| content |
HEADER HYDROLASE 13-OCT-19 6UNW
TITLE EPOXIDE HYDROLASE FROM AN ENDOPHYTIC STREPTOMYCES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SOLUBLE EPOXIDE HYDROLASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES SP. CBMAI 2042;
SOURCE 3 ORGANISM_TAXID: 2305222;
SOURCE 4 GENE: STAN_0072;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 866768
KEYWDS EPOXIDE HYDROLASE, BIOCATALYSIS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.WILSON,J.C.DOS SANTOS,M.V.B.DIAS
REVDAT 1 16-SEP-20 6UNW 0
JRNL AUTH G.D.TORMET-GONZALEZ,C.WILSON,G.S.DE OLIVEIRA,J.C.DOS SANTOS,
JRNL AUTH 2 L.G.DE OLIVEIRA,M.V.B.DIAS
JRNL TITL AN EPOXIDE HYDROLASE FROM ENDOPHYTIC STREPTOMYCES SHOWS
JRNL TITL 2 UNIQUE STRUCTURAL FEATURES AND WIDE BIOCATALYTIC ACTIVITY.
JRNL REF ACTA CRYSTALLOGR D STRUCT V. 76 868 2020
JRNL REF 2 BIOL
JRNL REFN ISSN 2059-7983
JRNL PMID 32876062
JRNL DOI 10.1107/S2059798320010402
REMARK 2
REMARK 2 RESOLUTION. 2.21 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 18.1-3865
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) : 2.21
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.52
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.9
REMARK 3 NUMBER OF REFLECTIONS : 64557
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 3267
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 48.5200 - 6.2900 0.99 3052 153 0.1754 0.1989
REMARK 3 2 6.2800 - 4.9900 1.00 2934 158 0.1708 0.2111
REMARK 3 3 4.9900 - 4.3600 1.00 2888 145 0.1410 0.1735
REMARK 3 4 4.3600 - 3.9600 1.00 2822 150 0.1417 0.1672
REMARK 3 5 3.9600 - 3.6800 1.00 2854 145 0.1459 0.1707
REMARK 3 6 3.6800 - 3.4600 1.00 2833 137 0.1526 0.2076
REMARK 3 7 3.4600 - 3.2900 1.00 2808 147 0.1637 0.1976
REMARK 3 8 3.2900 - 3.1500 1.00 2792 147 0.1707 0.1731
REMARK 3 9 3.1500 - 3.0200 1.00 2818 144 0.1832 0.2231
REMARK 3 10 3.0200 - 2.9200 1.00 2800 165 0.1923 0.2361
REMARK 3 11 2.9200 - 2.8300 1.00 2762 151 0.1947 0.2375
REMARK 3 12 2.8300 - 2.7500 1.00 2779 145 0.2053 0.2313
REMARK 3 13 2.7500 - 2.6800 1.00 2785 159 0.1981 0.2636
REMARK 3 14 2.6800 - 2.6100 1.00 2765 164 0.2024 0.2318
REMARK 3 15 2.6100 - 2.5500 1.00 2788 136 0.2077 0.2919
REMARK 3 16 2.5500 - 2.5000 1.00 2789 136 0.2079 0.2681
REMARK 3 17 2.5000 - 2.4500 1.00 2766 142 0.2106 0.3179
REMARK 3 18 2.4500 - 2.4000 1.00 2777 141 0.2300 0.2467
REMARK 3 19 2.4000 - 2.3600 0.77 2103 110 0.3808 0.4510
REMARK 3 20 2.3600 - 2.3200 0.38 1026 59 0.6414 0.7722
REMARK 3 21 2.3200 - 2.2800 0.75 2066 121 0.4425 0.4603
REMARK 3 22 2.2800 - 2.2400 1.00 2763 164 0.2685 0.3259
REMARK 3 23 2.2400 - 2.2100 0.93 2520 148 0.2796 0.3401
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.260
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.750
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.80
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
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): 20.9343 31.1737 4.9466
REMARK 3 T TENSOR
REMARK 3 T11: 0.1927 T22: 0.2323
REMARK 3 T33: 0.2475 T12: 0.0160
REMARK 3 T13: 0.0130 T23: 0.0381
REMARK 3 L TENSOR
REMARK 3 L11: 0.4160 L22: 0.8666
REMARK 3 L33: 0.3909 L12: -0.0179
REMARK 3 L13: 0.0178 L23: 0.0295
REMARK 3 S TENSOR
REMARK 3 S11: 0.0279 S12: 0.0486 S13: -0.0738
REMARK 3 S21: -0.0478 S22: -0.0474 S23: -0.1880
REMARK 3 S31: 0.0539 S32: 0.0847 S33: 0.0213
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: (CHAIN A AND (RESID 16 THROUGH 255 OR
REMARK 3 RESID 257 THROUGH 334 OR RESID 401))
REMARK 3 SELECTION : (CHAIN B AND (RESID 16 THROUGH 255 OR
REMARK 3 RESID 257 THROUGH 334 OR RESID 401))
REMARK 3 ATOM PAIRS NUMBER : 2904
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: (CHAIN A AND (RESID 16 THROUGH 255 OR
REMARK 3 RESID 257 THROUGH 334 OR RESID 401))
REMARK 3 SELECTION : (CHAIN C AND (RESID 16 THROUGH 255 OR
REMARK 3 RESID 257 THROUGH 334 OR RESID 401))
REMARK 3 ATOM PAIRS NUMBER : 2904
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6UNW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-OCT-19.
REMARK 100 THE DEPOSITION ID IS D_1000244922.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-OCT-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : LNLS
REMARK 200 BEAMLINE : W01B-MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.45
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.2.8
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 67798
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.210
REMARK 200 RESOLUTION RANGE LOW (A) : 48.520
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 17.50
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 21.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.21
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.26
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.0
REMARK 200 DATA REDUNDANCY IN SHELL : 11.90
REMARK 200 R MERGE FOR SHELL (I) : 1.24200
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: 2E3J
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS-CITRATE, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+1/4
REMARK 290 4555 Y,-X,Z+3/4
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z+1/2
REMARK 290 7555 Y,X,-Z+3/4
REMARK 290 8555 -Y,-X,-Z+1/4
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 116.51950
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 58.25975
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 174.77925
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 116.51950
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 174.77925
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 58.25975
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 567 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 668 LIES ON A SPECIAL POSITION.
REMARK 375 HOH C 617 LIES ON A SPECIAL POSITION.
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 VAL A 1
REMARK 465 PRO A 2
REMARK 465 GLN A 3
REMARK 465 PRO A 4
REMARK 465 PRO A 5
REMARK 465 THR A 6
REMARK 465 ASP A 7
REMARK 465 ASP A 8
REMARK 465 PRO A 9
REMARK 465 THR A 10
REMARK 465 THR A 11
REMARK 465 PRO A 12
REMARK 465 ALA A 13
REMARK 465 SER A 337
REMARK 465 SER A 338
REMARK 465 VAL A 339
REMARK 465 ASP A 340
REMARK 465 LYS A 341
REMARK 465 LEU A 342
REMARK 465 ALA A 343
REMARK 465 ALA A 344
REMARK 465 ALA A 345
REMARK 465 VAL B 1
REMARK 465 PRO B 2
REMARK 465 GLN B 3
REMARK 465 PRO B 4
REMARK 465 PRO B 5
REMARK 465 THR B 6
REMARK 465 ASP B 7
REMARK 465 ASP B 8
REMARK 465 PRO B 9
REMARK 465 THR B 10
REMARK 465 THR B 11
REMARK 465 PRO B 12
REMARK 465 ALA B 13
REMARK 465 SER B 336
REMARK 465 SER B 337
REMARK 465 SER B 338
REMARK 465 VAL B 339
REMARK 465 ASP B 340
REMARK 465 LYS B 341
REMARK 465 LEU B 342
REMARK 465 ALA B 343
REMARK 465 ALA B 344
REMARK 465 ALA B 345
REMARK 465 LEU B 346
REMARK 465 GLU B 347
REMARK 465 HIS B 348
REMARK 465 HIS B 349
REMARK 465 HIS B 350
REMARK 465 HIS B 351
REMARK 465 HIS B 352
REMARK 465 HIS B 353
REMARK 465 VAL C 1
REMARK 465 PRO C 2
REMARK 465 GLN C 3
REMARK 465 PRO C 4
REMARK 465 PRO C 5
REMARK 465 THR C 6
REMARK 465 ASP C 7
REMARK 465 ASP C 8
REMARK 465 PRO C 9
REMARK 465 THR C 10
REMARK 465 THR C 11
REMARK 465 PRO C 12
REMARK 465 ALA C 13
REMARK 465 GLU C 14
REMARK 465 LYS C 15
REMARK 465 SER C 336
REMARK 465 SER C 337
REMARK 465 SER C 338
REMARK 465 VAL C 339
REMARK 465 ASP C 340
REMARK 465 LYS C 341
REMARK 465 LEU C 342
REMARK 465 ALA C 343
REMARK 465 ALA C 344
REMARK 465 ALA C 345
REMARK 465 LEU C 346
REMARK 465 GLU C 347
REMARK 465 HIS C 348
REMARK 465 HIS C 349
REMARK 465 HIS C 350
REMARK 465 HIS C 351
REMARK 465 HIS C 352
REMARK 465 HIS C 353
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 347 CG CD OE1 OE2
REMARK 470 ASN B 335 CG OD1 ND2
REMARK 470 ASN C 335 CG OD1 ND2
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 OH TYR B 251 O2 CAC B 401 2.01
REMARK 500 OE2 GLU A 321 NH2 ARG A 324 2.06
REMARK 500 O HOH A 658 O HOH A 699 2.09
REMARK 500 O HOH B 515 O HOH B 584 2.17
REMARK 500 O HOH A 605 O HOH A 650 2.17
REMARK 500 O HOH A 659 O HOH A 686 2.19
REMARK 500 O HOH A 681 O HOH B 660 2.19
REMARK 500 O HOH C 564 O HOH C 672 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH B 671 O HOH C 645 3555 1.87
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 GLU C 146 CD GLU C 146 OE1 0.076
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 ARG B 20 NE - CZ - NH1 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG B 20 NE - CZ - NH2 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG B 250 NE - CZ - NH1 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ASP C 159 C - N - CA ANGL. DEV. = -16.6 DEGREES
REMARK 500 ASP C 159 CB - CG - OD1 ANGL. DEV. = 11.5 DEGREES
REMARK 500 ASP C 159 CB - CG - OD2 ANGL. DEV. = -20.7 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 GLU A 48 -144.90 -120.48
REMARK 500 ASP A 114 -124.80 55.22
REMARK 500 SER A 138 -49.98 68.34
REMARK 500 ASP A 159 -80.25 -21.60
REMARK 500 ASP A 180 84.46 -170.53
REMARK 500 GLN A 271 157.63 -49.45
REMARK 500 GLU B 48 -146.81 -121.64
REMARK 500 ASP B 114 -124.82 58.52
REMARK 500 SER B 138 -46.46 69.56
REMARK 500 ASP B 180 82.87 -167.76
REMARK 500 GLU C 48 -143.63 -118.99
REMARK 500 ASP C 114 -124.21 57.27
REMARK 500 SER C 138 -47.03 69.64
REMARK 500 ALA C 154 -74.05 -67.98
REMARK 500 ARG C 155 20.23 -67.91
REMARK 500 ASP C 159 -105.40 37.28
REMARK 500 ASP C 180 86.02 -169.73
REMARK 500 GLU C 200 -73.88 1.83
REMARK 500 ARG C 334 55.23 -92.21
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 GLY A 158 ASP A 159 135.34
REMARK 500 GLY C 158 ASP C 159 103.24
REMARK 500 PRO C 199 GLU C 200 129.84
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 250 0.08 SIDE CHAIN
REMARK 500 ARG B 250 0.08 SIDE CHAIN
REMARK 500 ARG C 155 0.09 SIDE CHAIN
REMARK 500 ASP C 159 0.11 SIDE CHAIN
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 A 709 DISTANCE = 6.14 ANGSTROMS
REMARK 525 HOH A 710 DISTANCE = 7.46 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CAC A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CAC B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CAC C 401
DBREF 6UNW A 1 353 PDB 6UNW 6UNW 1 353
DBREF 6UNW B 1 353 PDB 6UNW 6UNW 1 353
DBREF 6UNW C 1 353 PDB 6UNW 6UNW 1 353
SEQRES 1 A 353 VAL PRO GLN PRO PRO THR ASP ASP PRO THR THR PRO ALA
SEQRES 2 A 353 GLU LYS GLY ALA VAL HIS ARG LEU VAL ASP THR PRO GLY
SEQRES 3 A 353 GLY ARG ILE HIS LEU VAL GLU GLN GLY THR GLY PRO LEU
SEQRES 4 A 353 VAL LEU LEU VAL HIS GLY PHE PRO GLU SER TRP TYR SER
SEQRES 5 A 353 TRP ARG HIS GLN LEU PRO ALA LEU ALA ALA ALA GLY TYR
SEQRES 6 A 353 ARG ALA ALA ALA ILE ASP VAL ARG GLY TYR GLY ARG SER
SEQRES 7 A 353 ALA LYS PRO ALA ALA THR ASP ALA TYR ARG MET LEU ALA
SEQRES 8 A 353 HIS VAL ALA ASP ASN THR ALA VAL VAL HIS ALA LEU GLY
SEQRES 9 A 353 GLU GLU THR ALA THR VAL VAL GLY HIS ASP TRP GLY SER
SEQRES 10 A 353 PRO ILE ALA ALA ASN SER ALA LEU LEU ARG PRO ASP VAL
SEQRES 11 A 353 PHE THR ALA VAL GLY LEU LEU SER VAL PRO TYR ALA PRO
SEQRES 12 A 353 ARG GLY GLU HIS ARG PRO THR ASP GLY PHE ALA ARG ILE
SEQRES 13 A 353 GLY GLY ASP GLU GLU PHE TYR VAL SER TYR PHE GLN ALA
SEQRES 14 A 353 PRO GLY ARG ALA GLU ALA GLU ILE GLU ARG ASP VAL ARG
SEQRES 15 A 353 GLY TRP LEU ALA GLY PHE TYR THR GLY LEU THR GLY GLY
SEQRES 16 A 353 ALA LEU THR PRO GLU GLU HIS GLY ARG LEU PHE PHE VAL
SEQRES 17 A 353 PRO PRO GLY ALA HIS LEU ALA ASP ARG PHE PRO THR GLY
SEQRES 18 A 353 PRO LEU PRO ALA TRP LEU THR GLU ALA ASP LEU ASP VAL
SEQRES 19 A 353 TYR SER GLY GLU PHE GLU ARG SER GLY LEU THR GLY ALA
SEQRES 20 A 353 LEU ASN ARG TYR ARG ASN VAL ASP ARG ASP TRP GLU ASP
SEQRES 21 A 353 LEU ALA ALA TRP HIS GLY ALA PRO ILE THR GLN PRO SER
SEQRES 22 A 353 LEU PHE ILE GLY GLY ALA LEU ASP ALA SER THR THR TRP
SEQRES 23 A 353 MET ALA ASP ALA LEU ASP ALA TYR PRO ALA THR LEU PRO
SEQRES 24 A 353 GLY LEU SER ALA ALA HIS ILE LEU GLU GLY CYS GLY HIS
SEQRES 25 A 353 TRP ILE GLN GLN GLU ARG PRO ASP GLU VAL ASN ARG LEU
SEQRES 26 A 353 LEU THR GLN TRP LEU ASP GLY LEU ARG ASN SER SER SER
SEQRES 27 A 353 VAL ASP LYS LEU ALA ALA ALA LEU GLU HIS HIS HIS HIS
SEQRES 28 A 353 HIS HIS
SEQRES 1 B 353 VAL PRO GLN PRO PRO THR ASP ASP PRO THR THR PRO ALA
SEQRES 2 B 353 GLU LYS GLY ALA VAL HIS ARG LEU VAL ASP THR PRO GLY
SEQRES 3 B 353 GLY ARG ILE HIS LEU VAL GLU GLN GLY THR GLY PRO LEU
SEQRES 4 B 353 VAL LEU LEU VAL HIS GLY PHE PRO GLU SER TRP TYR SER
SEQRES 5 B 353 TRP ARG HIS GLN LEU PRO ALA LEU ALA ALA ALA GLY TYR
SEQRES 6 B 353 ARG ALA ALA ALA ILE ASP VAL ARG GLY TYR GLY ARG SER
SEQRES 7 B 353 ALA LYS PRO ALA ALA THR ASP ALA TYR ARG MET LEU ALA
SEQRES 8 B 353 HIS VAL ALA ASP ASN THR ALA VAL VAL HIS ALA LEU GLY
SEQRES 9 B 353 GLU GLU THR ALA THR VAL VAL GLY HIS ASP TRP GLY SER
SEQRES 10 B 353 PRO ILE ALA ALA ASN SER ALA LEU LEU ARG PRO ASP VAL
SEQRES 11 B 353 PHE THR ALA VAL GLY LEU LEU SER VAL PRO TYR ALA PRO
SEQRES 12 B 353 ARG GLY GLU HIS ARG PRO THR ASP GLY PHE ALA ARG ILE
SEQRES 13 B 353 GLY GLY ASP GLU GLU PHE TYR VAL SER TYR PHE GLN ALA
SEQRES 14 B 353 PRO GLY ARG ALA GLU ALA GLU ILE GLU ARG ASP VAL ARG
SEQRES 15 B 353 GLY TRP LEU ALA GLY PHE TYR THR GLY LEU THR GLY GLY
SEQRES 16 B 353 ALA LEU THR PRO GLU GLU HIS GLY ARG LEU PHE PHE VAL
SEQRES 17 B 353 PRO PRO GLY ALA HIS LEU ALA ASP ARG PHE PRO THR GLY
SEQRES 18 B 353 PRO LEU PRO ALA TRP LEU THR GLU ALA ASP LEU ASP VAL
SEQRES 19 B 353 TYR SER GLY GLU PHE GLU ARG SER GLY LEU THR GLY ALA
SEQRES 20 B 353 LEU ASN ARG TYR ARG ASN VAL ASP ARG ASP TRP GLU ASP
SEQRES 21 B 353 LEU ALA ALA TRP HIS GLY ALA PRO ILE THR GLN PRO SER
SEQRES 22 B 353 LEU PHE ILE GLY GLY ALA LEU ASP ALA SER THR THR TRP
SEQRES 23 B 353 MET ALA ASP ALA LEU ASP ALA TYR PRO ALA THR LEU PRO
SEQRES 24 B 353 GLY LEU SER ALA ALA HIS ILE LEU GLU GLY CYS GLY HIS
SEQRES 25 B 353 TRP ILE GLN GLN GLU ARG PRO ASP GLU VAL ASN ARG LEU
SEQRES 26 B 353 LEU THR GLN TRP LEU ASP GLY LEU ARG ASN SER SER SER
SEQRES 27 B 353 VAL ASP LYS LEU ALA ALA ALA LEU GLU HIS HIS HIS HIS
SEQRES 28 B 353 HIS HIS
SEQRES 1 C 353 VAL PRO GLN PRO PRO THR ASP ASP PRO THR THR PRO ALA
SEQRES 2 C 353 GLU LYS GLY ALA VAL HIS ARG LEU VAL ASP THR PRO GLY
SEQRES 3 C 353 GLY ARG ILE HIS LEU VAL GLU GLN GLY THR GLY PRO LEU
SEQRES 4 C 353 VAL LEU LEU VAL HIS GLY PHE PRO GLU SER TRP TYR SER
SEQRES 5 C 353 TRP ARG HIS GLN LEU PRO ALA LEU ALA ALA ALA GLY TYR
SEQRES 6 C 353 ARG ALA ALA ALA ILE ASP VAL ARG GLY TYR GLY ARG SER
SEQRES 7 C 353 ALA LYS PRO ALA ALA THR ASP ALA TYR ARG MET LEU ALA
SEQRES 8 C 353 HIS VAL ALA ASP ASN THR ALA VAL VAL HIS ALA LEU GLY
SEQRES 9 C 353 GLU GLU THR ALA THR VAL VAL GLY HIS ASP TRP GLY SER
SEQRES 10 C 353 PRO ILE ALA ALA ASN SER ALA LEU LEU ARG PRO ASP VAL
SEQRES 11 C 353 PHE THR ALA VAL GLY LEU LEU SER VAL PRO TYR ALA PRO
SEQRES 12 C 353 ARG GLY GLU HIS ARG PRO THR ASP GLY PHE ALA ARG ILE
SEQRES 13 C 353 GLY GLY ASP GLU GLU PHE TYR VAL SER TYR PHE GLN ALA
SEQRES 14 C 353 PRO GLY ARG ALA GLU ALA GLU ILE GLU ARG ASP VAL ARG
SEQRES 15 C 353 GLY TRP LEU ALA GLY PHE TYR THR GLY LEU THR GLY GLY
SEQRES 16 C 353 ALA LEU THR PRO GLU GLU HIS GLY ARG LEU PHE PHE VAL
SEQRES 17 C 353 PRO PRO GLY ALA HIS LEU ALA ASP ARG PHE PRO THR GLY
SEQRES 18 C 353 PRO LEU PRO ALA TRP LEU THR GLU ALA ASP LEU ASP VAL
SEQRES 19 C 353 TYR SER GLY GLU PHE GLU ARG SER GLY LEU THR GLY ALA
SEQRES 20 C 353 LEU ASN ARG TYR ARG ASN VAL ASP ARG ASP TRP GLU ASP
SEQRES 21 C 353 LEU ALA ALA TRP HIS GLY ALA PRO ILE THR GLN PRO SER
SEQRES 22 C 353 LEU PHE ILE GLY GLY ALA LEU ASP ALA SER THR THR TRP
SEQRES 23 C 353 MET ALA ASP ALA LEU ASP ALA TYR PRO ALA THR LEU PRO
SEQRES 24 C 353 GLY LEU SER ALA ALA HIS ILE LEU GLU GLY CYS GLY HIS
SEQRES 25 C 353 TRP ILE GLN GLN GLU ARG PRO ASP GLU VAL ASN ARG LEU
SEQRES 26 C 353 LEU THR GLN TRP LEU ASP GLY LEU ARG ASN SER SER SER
SEQRES 27 C 353 VAL ASP LYS LEU ALA ALA ALA LEU GLU HIS HIS HIS HIS
SEQRES 28 C 353 HIS HIS
HET CAC A 401 5
HET CL A 402 1
HET CL A 403 1
HET CL A 404 1
HET CAC B 401 5
HET CL B 402 1
HET CAC C 401 5
HET CL C 402 1
HETNAM CAC CACODYLATE ION
HETNAM CL CHLORIDE ION
HETSYN CAC DIMETHYLARSINATE
FORMUL 4 CAC 3(C2 H6 AS O2 1-)
FORMUL 5 CL 5(CL 1-)
FORMUL 12 HOH *593(H2 O)
HELIX 1 AA1 SER A 49 ARG A 54 5 6
HELIX 2 AA2 HIS A 55 ALA A 63 1 9
HELIX 3 AA3 ALA A 83 TYR A 87 5 5
HELIX 4 AA4 ARG A 88 LEU A 103 1 16
HELIX 5 AA5 TRP A 115 ARG A 127 1 13
HELIX 6 AA6 ARG A 148 ILE A 156 1 9
HELIX 7 AA7 TYR A 163 PHE A 167 1 5
HELIX 8 AA8 GLY A 171 ARG A 179 1 9
HELIX 9 AA9 ASP A 180 LEU A 192 1 13
HELIX 10 AB1 THR A 198 LEU A 205 1 8
HELIX 11 AB2 HIS A 213 PHE A 218 5 6
HELIX 12 AB3 THR A 228 GLY A 243 1 16
HELIX 13 AB4 LEU A 244 ARG A 252 1 9
HELIX 14 AB5 ASN A 253 LEU A 261 1 9
HELIX 15 AB6 ALA A 262 HIS A 265 5 4
HELIX 16 AB7 ASP A 281 TRP A 286 1 6
HELIX 17 AB8 MET A 287 ALA A 293 1 7
HELIX 18 AB9 ALA A 293 LEU A 298 1 6
HELIX 19 AC1 TRP A 313 ARG A 318 1 6
HELIX 20 AC2 ARG A 318 SER A 336 1 19
HELIX 21 AC3 SER B 49 ARG B 54 5 6
HELIX 22 AC4 HIS B 55 ALA B 63 1 9
HELIX 23 AC5 ALA B 83 TYR B 87 5 5
HELIX 24 AC6 ARG B 88 LEU B 103 1 16
HELIX 25 AC7 TRP B 115 ARG B 127 1 13
HELIX 26 AC8 ARG B 148 ILE B 156 1 9
HELIX 27 AC9 TYR B 163 PHE B 167 1 5
HELIX 28 AD1 GLY B 171 ARG B 179 1 9
HELIX 29 AD2 ASP B 180 LEU B 192 1 13
HELIX 30 AD3 THR B 198 LEU B 205 1 8
HELIX 31 AD4 HIS B 213 PHE B 218 5 6
HELIX 32 AD5 THR B 228 GLY B 243 1 16
HELIX 33 AD6 LEU B 244 ARG B 252 1 9
HELIX 34 AD7 ASN B 253 LEU B 261 1 9
HELIX 35 AD8 ALA B 262 HIS B 265 5 4
HELIX 36 AD9 ASP B 281 TRP B 286 1 6
HELIX 37 AE1 MET B 287 ALA B 293 1 7
HELIX 38 AE2 ALA B 293 LEU B 298 1 6
HELIX 39 AE3 TRP B 313 ARG B 318 1 6
HELIX 40 AE4 ARG B 318 ARG B 334 1 17
HELIX 41 AE5 SER C 49 ARG C 54 5 6
HELIX 42 AE6 HIS C 55 ALA C 63 1 9
HELIX 43 AE7 ALA C 83 TYR C 87 5 5
HELIX 44 AE8 ARG C 88 LEU C 103 1 16
HELIX 45 AE9 TRP C 115 ARG C 127 1 13
HELIX 46 AF1 ARG C 148 ARG C 155 1 8
HELIX 47 AF2 TYR C 163 PHE C 167 1 5
HELIX 48 AF3 GLY C 171 ARG C 179 1 9
HELIX 49 AF4 ASP C 180 LEU C 192 1 13
HELIX 50 AF5 THR C 198 PHE C 206 1 9
HELIX 51 AF6 HIS C 213 PHE C 218 5 6
HELIX 52 AF7 THR C 228 GLY C 243 1 16
HELIX 53 AF8 LEU C 244 ARG C 252 1 9
HELIX 54 AF9 ASN C 253 LEU C 261 1 9
HELIX 55 AG1 ALA C 262 HIS C 265 5 4
HELIX 56 AG2 ASP C 281 TRP C 286 1 6
HELIX 57 AG3 MET C 287 ALA C 293 1 7
HELIX 58 AG4 ALA C 293 LEU C 298 1 6
HELIX 59 AG5 TRP C 313 ARG C 318 1 6
HELIX 60 AG6 ARG C 318 ARG C 334 1 17
SHEET 1 AA1 9 VAL A 18 THR A 24 0
SHEET 2 AA1 9 GLY A 27 GLN A 34 -1 O ILE A 29 N VAL A 22
SHEET 3 AA1 9 ARG A 66 ILE A 70 -1 O ALA A 69 N VAL A 32
SHEET 4 AA1 9 LEU A 39 VAL A 43 1 N VAL A 40 O ARG A 66
SHEET 5 AA1 9 ALA A 108 HIS A 113 1 O VAL A 111 N LEU A 41
SHEET 6 AA1 9 PHE A 131 LEU A 137 1 O GLY A 135 N VAL A 110
SHEET 7 AA1 9 SER A 273 GLY A 278 1 O LEU A 274 N LEU A 136
SHEET 8 AA1 9 LEU A 301 LEU A 307 1 O SER A 302 N SER A 273
SHEET 9 AA1 9 HIS A 348 HIS A 351 1 O HIS A 349 N ALA A 304
SHEET 1 AA2 2 GLU A 161 PHE A 162 0
SHEET 2 AA2 2 PHE A 207 VAL A 208 -1 O VAL A 208 N GLU A 161
SHEET 1 AA3 8 VAL B 18 THR B 24 0
SHEET 2 AA3 8 GLY B 27 GLN B 34 -1 O GLU B 33 N VAL B 18
SHEET 3 AA3 8 ARG B 66 ILE B 70 -1 O ALA B 69 N VAL B 32
SHEET 4 AA3 8 LEU B 39 VAL B 43 1 N VAL B 40 O ARG B 66
SHEET 5 AA3 8 ALA B 108 HIS B 113 1 O VAL B 111 N LEU B 41
SHEET 6 AA3 8 PHE B 131 LEU B 137 1 O LEU B 137 N GLY B 112
SHEET 7 AA3 8 SER B 273 GLY B 278 1 O LEU B 274 N LEU B 136
SHEET 8 AA3 8 LEU B 301 LEU B 307 1 O HIS B 305 N PHE B 275
SHEET 1 AA4 2 GLU B 161 PHE B 162 0
SHEET 2 AA4 2 PHE B 207 VAL B 208 -1 O VAL B 208 N GLU B 161
SHEET 1 AA5 8 VAL C 18 THR C 24 0
SHEET 2 AA5 8 GLY C 27 GLN C 34 -1 O GLU C 33 N VAL C 18
SHEET 3 AA5 8 ARG C 66 ILE C 70 -1 O ALA C 69 N VAL C 32
SHEET 4 AA5 8 LEU C 39 VAL C 43 1 N LEU C 42 O ALA C 68
SHEET 5 AA5 8 ALA C 108 HIS C 113 1 O VAL C 111 N LEU C 41
SHEET 6 AA5 8 PHE C 131 LEU C 137 1 O LEU C 137 N GLY C 112
SHEET 7 AA5 8 SER C 273 GLY C 278 1 O LEU C 274 N LEU C 136
SHEET 8 AA5 8 LEU C 301 LEU C 307 1 O SER C 302 N SER C 273
SHEET 1 AA6 2 GLU C 161 PHE C 162 0
SHEET 2 AA6 2 PHE C 207 VAL C 208 -1 O VAL C 208 N GLU C 161
CISPEP 1 PHE A 46 PRO A 47 0 -8.86
CISPEP 2 PHE B 46 PRO B 47 0 -9.64
CISPEP 3 PHE C 46 PRO C 47 0 -9.52
SITE 1 AC1 5 ASP A 114 TRP A 115 TYR A 163 TYR A 251
SITE 2 AC1 5 SER A 283
SITE 1 AC2 7 PHE B 46 ASP B 114 TYR B 163 PHE B 206
SITE 2 AC2 7 TYR B 251 HIS B 312 HOH B 504
SITE 1 AC3 7 PHE C 46 ASP C 114 TRP C 115 TYR C 163
SITE 2 AC3 7 TYR C 251 SER C 283 HIS C 312
CRYST1 106.733 106.733 233.039 90.00 90.00 90.00 P 41 2 2 24
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 0.009369 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009369 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004291 0.00000
TER 2554 HIS A 353
TER 5026 ASN B 335
TER 7488 ASN C 335
MASTER 545 0 8 60 31 0 6 6 8090 3 15 84
END |