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HEADER HYDROLASE 15-FEB-24 8S1L
TITLE CRYSTAL STRUCTURE OF RENILLA RENIFORMIS LUCIFERASE RLUC8-GFP BRET
TITLE 2 COMPLEX AT PH 6.0
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GREEN FLUORESCENT PROTEIN;
COMPND 3 CHAIN: A, B, E, F;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: COELENTERAZINE H 2-MONOOXYGENASE;
COMPND 7 CHAIN: C, D, G, H;
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, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.MAREK,A.SMRCKOVA
REVDAT 1 03-SEP-25 8S1L 0
JRNL AUTH M.MAREK,A.SMRCKOVA
JRNL TITL CRYSTAL STRUCTURE OF RENILLA RENIFORMIS LUCIFERASE RLUC8-GFP
JRNL TITL 2 BRET COMPLEX AT PH 6.0
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.40 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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.54
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 142629
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.271
REMARK 3 R VALUE (WORKING SET) : 0.268
REMARK 3 FREE R VALUE : 0.340
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.950
REMARK 3 FREE R VALUE TEST SET COUNT : 7056
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 47.5400 - 7.4432 0.99 4527 226 0.2088 0.2285
REMARK 3 2 7.4432 - 5.9115 1.00 4612 196 0.2464 0.3488
REMARK 3 3 5.9115 - 5.1652 1.00 4595 209 0.2373 0.3253
REMARK 3 4 5.1652 - 4.6934 1.00 4585 208 0.2197 0.2633
REMARK 3 5 4.6934 - 4.3573 1.00 4448 270 0.2179 0.2951
REMARK 3 6 4.3573 - 4.1005 1.00 4639 202 0.2303 0.2988
REMARK 3 7 4.1005 - 3.8953 1.00 4587 226 0.2345 0.2790
REMARK 3 8 3.8953 - 3.7258 0.99 4559 212 0.2588 0.3244
REMARK 3 9 3.7258 - 3.5824 0.99 4520 231 0.2689 0.3696
REMARK 3 10 3.5824 - 3.4588 1.00 4531 216 0.2581 0.3639
REMARK 3 11 3.4588 - 3.3507 1.00 4617 198 0.2642 0.3524
REMARK 3 12 3.3507 - 3.2549 0.99 4488 263 0.2797 0.3569
REMARK 3 13 3.2549 - 3.1693 0.99 4533 248 0.3022 0.3865
REMARK 3 14 3.1693 - 3.0920 0.99 4518 212 0.2795 0.4185
REMARK 3 15 3.0920 - 3.0217 0.99 4601 202 0.2971 0.3704
REMARK 3 16 3.0217 - 2.9574 0.99 4502 286 0.3180 0.3917
REMARK 3 17 2.9574 - 2.8982 0.99 4469 307 0.3419 0.4105
REMARK 3 18 2.8982 - 2.8435 0.99 4522 248 0.3570 0.4437
REMARK 3 19 2.8435 - 2.7928 0.99 4534 198 0.3532 0.4405
REMARK 3 20 2.7928 - 2.7454 0.99 4486 236 0.3726 0.4351
REMARK 3 21 2.7454 - 2.7012 0.99 4603 231 0.3721 0.5062
REMARK 3 22 2.7012 - 2.6596 0.99 4531 199 0.3661 0.4369
REMARK 3 23 2.6596 - 2.6205 1.00 4476 301 0.3760 0.4340
REMARK 3 24 2.6205 - 2.5836 0.99 4471 283 0.3796 0.4534
REMARK 3 25 2.5836 - 2.5487 0.99 4540 251 0.3798 0.4291
REMARK 3 26 2.5487 - 2.5156 0.99 4398 262 0.3856 0.4172
REMARK 3 27 2.5156 - 2.4841 0.99 4498 304 0.4048 0.4667
REMARK 3 28 2.4841 - 2.4542 0.98 4457 211 0.4122 0.4774
REMARK 3 29 2.4542 - 2.4257 0.97 4513 205 0.4198 0.4664
REMARK 3 30 2.4257 - 2.3984 0.94 4213 215 0.3980 0.4545
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) : 0.520
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 44.190
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 : 0.011 18145
REMARK 3 ANGLE : 1.487 24531
REMARK 3 CHIRALITY : 0.073 2607
REMARK 3 PLANARITY : 0.009 3137
REMARK 3 DIHEDRAL : 6.389 12670
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): -0.6304 -28.7368 30.4056
REMARK 3 T TENSOR
REMARK 3 T11: 0.4026 T22: 0.8028
REMARK 3 T33: 0.4683 T12: 0.2863
REMARK 3 T13: 0.0122 T23: -0.0220
REMARK 3 L TENSOR
REMARK 3 L11: 0.0447 L22: 0.1126
REMARK 3 L33: -0.0302 L12: -0.0971
REMARK 3 L13: -0.0077 L23: 0.0145
REMARK 3 S TENSOR
REMARK 3 S11: 0.1029 S12: -0.1250 S13: 0.0093
REMARK 3 S21: -0.3067 S22: -0.1042 S23: 0.0067
REMARK 3 S31: 0.0102 S32: 0.0118 S33: 0.0770
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 8S1L 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_1292136643.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-OCT-20
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6
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 : 143749
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.398
REMARK 200 RESOLUTION RANGE LOW (A) : 47.540
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 10.50
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.48
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 (%): 67.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MES BUFFER, PEG 4000, PH 6, VAPOR
REMARK 280 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 238.08800
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 119.04400
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 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: 9960 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41530 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.0 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: 10080 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41400 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -54.0 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 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 B 1
REMARK 465 MET C 1
REMARK 465 PHE C 318
REMARK 465 GLN C 319
REMARK 465 MET D 1
REMARK 465 GLU D 310
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 F 1
REMARK 465 MET G 1
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 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 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 CD2 CRO E 66 OE1 GLU E 214 1.38
REMARK 500 OD1 ASP B 2 NZ LYS B 5 1.45
REMARK 500 C PHE E 65 CA1 CRO E 66 1.71
REMARK 500 OG SER C 91 OD2 ASP C 96 1.78
REMARK 500 OG1 THR B 150 O PRO B 189 1.90
REMARK 500 O PRO A 13 OH TYR A 70 1.96
REMARK 500 O LEU E 82 OG SER E 84 1.98
REMARK 500 OG1 THR E 150 O PRO E 189 1.99
REMARK 500 OG1 THR A 150 O PRO A 189 2.03
REMARK 500 O ARG A 68 OG1 THR A 71 2.04
REMARK 500 O ARG E 68 OG1 THR E 71 2.07
REMARK 500 NZ LYS G 207 O HOH G 501 2.08
REMARK 500 O ASP A 113 N LYS A 115 2.08
REMARK 500 OG SER H 91 OD2 ASP H 96 2.09
REMARK 500 O ALA B 206 OH TYR D 6 2.10
REMARK 500 OE1 GLN A 142 NE2 HIS A 170 2.11
REMARK 500 OE2 GLU D 144 OG SER D 263 2.11
REMARK 500 O ASP B 113 N LYS B 115 2.11
REMARK 500 OH TYR H 36 O HOH H 501 2.11
REMARK 500 OG1 THR H 16 OE1 GLN H 19 2.12
REMARK 500 OD2 ASP B 108 OG SER B 110 2.14
REMARK 500 O GLY A 88 N LYS A 182 2.16
REMARK 500 OG1 THR B 205 OG SER B 207 2.16
REMARK 500 O LEU D 244 OG SER D 247 2.17
REMARK 500 OG SER D 91 OD2 ASP D 96 2.17
REMARK 500 O SER F 28 OG1 THR F 49 2.18
REMARK 500 O GLY F 131 N VAL F 133 2.19
REMARK 500 OE1 GLU D 204 O HOH D 501 2.19
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 PRO A 13 CD PRO A 13 N -0.150
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 PHE A 85 CB - CG - CD1 ANGL. DEV. = -4.7 DEGREES
REMARK 500 PRO A 86 C - N - CA ANGL. DEV. = 15.7 DEGREES
REMARK 500 PRO A 86 C - N - CD ANGL. DEV. = -19.3 DEGREES
REMARK 500 LEU B 3 CA - CB - CG ANGL. DEV. = 14.3 DEGREES
REMARK 500 LEU B 127 CA - CB - CG ANGL. DEV. = -17.6 DEGREES
REMARK 500 PRO E 86 C - N - CD ANGL. DEV. = -15.4 DEGREES
REMARK 500 LEU F 3 CA - CB - CG ANGL. DEV. = 19.8 DEGREES
REMARK 500 MET F 188 C - N - CA ANGL. DEV. = 16.2 DEGREES
REMARK 500 LEU H 287 CA - CB - CG ANGL. DEV. = 18.7 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 LEU A 3 -56.32 -158.79
REMARK 500 GLU A 10 -65.53 56.26
REMARK 500 VAL A 11 103.49 -56.98
REMARK 500 PRO A 13 -141.78 -76.28
REMARK 500 LEU A 21 96.05 -169.17
REMARK 500 ASP A 24 -18.30 171.49
REMARK 500 SER A 28 91.67 -162.13
REMARK 500 GLU A 30 136.11 -174.44
REMARK 500 ILE A 37 -87.88 27.02
REMARK 500 GLU A 43 143.21 -170.45
REMARK 500 SER A 47 115.41 -161.15
REMARK 500 THR A 49 5.15 -151.21
REMARK 500 LYS A 50 147.34 -171.27
REMARK 500 ASP A 59 -3.14 -57.54
REMARK 500 GLU A 76 4.12 -67.39
REMARK 500 GLN A 83 -10.93 -43.92
REMARK 500 PRO A 86 -103.75 28.26
REMARK 500 GLU A 87 -46.79 -137.70
REMARK 500 GLU A 112 -110.30 -110.92
REMARK 500 LYS A 115 -158.15 -177.66
REMARK 500 LYS A 123 111.88 -167.84
REMARK 500 ARG A 129 -63.54 -28.50
REMARK 500 GLN A 136 53.51 24.17
REMARK 500 VAL A 152 -124.94 57.61
REMARK 500 THR A 153 7.92 -65.61
REMARK 500 LYS A 169 -177.05 -63.37
REMARK 500 GLU A 186 -96.65 -36.83
REMARK 500 LEU A 190 -88.06 -83.22
REMARK 500 THR A 201 -91.78 -44.66
REMARK 500 ASN A 202 90.04 -172.73
REMARK 500 ASP A 204 -103.04 29.01
REMARK 500 ALA A 206 -158.35 40.48
REMARK 500 ILE A 226 86.50 -64.74
REMARK 500 GLU A 227 -32.09 -37.62
REMARK 500 LEU B 3 46.79 -146.51
REMARK 500 ALA B 4 -85.20 -78.69
REMARK 500 LYS B 5 -78.48 35.34
REMARK 500 GLU B 10 -84.39 -52.43
REMARK 500 LEU B 21 93.21 -163.60
REMARK 500 SER B 28 69.10 -117.86
REMARK 500 MET B 29 -152.77 -63.15
REMARK 500 GLU B 30 175.95 169.40
REMARK 500 PRO B 55 36.28 -88.60
REMARK 500 PHE B 89 -158.19 -163.35
REMARK 500 ILE B 109 72.25 -109.76
REMARK 500 SER B 110 -145.32 -73.84
REMARK 500 GLU B 112 102.36 -164.74
REMARK 500 ASP B 113 121.56 56.27
REMARK 500 PHE B 116 81.74 -54.00
REMARK 500 ASN B 119 89.16 -158.20
REMARK 500
REMARK 500 THIS ENTRY HAS 262 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 PRO A 86 GLU A 87 -147.08
REMARK 500 VAL A 203 ASP A 204 139.10
REMARK 500 HIS B 196 ARG B 197 147.28
REMARK 500 ASN B 202 VAL B 203 147.62
REMARK 500 LYS B 225 ILE B 226 149.64
REMARK 500 TYR D 6 ASP D 7 146.18
REMARK 500 PRO D 76 ASP D 77 148.26
REMARK 500 LYS D 282 GLY D 283 148.33
REMARK 500 GLU E 39 GLY E 40 149.29
REMARK 500 GLN E 83 SER E 84 145.99
REMARK 500 SER E 84 PHE E 85 -129.26
REMARK 500 PHE E 85 PRO E 86 -117.70
REMARK 500 ASP F 2 LEU F 3 142.56
REMARK 500 THR F 201 ASN F 202 -146.33
REMARK 500 ILE G 34 ASN G 35 149.46
REMARK 500 PRO H 76 ASP H 77 147.30
REMARK 500
REMARK 500 REMARK: NULL
DBREF 8S1L A 1 231 UNP Q963I9 Q963I9_RENRE 1 233
DBREF 8S1L B 1 231 UNP Q963I9 Q963I9_RENRE 1 233
DBREF 8S1L C 1 311 UNP P27652 LUCI_RENRE 1 311
DBREF 8S1L D 1 311 UNP P27652 LUCI_RENRE 1 311
DBREF 8S1L E 1 231 UNP Q963I9 Q963I9_RENRE 1 233
DBREF 8S1L F 1 231 UNP Q963I9 Q963I9_RENRE 1 233
DBREF 8S1L G 1 311 UNP P27652 LUCI_RENRE 1 311
DBREF 8S1L H 1 311 UNP P27652 LUCI_RENRE 1 311
SEQADV 8S1L CRO A 66 UNP Q963I9 SER 66 CHROMOPHORE
SEQADV 8S1L CRO A 66 UNP Q963I9 TYR 67 CHROMOPHORE
SEQADV 8S1L CRO A 66 UNP Q963I9 GLY 68 CHROMOPHORE
SEQADV 8S1L CRO B 66 UNP Q963I9 SER 66 CHROMOPHORE
SEQADV 8S1L CRO B 66 UNP Q963I9 TYR 67 CHROMOPHORE
SEQADV 8S1L CRO B 66 UNP Q963I9 GLY 68 CHROMOPHORE
SEQADV 8S1L THR C 55 UNP P27652 ALA 55 ENGINEERED MUTATION
SEQADV 8S1L ALA C 124 UNP P27652 CYS 124 ENGINEERED MUTATION
SEQADV 8S1L ALA C 130 UNP P27652 SER 130 ENGINEERED MUTATION
SEQADV 8S1L ARG C 136 UNP P27652 LYS 136 ENGINEERED MUTATION
SEQADV 8S1L MET C 143 UNP P27652 ALA 143 ENGINEERED MUTATION
SEQADV 8S1L VAL C 185 UNP P27652 MET 185 ENGINEERED MUTATION
SEQADV 8S1L LEU C 253 UNP P27652 MET 253 ENGINEERED MUTATION
SEQADV 8S1L LEU C 287 UNP P27652 SER 287 ENGINEERED MUTATION
SEQADV 8S1L SER C 312 UNP P27652 EXPRESSION TAG
SEQADV 8S1L GLY C 313 UNP P27652 EXPRESSION TAG
SEQADV 8S1L LEU C 314 UNP P27652 EXPRESSION TAG
SEQADV 8S1L GLU C 315 UNP P27652 EXPRESSION TAG
SEQADV 8S1L VAL C 316 UNP P27652 EXPRESSION TAG
SEQADV 8S1L LEU C 317 UNP P27652 EXPRESSION TAG
SEQADV 8S1L PHE C 318 UNP P27652 EXPRESSION TAG
SEQADV 8S1L GLN C 319 UNP P27652 EXPRESSION TAG
SEQADV 8S1L THR D 55 UNP P27652 ALA 55 ENGINEERED MUTATION
SEQADV 8S1L ALA D 124 UNP P27652 CYS 124 ENGINEERED MUTATION
SEQADV 8S1L ALA D 130 UNP P27652 SER 130 ENGINEERED MUTATION
SEQADV 8S1L ARG D 136 UNP P27652 LYS 136 ENGINEERED MUTATION
SEQADV 8S1L MET D 143 UNP P27652 ALA 143 ENGINEERED MUTATION
SEQADV 8S1L VAL D 185 UNP P27652 MET 185 ENGINEERED MUTATION
SEQADV 8S1L LEU D 253 UNP P27652 MET 253 ENGINEERED MUTATION
SEQADV 8S1L LEU D 287 UNP P27652 SER 287 ENGINEERED MUTATION
SEQADV 8S1L SER D 312 UNP P27652 EXPRESSION TAG
SEQADV 8S1L GLY D 313 UNP P27652 EXPRESSION TAG
SEQADV 8S1L LEU D 314 UNP P27652 EXPRESSION TAG
SEQADV 8S1L GLU D 315 UNP P27652 EXPRESSION TAG
SEQADV 8S1L VAL D 316 UNP P27652 EXPRESSION TAG
SEQADV 8S1L LEU D 317 UNP P27652 EXPRESSION TAG
SEQADV 8S1L PHE D 318 UNP P27652 EXPRESSION TAG
SEQADV 8S1L GLN D 319 UNP P27652 EXPRESSION TAG
SEQADV 8S1L CRO E 66 UNP Q963I9 SER 66 CHROMOPHORE
SEQADV 8S1L CRO E 66 UNP Q963I9 TYR 67 CHROMOPHORE
SEQADV 8S1L CRO E 66 UNP Q963I9 GLY 68 CHROMOPHORE
SEQADV 8S1L CRO F 66 UNP Q963I9 SER 66 CHROMOPHORE
SEQADV 8S1L CRO F 66 UNP Q963I9 TYR 67 CHROMOPHORE
SEQADV 8S1L CRO F 66 UNP Q963I9 GLY 68 CHROMOPHORE
SEQADV 8S1L THR G 55 UNP P27652 ALA 55 ENGINEERED MUTATION
SEQADV 8S1L ALA G 124 UNP P27652 CYS 124 ENGINEERED MUTATION
SEQADV 8S1L ALA G 130 UNP P27652 SER 130 ENGINEERED MUTATION
SEQADV 8S1L ARG G 136 UNP P27652 LYS 136 ENGINEERED MUTATION
SEQADV 8S1L MET G 143 UNP P27652 ALA 143 ENGINEERED MUTATION
SEQADV 8S1L VAL G 185 UNP P27652 MET 185 ENGINEERED MUTATION
SEQADV 8S1L LEU G 253 UNP P27652 MET 253 ENGINEERED MUTATION
SEQADV 8S1L LEU G 287 UNP P27652 SER 287 ENGINEERED MUTATION
SEQADV 8S1L SER G 312 UNP P27652 EXPRESSION TAG
SEQADV 8S1L GLY G 313 UNP P27652 EXPRESSION TAG
SEQADV 8S1L LEU G 314 UNP P27652 EXPRESSION TAG
SEQADV 8S1L GLU G 315 UNP P27652 EXPRESSION TAG
SEQADV 8S1L VAL G 316 UNP P27652 EXPRESSION TAG
SEQADV 8S1L LEU G 317 UNP P27652 EXPRESSION TAG
SEQADV 8S1L PHE G 318 UNP P27652 EXPRESSION TAG
SEQADV 8S1L GLN G 319 UNP P27652 EXPRESSION TAG
SEQADV 8S1L THR H 55 UNP P27652 ALA 55 ENGINEERED MUTATION
SEQADV 8S1L ALA H 124 UNP P27652 CYS 124 ENGINEERED MUTATION
SEQADV 8S1L ALA H 130 UNP P27652 SER 130 ENGINEERED MUTATION
SEQADV 8S1L ARG H 136 UNP P27652 LYS 136 ENGINEERED MUTATION
SEQADV 8S1L MET H 143 UNP P27652 ALA 143 ENGINEERED MUTATION
SEQADV 8S1L VAL H 185 UNP P27652 MET 185 ENGINEERED MUTATION
SEQADV 8S1L LEU H 253 UNP P27652 MET 253 ENGINEERED MUTATION
SEQADV 8S1L LEU H 287 UNP P27652 SER 287 ENGINEERED MUTATION
SEQADV 8S1L SER H 312 UNP P27652 EXPRESSION TAG
SEQADV 8S1L GLY H 313 UNP P27652 EXPRESSION TAG
SEQADV 8S1L LEU H 314 UNP P27652 EXPRESSION TAG
SEQADV 8S1L GLU H 315 UNP P27652 EXPRESSION TAG
SEQADV 8S1L VAL H 316 UNP P27652 EXPRESSION TAG
SEQADV 8S1L LEU H 317 UNP P27652 EXPRESSION TAG
SEQADV 8S1L PHE H 318 UNP P27652 EXPRESSION TAG
SEQADV 8S1L GLN H 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
MODRES 8S1L CRO A 66 SER CHROMOPHORE
MODRES 8S1L CRO A 66 TYR CHROMOPHORE
MODRES 8S1L CRO A 66 GLY CHROMOPHORE
MODRES 8S1L CRO B 66 SER CHROMOPHORE
MODRES 8S1L CRO B 66 TYR CHROMOPHORE
MODRES 8S1L CRO B 66 GLY CHROMOPHORE
MODRES 8S1L CRO E 66 SER CHROMOPHORE
MODRES 8S1L CRO E 66 TYR CHROMOPHORE
MODRES 8S1L CRO E 66 GLY CHROMOPHORE
MODRES 8S1L CRO F 66 SER CHROMOPHORE
MODRES 8S1L CRO F 66 TYR CHROMOPHORE
MODRES 8S1L CRO F 66 GLY CHROMOPHORE
HET CRO A 66 21
HET CRO B 66 21
HET CRO E 66 21
HET CRO F 66 21
HET CEI C 401 31
HET CEI D 401 31
HET CEI G 401 31
HET CEI H 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 4(C15 H17 N3 O5)
FORMUL 9 CEI 4(C25 H21 N3 O3)
FORMUL 13 HOH *93(H2 O)
HELIX 1 AA1 LEU A 3 GLY A 7 5 5
HELIX 2 AA2 ALA A 57 VAL A 61 5 5
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 PHE B 81 PHE B 85 5 5
HELIX 6 AA6 ASP C 7 MET C 14 5 8
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 GLU C 132 1 13
HELIX 12 AB3 GLU C 161 LYS C 167 1 7
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 GLU C 195 GLU C 204 1 10
HELIX 16 AB7 PRO C 205 GLU C 208 5 4
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 LYS C 308 1 18
HELIX 24 AC6 ASN C 309 GLN C 311 5 3
HELIX 25 AC7 ASP D 7 MET D 14 5 8
HELIX 26 AC8 GLY D 17 ALA D 22 1 6
HELIX 27 AC9 SER D 56 ARG D 61 5 6
HELIX 28 AD1 VAL D 63 GLU D 68 1 6
HELIX 29 AD2 ARG D 93 LEU D 107 1 15
HELIX 30 AD3 TRP D 121 HIS D 133 1 13
HELIX 31 AD4 GLU D 161 LYS D 167 1 7
HELIX 32 AD5 GLU D 169 LEU D 176 1 8
HELIX 33 AD6 ASN D 179 THR D 184 1 6
HELIX 34 AD7 THR D 184 LYS D 189 1 6
HELIX 35 AD8 GLU D 195 GLU D 204 1 10
HELIX 36 AD9 PRO D 205 LYS D 207 5 3
HELIX 37 AE1 GLY D 210 VAL D 212 5 3
HELIX 38 AE2 ARG D 213 TRP D 219 1 7
HELIX 39 AE3 PRO D 220 ILE D 223 5 4
HELIX 40 AE4 LYS D 230 SER D 247 1 18
HELIX 41 AE5 PHE D 262 LYS D 272 1 11
HELIX 42 AE6 PHE D 286 ASP D 290 5 5
HELIX 43 AE7 ALA D 291 LEU D 307 1 17
HELIX 44 AE8 ALA E 57 VAL E 63 5 7
HELIX 45 AE9 ALA F 57 SER F 62 5 6
HELIX 46 AF1 PHE F 81 PHE F 85 5 5
HELIX 47 AF2 ASP G 7 MET G 14 5 8
HELIX 48 AF3 GLY G 17 ALA G 22 1 6
HELIX 49 AF4 SER G 56 ARG G 61 5 6
HELIX 50 AF5 VAL G 63 GLU G 68 1 6
HELIX 51 AF6 ARG G 93 GLU G 106 1 14
HELIX 52 AF7 LEU G 107 ASN G 109 5 3
HELIX 53 AF8 TRP G 121 HIS G 133 1 13
HELIX 54 AF9 GLU G 161 LYS G 167 1 7
HELIX 55 AG1 GLY G 171 LEU G 176 1 6
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 ARG G 245 1 16
HELIX 64 AH1 PHE G 262 LYS G 272 1 11
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 ARG H 23 1 8
HELIX 69 AH6 SER H 56 ARG H 61 5 6
HELIX 70 AH7 VAL H 63 ALA H 71 5 9
HELIX 71 AH8 ARG H 93 LEU H 107 1 15
HELIX 72 AH9 ASP H 120 GLU H 132 1 13
HELIX 73 AI1 GLU H 161 LYS H 167 1 7
HELIX 74 AI2 GLU H 170 GLU H 177 1 8
HELIX 75 AI3 ASN H 179 THR H 184 1 6
HELIX 76 AI4 GLU H 195 GLU H 204 1 10
HELIX 77 AI5 PRO H 205 GLU H 208 5 4
HELIX 78 AI6 GLY H 210 VAL H 212 5 3
HELIX 79 AI7 ARG H 213 TRP H 219 1 7
HELIX 80 AI8 PRO H 220 ILE H 223 5 4
HELIX 81 AI9 LYS H 230 SER H 247 1 18
HELIX 82 AJ1 PHE H 262 LYS H 272 1 11
HELIX 83 AJ2 PHE H 286 ALA H 291 1 6
HELIX 84 AJ3 ALA H 291 GLN H 311 1 21
SHEET 1 AA1 2 PRO A 13 ILE A 16 0
SHEET 2 AA1 2 GLY A 31 GLU A 34 -1 O GLY A 33 N THR A 14
SHEET 1 AA2 3 VAL A 44 ILE A 46 0
SHEET 2 AA2 3 VAL A 210 HIS A 213 -1 O GLN A 212 N VAL A 44
SHEET 3 AA2 3 VAL A 199 LYS A 200 -1 N VAL A 199 O HIS A 213
SHEET 1 AA3 9 THR A 71 GLY A 72 0
SHEET 2 AA3 9 ALA A 216 ALA A 219 1 O ALA A 218 N GLY A 72
SHEET 3 AA3 9 TYR A 191 HIS A 196 -1 N GLN A 195 O ILE A 217
SHEET 4 AA3 9 SER A 144 ASN A 151 -1 N GLU A 146 O ILE A 194
SHEET 5 AA3 9 SER A 154 LEU A 165 -1 O ILE A 156 N TYR A 149
SHEET 6 AA3 9 HIS A 170 TYR A 179 -1 O PHE A 171 N PHE A 163
SHEET 7 AA3 9 ARG A 93 TYR A 97 -1 N ARG A 96 O HIS A 174
SHEET 8 AA3 9 THR A 102 VAL A 105 -1 O ALA A 103 N ILE A 95
SHEET 9 AA3 9 ALA A 124 LYS A 125 -1 O LYS A 125 N THR A 102
SHEET 1 AA4 6 THR A 71 GLY A 72 0
SHEET 2 AA4 6 ALA A 216 ALA A 219 1 O ALA A 218 N GLY A 72
SHEET 3 AA4 6 TYR A 191 HIS A 196 -1 N GLN A 195 O ILE A 217
SHEET 4 AA4 6 SER A 144 ASN A 151 -1 N GLU A 146 O ILE A 194
SHEET 5 AA4 6 SER A 154 LEU A 165 -1 O ILE A 156 N TYR A 149
SHEET 6 AA4 6 ILE A 138 GLN A 142 -1 N GLY A 140 O LYS A 164
SHEET 1 AA5 2 ILE A 109 LEU A 111 0
SHEET 2 AA5 2 PHE A 116 VAL A 118 -1 O ILE A 117 N SER A 110
SHEET 1 AA612 HIS B 25 PHE B 27 0
SHEET 2 AA612 ILE B 16 VAL B 22 -1 N VAL B 22 O HIS B 25
SHEET 3 AA612 VAL B 118 LYS B 125 1 O VAL B 120 N ASN B 17
SHEET 4 AA612 THR B 102 ILE B 109 -1 N LYS B 106 O ASP B 121
SHEET 5 AA612 PHE B 89 TYR B 97 -1 N ILE B 95 O ALA B 103
SHEET 6 AA612 HIS B 170 SER B 181 -1 O VAL B 178 N GLU B 92
SHEET 7 AA612 VAL B 155 LEU B 165 -1 N PHE B 163 O PHE B 171
SHEET 8 AA612 SER B 144 THR B 150 -1 N SER B 147 O GLU B 158
SHEET 9 AA612 TYR B 191 LYS B 200 -1 O HIS B 192 N MET B 148
SHEET 10 AA612 TYR B 209 ALA B 219 -1 O ILE B 217 N GLN B 195
SHEET 11 AA612 GLN B 42 SER B 47 -1 N ILE B 46 O VAL B 210
SHEET 12 AA612 VAL B 32 GLY B 35 -1 N VAL B 32 O LYS B 45
SHEET 1 AA7 8 HIS B 25 PHE B 27 0
SHEET 2 AA7 8 ILE B 16 VAL B 22 -1 N VAL B 22 O HIS B 25
SHEET 3 AA7 8 VAL B 118 LYS B 125 1 O VAL B 120 N ASN B 17
SHEET 4 AA7 8 THR B 102 ILE B 109 -1 N LYS B 106 O ASP B 121
SHEET 5 AA7 8 PHE B 89 TYR B 97 -1 N ILE B 95 O ALA B 103
SHEET 6 AA7 8 HIS B 170 SER B 181 -1 O VAL B 178 N GLU B 92
SHEET 7 AA7 8 VAL B 155 LEU B 165 -1 N PHE B 163 O PHE B 171
SHEET 8 AA7 8 ILE B 138 MET B 141 -1 N GLY B 140 O LYS B 164
SHEET 1 AA8 2 LYS C 25 VAL C 29 0
SHEET 2 AA8 2 SER C 32 TYR C 36 -1 O SER C 32 N VAL C 29
SHEET 1 AA9 6 ARG C 72 ILE C 74 0
SHEET 2 AA9 6 ALA C 46 LEU C 50 1 N VAL C 47 O ARG C 72
SHEET 3 AA9 6 ILE C 114 GLY C 118 1 O VAL C 117 N LEU C 50
SHEET 4 AA9 6 ILE C 137 HIS C 142 1 O VAL C 141 N PHE C 116
SHEET 5 AA9 6 LYS C 252 SER C 257 1 O LEU C 253 N HIS C 142
SHEET 6 AA9 6 THR C 276 VAL C 281 1 O VAL C 279 N GLU C 256
SHEET 1 AB1 2 ASN D 28 VAL D 29 0
SHEET 2 AB1 2 SER D 32 PHE D 33 -1 O SER D 32 N VAL D 29
SHEET 1 AB2 7 TYR D 36 ASP D 38 0
SHEET 2 AB2 7 ARG D 72 PRO D 76 -1 O ILE D 75 N TYR D 37
SHEET 3 AB2 7 ALA D 46 LEU D 50 1 N VAL D 47 O ARG D 72
SHEET 4 AB2 7 ILE D 114 HIS D 119 1 O VAL D 117 N LEU D 50
SHEET 5 AB2 7 ILE D 137 MET D 143 1 O LYS D 138 N ILE D 114
SHEET 6 AB2 7 LYS D 252 PRO D 259 1 O LEU D 253 N HIS D 142
SHEET 7 AB2 7 THR D 276 GLY D 283 1 O GLU D 277 N PHE D 254
SHEET 1 AB3 5 PHE E 116 ILE E 117 0
SHEET 2 AB3 5 VAL E 11 LYS E 15 1 N LYS E 15 O PHE E 116
SHEET 3 AB3 5 GLY E 33 ASN E 36 -1 O GLY E 33 N THR E 14
SHEET 4 AB3 5 THR E 41 LYS E 45 -1 O GLU E 43 N GLU E 34
SHEET 5 AB3 5 VAL E 211 THR E 215 -1 O GLU E 214 N GLN E 42
SHEET 1 AB4 2 GLY E 20 VAL E 22 0
SHEET 2 AB4 2 HIS E 25 PHE E 27 -1 O HIS E 25 N VAL E 22
SHEET 1 AB5 4 PHE E 89 THR E 90 0
SHEET 2 AB5 4 HIS E 170 SER E 181 -1 O LYS E 180 N THR E 90
SHEET 3 AB5 4 SER E 154 LEU E 165 -1 N VAL E 155 O TYR E 179
SHEET 4 AB5 4 ILE E 138 MET E 141 -1 N VAL E 139 O LYS E 164
SHEET 1 AB6 7 ALA E 124 LYS E 125 0
SHEET 2 AB6 7 THR E 102 VAL E 105 -1 N THR E 102 O LYS E 125
SHEET 3 AB6 7 ARG E 93 TYR E 97 -1 N ARG E 93 O VAL E 105
SHEET 4 AB6 7 HIS E 170 SER E 181 -1 O ARG E 176 N ASN E 94
SHEET 5 AB6 7 SER E 154 LEU E 165 -1 N VAL E 155 O TYR E 179
SHEET 6 AB6 7 SER E 144 ASN E 151 -1 N TYR E 149 O ILE E 156
SHEET 7 AB6 7 TYR E 191 HIS E 196 -1 O ILE E 194 N GLU E 146
SHEET 1 AB711 MET F 12 LYS F 15 0
SHEET 2 AB711 GLU F 30 GLY F 35 -1 O GLY F 35 N MET F 12
SHEET 3 AB711 GLN F 42 SER F 47 -1 O SER F 47 N GLU F 30
SHEET 4 AB711 VAL F 210 ALA F 216 -1 O VAL F 210 N ILE F 46
SHEET 5 AB711 HIS F 192 LYS F 200 -1 N ARG F 197 O THR F 215
SHEET 6 AB711 SER F 144 THR F 150 -1 N MET F 148 O HIS F 192
SHEET 7 AB711 VAL F 155 LEU F 165 -1 O GLU F 158 N SER F 147
SHEET 8 AB711 HIS F 170 SER F 181 -1 O PHE F 171 N PHE F 163
SHEET 9 AB711 PHE F 89 THR F 90 -1 N THR F 90 O LYS F 180
SHEET 10 AB711 ASP F 108 ILE F 109 -1 O ILE F 109 N PHE F 89
SHEET 11 AB711 VAL F 118 ASN F 119 -1 O ASN F 119 N ASP F 108
SHEET 1 AB8 8 HIS F 25 PHE F 27 0
SHEET 2 AB8 8 GLU F 19 VAL F 22 -1 N GLY F 20 O PHE F 27
SHEET 3 AB8 8 ASP F 121 LYS F 125 1 O ALA F 124 N LEU F 21
SHEET 4 AB8 8 THR F 102 VAL F 105 -1 N ILE F 104 O LYS F 123
SHEET 5 AB8 8 ARG F 93 TYR F 97 -1 N ILE F 95 O ALA F 103
SHEET 6 AB8 8 HIS F 170 SER F 181 -1 O ARG F 176 N ASN F 94
SHEET 7 AB8 8 VAL F 155 LEU F 165 -1 N PHE F 163 O PHE F 171
SHEET 8 AB8 8 ILE F 138 MET F 141 -1 N GLY F 140 O LYS F 164
SHEET 1 AB9 8 LYS G 25 VAL G 29 0
SHEET 2 AB9 8 SER G 32 ASP G 38 -1 O SER G 32 N VAL G 29
SHEET 3 AB9 8 ARG G 72 PRO G 76 -1 O ILE G 75 N TYR G 37
SHEET 4 AB9 8 ALA G 46 LEU G 50 1 N VAL G 47 O ARG G 72
SHEET 5 AB9 8 ILE G 114 HIS G 119 1 O ILE G 115 N ILE G 48
SHEET 6 AB9 8 ILE G 137 MET G 143 1 O LYS G 138 N ILE G 114
SHEET 7 AB9 8 LYS G 252 SER G 257 1 O ILE G 255 N HIS G 142
SHEET 8 AB9 8 THR G 276 VAL G 281 1 O GLU G 277 N PHE G 254
SHEET 1 AC1 8 LYS H 25 VAL H 29 0
SHEET 2 AC1 8 SER H 32 ASP H 38 -1 O SER H 32 N VAL H 29
SHEET 3 AC1 8 ARG H 72 PRO H 76 -1 O ILE H 75 N TYR H 37
SHEET 4 AC1 8 ALA H 46 LEU H 50 1 N VAL H 47 O ARG H 72
SHEET 5 AC1 8 ILE H 114 GLY H 118 1 O ILE H 115 N ILE H 48
SHEET 6 AC1 8 ILE H 137 HIS H 142 1 O LYS H 138 N ILE H 114
SHEET 7 AC1 8 LYS H 252 PRO H 259 1 O ILE H 255 N HIS H 142
SHEET 8 AC1 8 THR H 276 GLY H 283 1 O VAL H 279 N GLU H 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
CISPEP 1 ALA A 52 PRO A 53 0 -3.22
CISPEP 2 PHE A 85 PRO A 86 0 3.36
CISPEP 3 LEU A 230 PRO A 231 0 3.78
CISPEP 4 ALA B 52 PRO B 53 0 -3.35
CISPEP 5 PHE B 85 PRO B 86 0 3.99
CISPEP 6 LEU B 230 PRO B 231 0 -3.24
CISPEP 7 ASP C 258 PRO C 259 0 2.81
CISPEP 8 VAL C 316 LEU C 317 0 0.35
CISPEP 9 ASP D 258 PRO D 259 0 6.53
CISPEP 10 ALA E 52 PRO E 53 0 -2.54
CISPEP 11 LEU E 230 PRO E 231 0 0.08
CISPEP 12 ALA F 52 PRO F 53 0 -3.63
CISPEP 13 PHE F 85 PRO F 86 0 17.22
CISPEP 14 LEU F 230 PRO F 231 0 3.77
CISPEP 15 ASP G 258 PRO G 259 0 7.73
CISPEP 16 ASP H 258 PRO H 259 0 -5.97
CRYST1 95.934 95.934 357.132 90.00 90.00 120.00 P 32 12
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 0.010424 0.006018 0.000000 0.00000
SCALE2 0.000000 0.012036 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002800 0.00000
TER 1829 PRO A 231
TER 3650 PRO B 231
TER 6243 LEU C 317
TER 8776 ASN D 309
TER 10605 PRO E 231
TER 12426 PRO F 231
TER 14959 ASN G 309
TER 17563 GLN H 319
MASTER 468 0 8 84 112 0 0 617745 8 216 172
END |