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HEADER UNKNOWN FUNCTION 05-OCT-20 7AL5
TITLE CRYSTAL STRUCTURE OF THE SELENOMETHIONINE SUBSTITUTED HYPOTHETICAL
TITLE 2 PROTEIN PA1622 FROM PSEUDOMONAS AERUGINOSA PAO1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE HYDROLASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA (STRAIN ATCC 15692 / DSM
SOURCE 3 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1);
SOURCE 4 ORGANISM_TAXID: 208964;
SOURCE 5 STRAIN: ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228
SOURCE 6 / 1C / PRS 101 / PAO1;
SOURCE 7 GENE: PA1622;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: P10$
KEYWDS ESTERASE FOLD, HYPOTHETICAL PROTEIN, PSEUDOMONAS AERUGINOSA PAO1,
KEYWDS 2 POSSIBLE DRUG TARGET, SELENOMETHIONINE, ALPHA/BETA HYDROLASE FOLD,
KEYWDS 3 PUTATIVE LIPOLYTIC ENZYME, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR C.G.FEILER,W.BLANKENFELDT
REVDAT 1 11-NOV-20 7AL5 0
JRNL AUTH C.G.FEILER,W.BLANKENFELDT
JRNL TITL CRYSTAL STRUCTURE OF THE SELENOMETHIONINE SUBSTITUTED
JRNL TITL 2 HYPOTHETICAL PROTEIN PA1622 FROM PSEUDOMONAS AERUGINOSA PAO1
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.42 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.18.2_3874: ???)
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) : 2.42
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.93
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 59516
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.164
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.950
REMARK 3 FREE R VALUE TEST SET COUNT : 2946
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 19.9300 - 6.5900 1.00 2756 138 0.1567 0.2051
REMARK 3 2 6.5800 - 5.2600 1.00 2709 138 0.1633 0.2102
REMARK 3 3 5.2600 - 4.6000 1.00 2738 141 0.1218 0.1719
REMARK 3 4 4.6000 - 4.1900 1.00 2694 154 0.1209 0.1828
REMARK 3 5 4.1900 - 3.8900 1.00 2682 151 0.1251 0.1834
REMARK 3 6 3.8900 - 3.6600 1.00 2694 153 0.1361 0.2093
REMARK 3 7 3.6600 - 3.4800 1.00 2707 133 0.1423 0.2216
REMARK 3 8 3.4800 - 3.3300 1.00 2685 149 0.1480 0.2147
REMARK 3 9 3.3300 - 3.2000 1.00 2707 138 0.1685 0.2658
REMARK 3 10 3.2000 - 3.0900 1.00 2699 143 0.1742 0.2303
REMARK 3 11 3.0900 - 2.9900 1.00 2713 136 0.1705 0.2533
REMARK 3 12 2.9900 - 2.9100 1.00 2697 122 0.1757 0.2479
REMARK 3 13 2.9100 - 2.8300 1.00 2702 129 0.1728 0.2507
REMARK 3 14 2.8300 - 2.7600 1.00 2705 130 0.1924 0.3003
REMARK 3 15 2.7600 - 2.7000 1.00 2692 138 0.1994 0.2497
REMARK 3 16 2.7000 - 2.6400 1.00 2675 162 0.2107 0.3148
REMARK 3 17 2.6400 - 2.5900 1.00 2714 108 0.2079 0.3042
REMARK 3 18 2.5900 - 2.5400 1.00 2687 125 0.2193 0.2501
REMARK 3 19 2.5400 - 2.5000 1.00 2689 151 0.2353 0.2914
REMARK 3 20 2.5000 - 2.4500 1.00 2640 169 0.2522 0.2979
REMARK 3 21 2.4500 - 2.4200 0.95 2585 138 0.2839 0.3683
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) : 0.320
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.900
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 : 0.014 8977
REMARK 3 ANGLE : 1.750 12167
REMARK 3 CHIRALITY : 0.066 1356
REMARK 3 PLANARITY : 0.011 1581
REMARK 3 DIHEDRAL : 23.462 1249
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 7AL5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-OCT-20.
REMARK 100 THE DEPOSITION ID IS D_1292111611.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-NOV-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8 - 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.976000
REMARK 200 MONOCHROMATOR : SI111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59611
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.420
REMARK 200 RESOLUTION RANGE LOW (A) : 19.930
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 22.90
REMARK 200 R MERGE (I) : 0.43000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.42
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) : 2.55500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXCD
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.25
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES PH7 5% PEG 6000, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
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 49.40367
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 98.80733
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 74.10550
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 123.50917
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 24.70183
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 43510 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -68.0 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 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 174
REMARK 465 GLY A 175
REMARK 465 MSE B 1
REMARK 465 GLY B 173
REMARK 465 VAL B 174
REMARK 465 MSE C 1
REMARK 465 GLY C 173
REMARK 465 MSE D 1
REMARK 465 SER D 2
REMARK 465 LEU D 3
REMARK 465 GLN D 4
REMARK 465 VAL D 174
REMARK 465 GLY D 175
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 HE1 MSE C 171 HD2 ARG C 179 1.34
REMARK 500 HE ARG B 179 OE2 GLU B 183 1.47
REMARK 500 HH22 ARG D 45 OE1 GLU D 180 1.58
REMARK 500 O GLU B 94 HE ARG B 118 1.58
REMARK 500 OD1 ASP B 269 H GLY B 272 1.60
REMARK 500 OE1 GLU A 255 O HOH A 401 1.62
REMARK 500 OD1 ASN B 220 O HOH B 401 2.10
REMARK 500 OE2 GLU A 144 O HOH A 402 2.16
REMARK 500 O HOH B 402 O HOH B 444 2.16
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 A 255 CD GLU A 255 OE2 -0.077
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 MSE C 171 CG - SE - CE ANGL. DEV. = 22.8 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 37 -0.32 75.60
REMARK 500 ASP A 38 -155.03 -92.16
REMARK 500 TYR A 75 60.19 -112.52
REMARK 500 GLU A 94 -70.67 -90.22
REMARK 500 SER A 102 -123.27 55.04
REMARK 500 LEU A 128 -67.33 -147.21
REMARK 500 PRO A 253 22.01 -79.67
REMARK 500 LEU B 50 77.70 -113.77
REMARK 500 TYR B 75 64.27 -116.14
REMARK 500 GLU B 94 -60.78 -92.43
REMARK 500 SER B 102 -120.76 53.60
REMARK 500 LEU B 128 -65.96 -149.07
REMARK 500 HIS B 264 40.56 -109.30
REMARK 500 LEU B 267 -33.24 -132.55
REMARK 500 LEU C 37 11.27 57.37
REMARK 500 ASP C 38 -155.44 -90.18
REMARK 500 TYR C 75 61.97 -115.11
REMARK 500 GLU C 94 -81.02 -88.62
REMARK 500 SER C 102 -120.61 56.38
REMARK 500 LEU C 128 -66.28 -150.12
REMARK 500 ASP D 38 -156.43 -94.95
REMARK 500 LEU D 50 70.13 -112.57
REMARK 500 TYR D 75 60.65 -110.72
REMARK 500 GLU D 94 -63.45 -105.27
REMARK 500 SER D 102 -116.70 54.13
REMARK 500 LEU D 128 -64.16 -146.21
REMARK 500 LEU D 211 105.87 -167.54
REMARK 500
REMARK 500 REMARK: NULL
DBREF 7AL5 A 1 286 UNP Q9I3A0 Q9I3A0_PSEAE 1 286
DBREF 7AL5 B 1 286 UNP Q9I3A0 Q9I3A0_PSEAE 1 286
DBREF 7AL5 C 1 286 UNP Q9I3A0 Q9I3A0_PSEAE 1 286
DBREF 7AL5 D 1 286 UNP Q9I3A0 Q9I3A0_PSEAE 1 286
SEQRES 1 A 286 MSE SER LEU GLN VAL GLU GLU VAL ARG ILE SER LEU PRO
SEQRES 2 A 286 HIS ILE GLU LEU ALA ALA HIS LEU PHE GLY PRO PRO ASP
SEQRES 3 A 286 GLY LYS PRO VAL ILE ALA LEU HIS GLY TRP LEU ASP ASN
SEQRES 4 A 286 ALA MSE SER PHE SER ARG LEU ALA PRO LYS LEU ALA GLY
SEQRES 5 A 286 LEU ARG ILE VAL ALA LEU ASP PHE ALA GLY HIS GLY HIS
SEQRES 6 A 286 SER ALA HIS ARG ALA GLU GLY ALA SER TYR LEU LEU TRP
SEQRES 7 A 286 ASP TYR ALA LEU ASP VAL LEU MSE VAL ALA GLU GLN LEU
SEQRES 8 A 286 GLY TRP GLU ARG PHE SER LEU LEU GLY HIS SER MSE GLY
SEQRES 9 A 286 ALA ILE VAL SER VAL LEU LEU ALA GLY ALA LEU PRO GLU
SEQRES 10 A 286 ARG ILE GLU ARG LEU ALA LEU ILE ASP GLY LEU ILE PRO
SEQRES 11 A 286 TYR THR GLY GLU ALA ASP LYS ALA PRO GLN LYS LEU GLY
SEQRES 12 A 286 GLU ALA LEU LYS ALA GLN LEU ALA LEU ARG HIS LYS ARG
SEQRES 13 A 286 LYS PRO VAL TYR ALA GLU LEU GLU LYS ALA VAL GLU ALA
SEQRES 14 A 286 ARG MSE ARG GLY VAL GLY GLU ILE SER ARG GLU ALA ALA
SEQRES 15 A 286 GLU LEU LEU ALA GLN ARG GLY LEU GLU PRO VAL PRO GLY
SEQRES 16 A 286 GLY TYR THR TRP ARG THR ASP ALA ARG LEU THR LEU PRO
SEQRES 17 A 286 SER PRO LEU ARG LEU THR GLN ALA HIS ALA LEU ASN PHE
SEQRES 18 A 286 VAL ARG SER VAL GLU CYS PRO VAL SER LEU VAL LEU ALA
SEQRES 19 A 286 GLU GLN GLY MSE LEU ALA VAL GLU PRO ARG MSE ARG ALA
SEQRES 20 A 286 LEU LEU GLU THR LEU PRO PHE GLU ARG HIS HIS LEU PRO
SEQRES 21 A 286 GLY GLY HIS HIS LEU HIS LEU ASP ASP GLU ALA GLY ALA
SEQRES 22 A 286 GLN ALA VAL ALA ARG VAL PHE ALA ALA PHE PHE ALA ARG
SEQRES 1 B 286 MSE SER LEU GLN VAL GLU GLU VAL ARG ILE SER LEU PRO
SEQRES 2 B 286 HIS ILE GLU LEU ALA ALA HIS LEU PHE GLY PRO PRO ASP
SEQRES 3 B 286 GLY LYS PRO VAL ILE ALA LEU HIS GLY TRP LEU ASP ASN
SEQRES 4 B 286 ALA MSE SER PHE SER ARG LEU ALA PRO LYS LEU ALA GLY
SEQRES 5 B 286 LEU ARG ILE VAL ALA LEU ASP PHE ALA GLY HIS GLY HIS
SEQRES 6 B 286 SER ALA HIS ARG ALA GLU GLY ALA SER TYR LEU LEU TRP
SEQRES 7 B 286 ASP TYR ALA LEU ASP VAL LEU MSE VAL ALA GLU GLN LEU
SEQRES 8 B 286 GLY TRP GLU ARG PHE SER LEU LEU GLY HIS SER MSE GLY
SEQRES 9 B 286 ALA ILE VAL SER VAL LEU LEU ALA GLY ALA LEU PRO GLU
SEQRES 10 B 286 ARG ILE GLU ARG LEU ALA LEU ILE ASP GLY LEU ILE PRO
SEQRES 11 B 286 TYR THR GLY GLU ALA ASP LYS ALA PRO GLN LYS LEU GLY
SEQRES 12 B 286 GLU ALA LEU LYS ALA GLN LEU ALA LEU ARG HIS LYS ARG
SEQRES 13 B 286 LYS PRO VAL TYR ALA GLU LEU GLU LYS ALA VAL GLU ALA
SEQRES 14 B 286 ARG MSE ARG GLY VAL GLY GLU ILE SER ARG GLU ALA ALA
SEQRES 15 B 286 GLU LEU LEU ALA GLN ARG GLY LEU GLU PRO VAL PRO GLY
SEQRES 16 B 286 GLY TYR THR TRP ARG THR ASP ALA ARG LEU THR LEU PRO
SEQRES 17 B 286 SER PRO LEU ARG LEU THR GLN ALA HIS ALA LEU ASN PHE
SEQRES 18 B 286 VAL ARG SER VAL GLU CYS PRO VAL SER LEU VAL LEU ALA
SEQRES 19 B 286 GLU GLN GLY MSE LEU ALA VAL GLU PRO ARG MSE ARG ALA
SEQRES 20 B 286 LEU LEU GLU THR LEU PRO PHE GLU ARG HIS HIS LEU PRO
SEQRES 21 B 286 GLY GLY HIS HIS LEU HIS LEU ASP ASP GLU ALA GLY ALA
SEQRES 22 B 286 GLN ALA VAL ALA ARG VAL PHE ALA ALA PHE PHE ALA ARG
SEQRES 1 C 286 MSE SER LEU GLN VAL GLU GLU VAL ARG ILE SER LEU PRO
SEQRES 2 C 286 HIS ILE GLU LEU ALA ALA HIS LEU PHE GLY PRO PRO ASP
SEQRES 3 C 286 GLY LYS PRO VAL ILE ALA LEU HIS GLY TRP LEU ASP ASN
SEQRES 4 C 286 ALA MSE SER PHE SER ARG LEU ALA PRO LYS LEU ALA GLY
SEQRES 5 C 286 LEU ARG ILE VAL ALA LEU ASP PHE ALA GLY HIS GLY HIS
SEQRES 6 C 286 SER ALA HIS ARG ALA GLU GLY ALA SER TYR LEU LEU TRP
SEQRES 7 C 286 ASP TYR ALA LEU ASP VAL LEU MSE VAL ALA GLU GLN LEU
SEQRES 8 C 286 GLY TRP GLU ARG PHE SER LEU LEU GLY HIS SER MSE GLY
SEQRES 9 C 286 ALA ILE VAL SER VAL LEU LEU ALA GLY ALA LEU PRO GLU
SEQRES 10 C 286 ARG ILE GLU ARG LEU ALA LEU ILE ASP GLY LEU ILE PRO
SEQRES 11 C 286 TYR THR GLY GLU ALA ASP LYS ALA PRO GLN LYS LEU GLY
SEQRES 12 C 286 GLU ALA LEU LYS ALA GLN LEU ALA LEU ARG HIS LYS ARG
SEQRES 13 C 286 LYS PRO VAL TYR ALA GLU LEU GLU LYS ALA VAL GLU ALA
SEQRES 14 C 286 ARG MSE ARG GLY VAL GLY GLU ILE SER ARG GLU ALA ALA
SEQRES 15 C 286 GLU LEU LEU ALA GLN ARG GLY LEU GLU PRO VAL PRO GLY
SEQRES 16 C 286 GLY TYR THR TRP ARG THR ASP ALA ARG LEU THR LEU PRO
SEQRES 17 C 286 SER PRO LEU ARG LEU THR GLN ALA HIS ALA LEU ASN PHE
SEQRES 18 C 286 VAL ARG SER VAL GLU CYS PRO VAL SER LEU VAL LEU ALA
SEQRES 19 C 286 GLU GLN GLY MSE LEU ALA VAL GLU PRO ARG MSE ARG ALA
SEQRES 20 C 286 LEU LEU GLU THR LEU PRO PHE GLU ARG HIS HIS LEU PRO
SEQRES 21 C 286 GLY GLY HIS HIS LEU HIS LEU ASP ASP GLU ALA GLY ALA
SEQRES 22 C 286 GLN ALA VAL ALA ARG VAL PHE ALA ALA PHE PHE ALA ARG
SEQRES 1 D 286 MSE SER LEU GLN VAL GLU GLU VAL ARG ILE SER LEU PRO
SEQRES 2 D 286 HIS ILE GLU LEU ALA ALA HIS LEU PHE GLY PRO PRO ASP
SEQRES 3 D 286 GLY LYS PRO VAL ILE ALA LEU HIS GLY TRP LEU ASP ASN
SEQRES 4 D 286 ALA MSE SER PHE SER ARG LEU ALA PRO LYS LEU ALA GLY
SEQRES 5 D 286 LEU ARG ILE VAL ALA LEU ASP PHE ALA GLY HIS GLY HIS
SEQRES 6 D 286 SER ALA HIS ARG ALA GLU GLY ALA SER TYR LEU LEU TRP
SEQRES 7 D 286 ASP TYR ALA LEU ASP VAL LEU MSE VAL ALA GLU GLN LEU
SEQRES 8 D 286 GLY TRP GLU ARG PHE SER LEU LEU GLY HIS SER MSE GLY
SEQRES 9 D 286 ALA ILE VAL SER VAL LEU LEU ALA GLY ALA LEU PRO GLU
SEQRES 10 D 286 ARG ILE GLU ARG LEU ALA LEU ILE ASP GLY LEU ILE PRO
SEQRES 11 D 286 TYR THR GLY GLU ALA ASP LYS ALA PRO GLN LYS LEU GLY
SEQRES 12 D 286 GLU ALA LEU LYS ALA GLN LEU ALA LEU ARG HIS LYS ARG
SEQRES 13 D 286 LYS PRO VAL TYR ALA GLU LEU GLU LYS ALA VAL GLU ALA
SEQRES 14 D 286 ARG MSE ARG GLY VAL GLY GLU ILE SER ARG GLU ALA ALA
SEQRES 15 D 286 GLU LEU LEU ALA GLN ARG GLY LEU GLU PRO VAL PRO GLY
SEQRES 16 D 286 GLY TYR THR TRP ARG THR ASP ALA ARG LEU THR LEU PRO
SEQRES 17 D 286 SER PRO LEU ARG LEU THR GLN ALA HIS ALA LEU ASN PHE
SEQRES 18 D 286 VAL ARG SER VAL GLU CYS PRO VAL SER LEU VAL LEU ALA
SEQRES 19 D 286 GLU GLN GLY MSE LEU ALA VAL GLU PRO ARG MSE ARG ALA
SEQRES 20 D 286 LEU LEU GLU THR LEU PRO PHE GLU ARG HIS HIS LEU PRO
SEQRES 21 D 286 GLY GLY HIS HIS LEU HIS LEU ASP ASP GLU ALA GLY ALA
SEQRES 22 D 286 GLN ALA VAL ALA ARG VAL PHE ALA ALA PHE PHE ALA ARG
MODRES 7AL5 MSE A 1 MET MODIFIED RESIDUE
MODRES 7AL5 MSE A 41 MET MODIFIED RESIDUE
MODRES 7AL5 MSE A 86 MET MODIFIED RESIDUE
MODRES 7AL5 MSE A 103 MET MODIFIED RESIDUE
MODRES 7AL5 MSE A 171 MET MODIFIED RESIDUE
MODRES 7AL5 MSE A 238 MET MODIFIED RESIDUE
MODRES 7AL5 MSE A 245 MET MODIFIED RESIDUE
MODRES 7AL5 MSE B 41 MET MODIFIED RESIDUE
MODRES 7AL5 MSE B 86 MET MODIFIED RESIDUE
MODRES 7AL5 MSE B 103 MET MODIFIED RESIDUE
MODRES 7AL5 MSE B 171 MET MODIFIED RESIDUE
MODRES 7AL5 MSE B 238 MET MODIFIED RESIDUE
MODRES 7AL5 MSE B 245 MET MODIFIED RESIDUE
MODRES 7AL5 MSE C 41 MET MODIFIED RESIDUE
MODRES 7AL5 MSE C 86 MET MODIFIED RESIDUE
MODRES 7AL5 MSE C 103 MET MODIFIED RESIDUE
MODRES 7AL5 MSE C 171 MET MODIFIED RESIDUE
MODRES 7AL5 MSE C 245 MET MODIFIED RESIDUE
MODRES 7AL5 MSE D 41 MET MODIFIED RESIDUE
MODRES 7AL5 MSE D 86 MET MODIFIED RESIDUE
MODRES 7AL5 MSE D 103 MET MODIFIED RESIDUE
MODRES 7AL5 MSE D 171 MET MODIFIED RESIDUE
MODRES 7AL5 MSE D 238 MET MODIFIED RESIDUE
MODRES 7AL5 MSE D 245 MET MODIFIED RESIDUE
HET MSE A 1 9
HET MSE A 41 29
HET MSE A 86 17
HET MSE A 103 17
HET MSE A 171 17
HET MSE A 238 17
HET MSE A 245 17
HET MSE B 41 17
HET MSE B 86 17
HET MSE B 103 17
HET MSE B 171 17
HET MSE B 238 17
HET MSE B 245 17
HET MSE C 41 17
HET MSE C 86 17
HET MSE C 103 17
HET MSE C 171 17
HET MSE C 238 17
HET MSE C 245 17
HET MSE D 41 17
HET MSE D 86 17
HET MSE D 103 17
HET MSE D 171 17
HET MSE D 238 17
HET MSE D 245 17
HET PEG A 301 17
HET PGE B 301 24
HET PEG C 301 17
HET EDO C 302 10
HET GOL D 301 14
HETNAM MSE SELENOMETHIONINE
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM EDO 1,2-ETHANEDIOL
HETNAM GOL GLYCEROL
HETSYN EDO ETHYLENE GLYCOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 MSE 25(C5 H11 N O2 SE)
FORMUL 5 PEG 2(C4 H10 O3)
FORMUL 6 PGE C6 H14 O4
FORMUL 8 EDO C2 H6 O2
FORMUL 9 GOL C3 H8 O3
FORMUL 10 HOH *567(H2 O)
HELIX 1 AA1 ASN A 39 SER A 44 5 6
HELIX 2 AA2 LEU A 46 LEU A 50 5 5
HELIX 3 AA3 LEU A 76 LEU A 91 1 16
HELIX 4 AA4 SER A 102 LEU A 115 1 14
HELIX 5 AA5 GLU A 134 ASP A 136 5 3
HELIX 6 AA6 LYS A 137 ALA A 151 1 15
HELIX 7 AA7 LEU A 152 LYS A 155 5 4
HELIX 8 AA8 GLU A 162 ARG A 172 1 11
HELIX 9 AA9 SER A 178 GLY A 189 1 12
HELIX 10 AB1 ASP A 202 LEU A 207 5 6
HELIX 11 AB2 THR A 214 SER A 224 1 11
HELIX 12 AB3 GLY A 237 GLU A 242 1 6
HELIX 13 AB4 ARG A 244 GLU A 250 1 7
HELIX 14 AB5 HIS A 264 ASP A 269 1 6
HELIX 15 AB6 ASP A 269 ARG A 286 1 18
HELIX 16 AB7 ASN B 39 SER B 44 5 6
HELIX 17 AB8 LEU B 46 LEU B 50 5 5
HELIX 18 AB9 LEU B 76 LEU B 91 1 16
HELIX 19 AC1 SER B 102 LEU B 115 1 14
HELIX 20 AC2 GLU B 134 ASP B 136 5 3
HELIX 21 AC3 LYS B 137 ARG B 153 1 17
HELIX 22 AC4 GLU B 162 ARG B 172 1 11
HELIX 23 AC5 SER B 178 GLY B 189 1 12
HELIX 24 AC6 ASP B 202 LEU B 207 5 6
HELIX 25 AC7 THR B 214 ARG B 223 1 10
HELIX 26 AC8 GLY B 237 GLU B 242 1 6
HELIX 27 AC9 GLU B 242 THR B 251 1 10
HELIX 28 AD1 HIS B 264 ASP B 269 1 6
HELIX 29 AD2 ASP B 269 ARG B 286 1 18
HELIX 30 AD3 ASN C 39 SER C 44 5 6
HELIX 31 AD4 ARG C 45 LEU C 50 1 6
HELIX 32 AD5 LEU C 76 LEU C 91 1 16
HELIX 33 AD6 SER C 102 LEU C 115 1 14
HELIX 34 AD7 LYS C 137 ALA C 151 1 15
HELIX 35 AD8 LEU C 152 LYS C 155 5 4
HELIX 36 AD9 GLU C 162 ARG C 172 1 11
HELIX 37 AE1 SER C 178 GLY C 189 1 12
HELIX 38 AE2 ASP C 202 LEU C 207 5 6
HELIX 39 AE3 THR C 214 ARG C 223 1 10
HELIX 40 AE4 MSE C 238 VAL C 241 5 4
HELIX 41 AE5 GLU C 242 GLU C 250 1 9
HELIX 42 AE6 HIS C 264 ASP C 269 1 6
HELIX 43 AE7 ASP C 269 ALA C 285 1 17
HELIX 44 AE8 ASN D 39 SER D 44 5 6
HELIX 45 AE9 LEU D 46 LEU D 50 5 5
HELIX 46 AF1 LEU D 76 LEU D 91 1 16
HELIX 47 AF2 SER D 102 LEU D 115 1 14
HELIX 48 AF3 GLU D 134 ASP D 136 5 3
HELIX 49 AF4 LYS D 137 ALA D 151 1 15
HELIX 50 AF5 LEU D 152 LYS D 155 5 4
HELIX 51 AF6 GLU D 162 ARG D 172 1 11
HELIX 52 AF7 SER D 178 GLY D 189 1 12
HELIX 53 AF8 ASP D 202 LEU D 207 5 6
HELIX 54 AF9 THR D 214 VAL D 225 1 12
HELIX 55 AG1 GLY D 237 GLU D 242 1 6
HELIX 56 AG2 PRO D 243 THR D 251 1 9
HELIX 57 AG3 HIS D 264 ASP D 269 1 6
HELIX 58 AG4 ASP D 269 ARG D 286 1 18
SHEET 1 AA1 8 GLU A 7 SER A 11 0
SHEET 2 AA1 8 GLU A 16 PHE A 22 -1 O LEU A 17 N ILE A 10
SHEET 3 AA1 8 LEU A 53 LEU A 58 -1 O ALA A 57 N HIS A 20
SHEET 4 AA1 8 LYS A 28 LEU A 33 1 N LYS A 28 O ARG A 54
SHEET 5 AA1 8 PHE A 96 HIS A 101 1 O LEU A 99 N LEU A 33
SHEET 6 AA1 8 ILE A 119 ILE A 125 1 O ILE A 125 N GLY A 100
SHEET 7 AA1 8 VAL A 229 ALA A 234 1 O SER A 230 N LEU A 124
SHEET 8 AA1 8 GLU A 255 LEU A 259 1 O GLU A 255 N LEU A 231
SHEET 1 AA2 2 LEU A 190 VAL A 193 0
SHEET 2 AA2 2 GLY A 196 TRP A 199 -1 O GLY A 196 N VAL A 193
SHEET 1 AA3 8 GLU B 7 SER B 11 0
SHEET 2 AA3 8 GLU B 16 PHE B 22 -1 O ALA B 19 N VAL B 8
SHEET 3 AA3 8 LEU B 53 LEU B 58 -1 O ALA B 57 N HIS B 20
SHEET 4 AA3 8 LYS B 28 LEU B 33 1 N VAL B 30 O VAL B 56
SHEET 5 AA3 8 PHE B 96 HIS B 101 1 O LEU B 99 N LEU B 33
SHEET 6 AA3 8 ILE B 119 ILE B 125 1 O ILE B 125 N GLY B 100
SHEET 7 AA3 8 VAL B 229 ALA B 234 1 O SER B 230 N LEU B 122
SHEET 8 AA3 8 GLU B 255 LEU B 259 1 O HIS B 257 N LEU B 233
SHEET 1 AA4 2 LEU B 190 VAL B 193 0
SHEET 2 AA4 2 GLY B 196 TRP B 199 -1 O GLY B 196 N VAL B 193
SHEET 1 AA5 8 GLU C 7 LEU C 12 0
SHEET 2 AA5 8 ILE C 15 PHE C 22 -1 O LEU C 17 N ILE C 10
SHEET 3 AA5 8 LEU C 53 LEU C 58 -1 O ALA C 57 N HIS C 20
SHEET 4 AA5 8 LYS C 28 LEU C 33 1 N VAL C 30 O VAL C 56
SHEET 5 AA5 8 PHE C 96 HIS C 101 1 O SER C 97 N PRO C 29
SHEET 6 AA5 8 ILE C 119 ILE C 125 1 O ILE C 125 N GLY C 100
SHEET 7 AA5 8 VAL C 229 ALA C 234 1 O VAL C 232 N LEU C 124
SHEET 8 AA5 8 GLU C 255 LEU C 259 1 O HIS C 257 N LEU C 233
SHEET 1 AA6 2 LEU C 190 PRO C 192 0
SHEET 2 AA6 2 TYR C 197 TRP C 199 -1 O THR C 198 N GLU C 191
SHEET 1 AA7 8 GLU D 7 LEU D 12 0
SHEET 2 AA7 8 ILE D 15 PHE D 22 -1 O LEU D 17 N ILE D 10
SHEET 3 AA7 8 LEU D 53 LEU D 58 -1 O ILE D 55 N PHE D 22
SHEET 4 AA7 8 LYS D 28 LEU D 33 1 N VAL D 30 O VAL D 56
SHEET 5 AA7 8 PHE D 96 HIS D 101 1 O SER D 97 N PRO D 29
SHEET 6 AA7 8 ILE D 119 ILE D 125 1 O ILE D 125 N GLY D 100
SHEET 7 AA7 8 VAL D 229 ALA D 234 1 O SER D 230 N LEU D 124
SHEET 8 AA7 8 GLU D 255 LEU D 259 1 O GLU D 255 N LEU D 231
SHEET 1 AA8 2 LEU D 190 PRO D 192 0
SHEET 2 AA8 2 TYR D 197 TRP D 199 -1 O THR D 198 N GLU D 191
LINK C MSE A 1 N SER A 2 1555 1555 1.33
LINK C ALA A 40 N MSE A 41 1555 1555 1.33
LINK C MSE A 41 N SER A 42 1555 1555 1.34
LINK C LEU A 85 N MSE A 86 1555 1555 1.31
LINK C MSE A 86 N VAL A 87 1555 1555 1.33
LINK C SER A 102 N MSE A 103 1555 1555 1.33
LINK C MSE A 103 N GLY A 104 1555 1555 1.33
LINK C ARG A 170 N MSE A 171 1555 1555 1.32
LINK C MSE A 171 N ARG A 172 1555 1555 1.32
LINK C GLY A 237 N MSE A 238 1555 1555 1.34
LINK C MSE A 238 N LEU A 239 1555 1555 1.33
LINK C ARG A 244 N MSE A 245 1555 1555 1.33
LINK C MSE A 245 N ARG A 246 1555 1555 1.33
LINK C ALA B 40 N MSE B 41 1555 1555 1.32
LINK C MSE B 41 N SER B 42 1555 1555 1.34
LINK C LEU B 85 N MSE B 86 1555 1555 1.32
LINK C MSE B 86 N VAL B 87 1555 1555 1.33
LINK C SER B 102 N MSE B 103 1555 1555 1.33
LINK C MSE B 103 N GLY B 104 1555 1555 1.34
LINK C ARG B 170 N MSE B 171 1555 1555 1.33
LINK C MSE B 171 N ARG B 172 1555 1555 1.32
LINK C GLY B 237 N MSE B 238 1555 1555 1.33
LINK C MSE B 238 N LEU B 239 1555 1555 1.32
LINK C ARG B 244 N MSE B 245 1555 1555 1.33
LINK C MSE B 245 N ARG B 246 1555 1555 1.35
LINK C ALA C 40 N MSE C 41 1555 1555 1.30
LINK C MSE C 41 N SER C 42 1555 1555 1.34
LINK C LEU C 85 N MSE C 86 1555 1555 1.32
LINK C MSE C 86 N VAL C 87 1555 1555 1.33
LINK C SER C 102 N MSE C 103 1555 1555 1.33
LINK C MSE C 103 N GLY C 104 1555 1555 1.34
LINK C ARG C 170 N MSE C 171 1555 1555 1.32
LINK C MSE C 171 N ARG C 172 1555 1555 1.32
LINK C GLY C 237 N MSE C 238 1555 1555 1.32
LINK C MSE C 238 N LEU C 239 1555 1555 1.33
LINK C ARG C 244 N MSE C 245 1555 1555 1.33
LINK C MSE C 245 N ARG C 246 1555 1555 1.34
LINK C ALA D 40 N MSE D 41 1555 1555 1.33
LINK C MSE D 41 N SER D 42 1555 1555 1.33
LINK C LEU D 85 N MSE D 86 1555 1555 1.32
LINK C MSE D 86 N VAL D 87 1555 1555 1.34
LINK C SER D 102 N MSE D 103 1555 1555 1.33
LINK C MSE D 103 N GLY D 104 1555 1555 1.33
LINK C ARG D 170 N MSE D 171 1555 1555 1.33
LINK C MSE D 171 N ARG D 172 1555 1555 1.32
LINK C GLY D 237 N MSE D 238 1555 1555 1.35
LINK C MSE D 238 N LEU D 239 1555 1555 1.33
LINK C ARG D 244 N MSE D 245 1555 1555 1.33
LINK C MSE D 245 N ARG D 246 1555 1555 1.32
CRYST1 136.308 136.308 148.211 90.00 90.00 120.00 P 61 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 0.007336 0.004236 0.000000 0.00000
SCALE2 0.000000 0.008471 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006747 0.00000
TER 4432 ARG A 286
TER 8825 ARG B 286
TER 13187 ARG C 286
TER 17542 ARG D 286
MASTER 340 0 30 58 40 0 0 6 9348 4 560 88
END |