E 22 1 N ASN E 17 O VAL E 120
SHEET 8 AA613 HIS E 25 ASN E 36 -1 O GLY E 31 N ILE E 16
SHEET 9 AA613 THR E 41 LYS E 50 -1 O LYS E 45 N VAL E 32
SHEET 10 AA613 VAL E 210 ALA E 219 -1 O VAL E 210 N ILE E 46
SHEET 11 AA613 HIS E 192 LYS E 200 -1 N GLN E 195 O ILE E 217
SHEET 12 AA613 SER E 144 ASN E 151 -1 N MET E 148 O HIS E 192
SHEET 13 AA613 SER E 154 LEU E 165 -1 O SER E 154 N ASN E 151
SHEET 1 AA713 ILE F 138 MET F 141 0
SHEET 2 AA713 SER F 154 LEU F 165 -1 O LYS F 164 N VAL F 139
SHEET 3 AA713 HIS F 170 SER F 181 -1 O TYR F 179 N VAL F 155
SHEET 4 AA713 GLY F 88 TYR F 97 -1 N ASN F 94 O ARG F 176
SHEET 5 AA713 THR F 102 GLU F 112 -1 O ALA F 103 N ILE F 95
SHEET 6 AA713 LYS F 115 LYS F 125 -1 O ILE F 117 N SER F 110
SHEET 7 AA713 VAL F 11 VAL F 22 1 N PRO F 13 O PHE F 116
SHEET 8 AA713 HIS F 25 ASN F 36 -1 O GLY F 35 N MET F 12
SHEET 9 AA713 THR F 41 LYS F 50 -1 O SER F 47 N GLU F 30
SHEET 10 AA713 VAL F 210 ALA F 219 -1 O VAL F 210 N ILE F 46
SHEET 11 AA713 HIS F 192 LYS F 200 -1 N GLN F 195 O ILE F 217
SHEET 12 AA713 SER F 144 ASN F 151 -1 N GLU F 146 O ILE F 194
SHEET 13 AA713 SER F 154 LEU F 165 -1 O ILE F 156 N TYR F 149
SHEET 1 AA8 8 LYS G 25 VAL G 29 0
SHEET 2 AA8 8 SER G 32 ASP G 38 -1 O TYR G 36 N LYS G 25
SHEET 3 AA8 8 ARG G 72 PRO G 76 -1 O ILE G 75 N TYR G 37
SHEET 4 AA8 8 ALA G 46 LEU G 50 1 N VAL G 47 O ARG G 72
SHEET 5 AA8 8 ILE G 114 HIS G 119 1 O ILE G 115 N ILE G 48
SHEET 6 AA8 8 ILE G 137 MET G 143 1 O VAL G 141 N PHE G 116
SHEET 7 AA8 8 LYS G 252 PRO G 259 1 O LEU G 253 N HIS G 142
SHEET 8 AA8 8 THR G 276 GLY G 283 1 O VAL G 279 N GLU G 256
SHEET 1 AA9 8 LYS H 25 VAL H 29 0
SHEET 2 AA9 8 SER H 32 ASP H 38 -1 O TYR H 36 N LYS H 25
SHEET 3 AA9 8 ARG H 72 PRO H 76 -1 O ILE H 75 N TYR H 37
SHEET 4 AA9 8 ALA H 46 LEU H 50 1 N VAL H 47 O ARG H 72
SHEET 5 AA9 8 ILE H 114 HIS H 119 1 O ILE H 115 N ALA H 46
SHEET 6 AA9 8 ILE H 137 MET H 143 1 O VAL H 141 N PHE H 116
SHEET 7 AA9 8 LYS H 252 PRO H 259 1 O LEU H 253 N HIS H 142
SHEET 8 AA9 8 THR H 276 GLY H 283 1 O VAL H 279 N GLU H 256
SHEET 1 AB1 5 ILE I 138 MET I 141 0
SHEET 2 AB1 5 SER I 154 LEU I 165 -1 O LYS I 164 N VAL I 139
SHEET 3 AB1 5 SER I 144 ASN I 151 -1 N TYR I 149 O ILE I 156
SHEET 4 AB1 5 TYR I 191 THR I 201 -1 O HIS I 192 N MET I 148
SHEET 5 AB1 5 SER J 229 LEU J 230 -1 O LEU J 230 N LYS I 200
SHEET 1 AB212 ILE I 138 MET I 141 0
SHEET 2 AB212 SER I 154 LEU I 165 -1 O LYS I 164 N VAL I 139
SHEET 3 AB212 HIS I 170 SER I 181 -1 O TYR I 179 N VAL I 155
SHEET 4 AB212 PHE I 89 TYR I 97 -1 N THR I 90 O LYS I 180
SHEET 5 AB212 THR I 102 LEU I 111 -1 O SER I 107 N TYR I 91
SHEET 6 AB212 PHE I 116 LYS I 125 -1 O ASN I 119 N ASP I 108
SHEET 7 AB212 VAL I 11 VAL I 22 1 N PRO I 13 O PHE I 116
SHEET 8 AB212 HIS I 25 ASN I 36 -1 O MET I 29 N LEU I 18
SHEET 9 AB212 THR I 41 LYS I 50 -1 O LYS I 45 N VAL I 32
SHEET 10 AB212 TYR I 209 ALA I 219 -1 O GLN I 212 N VAL I 44
SHEET 11 AB212 TYR I 191 THR I 201 -1 N GLN I 195 O ILE I 217
SHEET 12 AB212 SER J 229 LEU J 230 -1 O LEU J 230 N LYS I 200
SHEET 1 AB313 ILE J 138 MET J 141 0
SHEET 2 AB313 SER J 154 LEU J 165 -1 O LYS J 164 N GLY J 140
SHEET 3 AB313 HIS J 170 SER J 181 -1 O PHE J 171 N PHE J 163
SHEET 4 AB313 PHE J 89 TYR J 97 -1 N ASN J 94 O ARG J 176
SHEET 5 AB313 THR J 102 ILE J 109 -1 O SER J 107 N TYR J 91
SHEET 6 AB313 PHE J 116 LYS J 125 -1 O LYS J 125 N THR J 102
SHEET 7 AB313 VAL J 11 VAL J 22 1 N PRO J 13 O PHE J 116
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 210 ALA J 219 -1 O VAL J 210 N ILE J 46
SHEET 11 AB313 HIS J 192 LYS J 200 -1 N GLN J 195 O ILE J 217
SHEET 12 AB313 SER J 144 ASN J 151 -1 N GLU J 146 O ILE J 194
SHEET 13 AB313 SER J 154 LEU J 165 -1 O ILE J 156 N TYR J 149
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 ILE K 48
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 HIS K 142
SHEET 8 AB4 8 THR K 276 GLY K 283 1 O GLU K 277 N PHE K 254
SHEET 1 AB5 8 LYS L 25 VAL L 29 0
SHEET 2 AB5 8 SER L 32 ASP L 38 -1 O SER L 32 N VAL L 29
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 66 1555 1555 1.43
LINK C3 CRO A 66 N ASN A 67 1555 1555 1.43
LINK C PHE B 65 N1 CRO B 66 1555 1555 1.43
LINK C3 CRO B 66 N ASN B 67 1555 1555 1.43
LINK C PHE E 65 N1 CRO E 66 1555 1555 1.43
LINK C3 CRO E 66 N ASN E 67 1555 1555 1.43
LINK C PHE F 65 N1 CRO F 66 1555 1555 1.43
LINK C3 CRO F 66 N ASN F 67 1555 1555 1.43
LINK C PHE I 65 N1 CRO I 66 1555 1555 1.43
LINK C3 CRO I 66 N ASN I 67 1555 1555 1.43
LINK C PHE J 65 N1 CRO J 66 1555 1555 1.43
LINK C3 CRO J 66 N ASN J 67 1555 1555 1.43
CISPEP 1 ALA A 52 PRO A 53 0 -0.35
CISPEP 2 PHE A 85 PRO A 86 0 -1.30
CISPEP 3 LEU A 230 PRO A 231 0 -7.46
CISPEP 4 ALA B 52 PRO B 53 0 -0.09
CISPEP 5 PHE B 85 PRO B 86 0 7.12
CISPEP 6 ASP C 258 PRO C 259 0 3.40
CISPEP 7 ASP D 258 PRO D 259 0 -3.73
CISPEP 8 ALA E 52 PRO E 53 0 -0.21
CISPEP 9 PHE E 85 PRO E 86 0 5.66
CISPEP 10 LEU E 230 PRO E 231 0 14.76
CISPEP 11 ALA F 52 PRO F 53 0 0.15
CISPEP 12 PHE F 85 PRO F 86 0 8.35
CISPEP 13 LEU F 230 PRO F 231 0 -19.39
CISPEP 14 ASP G 258 PRO G 259 0 -2.07
CISPEP 15 ASP H 258 PRO H 259 0 -1.45
CISPEP 16 ALA I 52 PRO I 53 0 -0.29
CISPEP 17 PHE I 85 PRO I 86 0 5.99
CISPEP 18 LEU I 230 PRO I 231 0 5.28
CISPEP 19 MET J 1 ASP J 2 0 -1.31
CISPEP 20 ALA J 52 PRO J 53 0 -1.15
CISPEP 21 PHE J 85 PRO J 86 0 6.77
CISPEP 22 LEU J 230 PRO J 231 0 -3.51
CISPEP 23 ASP K 258 PRO K 259 0 -2.27
CISPEP 24 ASP L 258 PRO L 259 0 -5.11
CRYST1 97.988 97.988 361.996 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 0.010205 0.005892 0.000000 0.00000
SCALE2 0.000000 0.011784 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002762 0.00000
TER 1813 PRO A 231
TER 3643 PRO B 231
TER 6159 LYS C 308
TER 8701 GLN D 321
TER 10541 PRO E 231
TER 12362 PRO F 231
TER 14878 LYS G 308
TER 17402 ASN H 309
TER 19224 PRO I 231
TER 21059 PRO J 231
TER 23586 LYS K 308
TER 26136 GLN L 321
MASTER 452 0 11 122 131 0 0 626880 12 293 258
END |