| content |
HEADER HYDROLASE 06-MAY-16 5JRK
TITLE CRYSTAL STRUCTURE OF THE SPHINGOPYXIN I LASSO PEPTIDE ISOPEPTIDASE
TITLE 2 SPI-ISOP (SEMET-DERIVED)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL AMINOPEPTIDASES/ACYLAMINOACYL-PEPTIDASES-LIKE
COMPND 3 PROTEIN;
COMPND 4 CHAIN: A, B;
COMPND 5 SYNONYM: SPI-ISOP;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SPHINGOPYXIS ALASKENSIS RB2256;
SOURCE 3 ORGANISM_TAXID: 317655;
SOURCE 4 GENE: SALA_2532;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI B;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 37762;
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: B834(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET28A
KEYWDS LASSO PEPTIDE ISOPEPTIDASE, SERINE PROTEASE, BETA-PROPELLER,
KEYWDS 2 ALPHA/BETA-HYDROLASE, CATALYTIC TRIAD, OXYANION HOLE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.D.FAGE,J.D.HEGEMANN,G.BANGE,M.A.MARAHIEL
REVDAT 1 28-SEP-16 5JRK 0
JRNL AUTH C.D.FAGE,J.D.HEGEMANN,A.J.NEBEL,R.M.STEINBACH,S.ZHU,U.LINNE,
JRNL AUTH 2 K.HARMS,G.BANGEM,M.A.MARAHIEL
JRNL TITL CRYSTAL STRUCTURE AND CHARACTERIZATION OF SPI-ISOP, AN
JRNL TITL 2 ISOPEPTIDASE THAT HYDROLYZES THE LASSO PEPTIDE SPHINGOPYXIN
JRNL TITL 3 I
JRNL REF ANGEW.CHEM.INT.ED.ENGL. 2016
JRNL REFN ESSN 1521-3773
JRNL DOI 10.1002/ANIE.201605232
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.10_2152
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.08
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 51018
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.238
REMARK 3 R VALUE (WORKING SET) : 0.237
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.190
REMARK 3 FREE R VALUE TEST SET COUNT : 2647
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 49.0870 - 7.9944 1.00 2706 165 0.2153 0.2323
REMARK 3 2 7.9944 - 6.3497 1.00 2631 129 0.2242 0.2091
REMARK 3 3 6.3497 - 5.5483 1.00 2608 121 0.2235 0.2630
REMARK 3 4 5.5483 - 5.0416 1.00 2569 138 0.2128 0.2303
REMARK 3 5 5.0416 - 4.6805 1.00 2547 144 0.1898 0.1874
REMARK 3 6 4.6805 - 4.4048 1.00 2561 132 0.2007 0.1944
REMARK 3 7 4.4048 - 4.1843 1.00 2543 141 0.2062 0.2212
REMARK 3 8 4.1843 - 4.0022 1.00 2536 138 0.2152 0.2427
REMARK 3 9 4.0022 - 3.8482 1.00 2532 130 0.2322 0.3023
REMARK 3 10 3.8482 - 3.7155 1.00 2530 128 0.2508 0.3140
REMARK 3 11 3.7155 - 3.5993 1.00 2513 151 0.2777 0.2942
REMARK 3 12 3.5993 - 3.4965 1.00 2537 144 0.2707 0.2807
REMARK 3 13 3.4965 - 3.4045 1.00 2501 150 0.2861 0.3080
REMARK 3 14 3.4045 - 3.3214 1.00 2502 134 0.3008 0.3808
REMARK 3 15 3.3214 - 3.2459 1.00 2510 152 0.3221 0.3573
REMARK 3 16 3.2459 - 3.1769 1.00 2504 140 0.3373 0.3844
REMARK 3 17 3.1769 - 3.1133 1.00 2522 141 0.3424 0.3650
REMARK 3 18 3.1133 - 3.0546 1.00 2540 127 0.3671 0.4103
REMARK 3 19 3.0546 - 3.0000 1.00 2479 142 0.3847 0.4375
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.450
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.220
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 89.21
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 79.43
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.003 10918
REMARK 3 ANGLE : 0.543 14828
REMARK 3 CHIRALITY : 0.043 1619
REMARK 3 PLANARITY : 0.003 1954
REMARK 3 DIHEDRAL : 15.276 6553
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 5JRK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-MAY-16.
REMARK 100 THE DEPOSITION ID IS D_1000221066.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-DEC-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9790
REMARK 200 MONOCHROMATOR : SI (111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS OCT 15, 2015
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.17
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51096
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 49.080
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 13.30
REMARK 200 R MERGE (I) : 0.21900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.09
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 27.80
REMARK 200 R MERGE FOR SHELL (I) : 2.78000
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: SAD
REMARK 200 SOFTWARE USED: PHENIX 1.10-2152
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: POLYHEDRAL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BICINE, 10%(W/V) PEG 6000, PH
REMARK 280 9.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
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 55.55250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 84.53500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 66.75050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 84.53500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 55.55250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 66.75050
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4870 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 56110 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 MSE A -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MSE A 1
REMARK 465 LYS A 2
REMARK 465 ILE A 3
REMARK 465 ALA A 4
REMARK 465 LEU A 5
REMARK 465 ARG A 6
REMARK 465 SER A 7
REMARK 465 GLY A 8
REMARK 465 LEU A 9
REMARK 465 PRO A 10
REMARK 465 ALA A 11
REMARK 465 VAL A 12
REMARK 465 ALA A 13
REMARK 465 LEU A 14
REMARK 465 LEU A 15
REMARK 465 ALA A 16
REMARK 465 ALA A 17
REMARK 465 ALA A 18
REMARK 465 ALA A 19
REMARK 465 LEU A 20
REMARK 465 SER A 21
REMARK 465 PRO A 22
REMARK 465 ALA A 23
REMARK 465 ALA A 24
REMARK 465 GLN A 25
REMARK 465 ALA A 26
REMARK 465 GLY A 27
REMARK 465 GLU A 28
REMARK 465 SER A 29
REMARK 465 THR A 254
REMARK 465 LEU A 255
REMARK 465 SER A 727
REMARK 465 ALA A 728
REMARK 465 TRP A 729
REMARK 465 SER A 730
REMARK 465 HIS A 731
REMARK 465 PRO A 732
REMARK 465 GLN A 733
REMARK 465 PHE A 734
REMARK 465 GLU A 735
REMARK 465 LYS A 736
REMARK 465 MSE B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MSE B 1
REMARK 465 LYS B 2
REMARK 465 ILE B 3
REMARK 465 ALA B 4
REMARK 465 LEU B 5
REMARK 465 ARG B 6
REMARK 465 SER B 7
REMARK 465 GLY B 8
REMARK 465 LEU B 9
REMARK 465 PRO B 10
REMARK 465 ALA B 11
REMARK 465 VAL B 12
REMARK 465 ALA B 13
REMARK 465 LEU B 14
REMARK 465 LEU B 15
REMARK 465 ALA B 16
REMARK 465 ALA B 17
REMARK 465 ALA B 18
REMARK 465 ALA B 19
REMARK 465 LEU B 20
REMARK 465 SER B 21
REMARK 465 PRO B 22
REMARK 465 ALA B 23
REMARK 465 ALA B 24
REMARK 465 GLN B 25
REMARK 465 ALA B 26
REMARK 465 GLY B 27
REMARK 465 GLU B 28
REMARK 465 THR B 250
REMARK 465 SER B 251
REMARK 465 ASP B 252
REMARK 465 GLY B 253
REMARK 465 THR B 254
REMARK 465 LEU B 255
REMARK 465 GLY B 256
REMARK 465 GLY B 257
REMARK 465 ALA B 258
REMARK 465 PHE B 259
REMARK 465 GLU B 260
REMARK 465 GLN B 277
REMARK 465 ARG B 278
REMARK 465 ASP B 279
REMARK 465 LEU B 280
REMARK 465 LEU B 281
REMARK 465 SER B 282
REMARK 465 MSE B 283
REMARK 465 ALA B 724
REMARK 465 ALA B 725
REMARK 465 PRO B 726
REMARK 465 SER B 727
REMARK 465 ALA B 728
REMARK 465 TRP B 729
REMARK 465 SER B 730
REMARK 465 HIS B 731
REMARK 465 PRO B 732
REMARK 465 GLN B 733
REMARK 465 PHE B 734
REMARK 465 GLU B 735
REMARK 465 LYS B 736
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 SER B 284 CB OG
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 NZ LYS A 710 OD2 ASP B 188 1.81
REMARK 500 NH1 ARG A 446 OE2 GLU A 485 1.93
REMARK 500 NH1 ARG A 32 OD2 ASP A 38 2.08
REMARK 500 OE2 GLU B 243 NH1 ARG B 272 2.08
REMARK 500 NH1 ARG A 428 OE2 GLU A 545 2.09
REMARK 500 NH2 ARG B 433 OD2 ASP B 537 2.13
REMARK 500 O ASP A 624 NH1 ARG A 721 2.14
REMARK 500 OG1 THR B 670 O VAL B 672 2.15
REMARK 500 NH2 ARG B 32 OD2 ASP B 38 2.17
REMARK 500 O LEU A 280 OG SER A 284 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PRO A 33 -175.82 -69.52
REMARK 500 LEU A 88 -66.61 -101.23
REMARK 500 LEU A 130 -62.63 -107.60
REMARK 500 LEU A 148 -73.03 -82.59
REMARK 500 ALA A 258 174.36 177.93
REMARK 500 VAL A 267 -69.83 -98.62
REMARK 500 THR A 373 -64.45 -97.16
REMARK 500 ASP A 466 -169.89 -160.37
REMARK 500 ASN A 474 -62.87 -106.77
REMARK 500 TRP A 476 -123.40 52.72
REMARK 500 TRP A 528 -63.24 -127.40
REMARK 500 SER A 559 -114.57 55.70
REMARK 500 LEU A 586 -6.17 79.81
REMARK 500 ALA A 628 175.46 173.97
REMARK 500 LEU B 130 -72.37 -108.37
REMARK 500 LYS B 169 -64.79 -99.05
REMARK 500 ASP B 188 -72.01 -43.69
REMARK 500 ILE B 220 -70.01 -99.18
REMARK 500 THR B 231 -71.64 -103.80
REMARK 500 THR B 373 -64.39 -92.76
REMARK 500 ILE B 413 -62.66 -105.67
REMARK 500 ALA B 451 -5.84 66.89
REMARK 500 ASN B 474 -63.04 -106.58
REMARK 500 TRP B 476 -123.21 52.46
REMARK 500 PRO B 479 76.07 -68.16
REMARK 500 TRP B 528 -63.60 -121.32
REMARK 500 SER B 559 -116.93 56.48
REMARK 500 LEU B 586 -5.31 79.07
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BGC A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BGC B 801
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5JQF RELATED DB: PDB
REMARK 900 5JQF (SPHINGOPYXIN I) IS THE SUBSTRATE FOR SPI-ISOP
REMARK 900 RELATED ID: 5JRL RELATED DB: PDB
REMARK 900 5JRL IS THE NATIVE FORM OF THIS PROTEIN
DBREF 5JRK A 1 726 UNP Q1GQ33 Q1GQ33_SPHAL 1 726
DBREF 5JRK B 1 726 UNP Q1GQ33 Q1GQ33_SPHAL 1 726
SEQADV 5JRK MSE A -19 UNP Q1GQ33 INITIATING METHIONINE
SEQADV 5JRK GLY A -18 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK SER A -17 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK SER A -16 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK HIS A -15 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK HIS A -14 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK HIS A -13 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK HIS A -12 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK HIS A -11 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK HIS A -10 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK SER A -9 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK SER A -8 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK GLY A -7 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK LEU A -6 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK VAL A -5 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK PRO A -4 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK ARG A -3 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK GLY A -2 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK SER A -1 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK HIS A 0 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK SER A 727 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK ALA A 728 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK TRP A 729 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK SER A 730 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK HIS A 731 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK PRO A 732 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK GLN A 733 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK PHE A 734 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK GLU A 735 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK LYS A 736 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK MSE B -19 UNP Q1GQ33 INITIATING METHIONINE
SEQADV 5JRK GLY B -18 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK SER B -17 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK SER B -16 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK HIS B -15 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK HIS B -14 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK HIS B -13 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK HIS B -12 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK HIS B -11 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK HIS B -10 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK SER B -9 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK SER B -8 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK GLY B -7 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK LEU B -6 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK VAL B -5 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK PRO B -4 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK ARG B -3 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK GLY B -2 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK SER B -1 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK HIS B 0 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK SER B 727 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK ALA B 728 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK TRP B 729 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK SER B 730 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK HIS B 731 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK PRO B 732 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK GLN B 733 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK PHE B 734 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK GLU B 735 UNP Q1GQ33 EXPRESSION TAG
SEQADV 5JRK LYS B 736 UNP Q1GQ33 EXPRESSION TAG
SEQRES 1 A 756 MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 756 LEU VAL PRO ARG GLY SER HIS MSE LYS ILE ALA LEU ARG
SEQRES 3 A 756 SER GLY LEU PRO ALA VAL ALA LEU LEU ALA ALA ALA ALA
SEQRES 4 A 756 LEU SER PRO ALA ALA GLN ALA GLY GLU SER LYS GLY ARG
SEQRES 5 A 756 PRO TRP THR LEU GLU ASP ILE LEU THR VAL PRO GLU VAL
SEQRES 6 A 756 ASN GLU ILE ALA LEU SER ASP ASN GLY ARG LEU ALA ILE
SEQRES 7 A 756 TYR ALA ALA GLU ILE ALA ASP LEU ASP ALA GLY LYS PRO
SEQRES 8 A 756 ARG SER HIS ILE ARG ILE VAL ASP VAL GLU THR GLY ARG
SEQRES 9 A 756 THR LYS GLU LEU LEU THR VAL ASP THR ILE LYS SER LEU
SEQRES 10 A 756 ARG SER VAL PRO GLY THR GLN ASP TRP SER ALA LEU VAL
SEQRES 11 A 756 ASP LEU GLY GLU GLY GLN GLN LEU TYR ARG ILE ASP THR
SEQRES 12 A 756 GLU GLY LYS LEU LEU PRO LEU ILE VAL ASN PRO ASN PRO
SEQRES 13 A 756 VAL PRO VAL GLY LYS ALA ASP MSE SER PHE PRO LEU GLY
SEQRES 14 A 756 GLY GLY ILE ARG PRO SER HIS ILE GLY ILE LEU ASP TYR
SEQRES 15 A 756 ASP TRP SER PRO ASP GLY LYS TRP LEU TRP TYR SER GLN
SEQRES 16 A 756 LEU ARG ALA LYS SER ASP GLY PRO ARG VAL ARG PHE ASP
SEQRES 17 A 756 GLU GLU VAL THR ALA LEU LEU GLY ARG ARG ARG SER THR
SEQRES 18 A 756 ILE ASP VAL GLU VAL ASP PHE PHE LEU ARG ASN PRO GLU
SEQRES 19 A 756 GLY ASP THR THR ARG ILE MSE ALA ARG PRO SER THR ASP
SEQRES 20 A 756 ARG VAL ALA THR ARG GLY GLY GLY ARG VAL LEU TRP ARG
SEQRES 21 A 756 GLY ASN GLU VAL GLN PHE ARG ILE GLU THR SER ASP GLY
SEQRES 22 A 756 THR LEU GLY GLY ALA PHE GLU PHE VAL ALA TRP ASN ARG
SEQRES 23 A 756 VAL ASN ARG THR VAL ARG THR LEU ALA LYS GLN ARG ASP
SEQRES 24 A 756 LEU LEU SER MSE SER ILE LEU VAL GLY PRO ARG GLY GLY
SEQRES 25 A 756 GLN LEU SER THR SER GLY LEU GLY SER ASP ARG GLU LEU
SEQRES 26 A 756 ILE GLU THR SER ALA GLU GLY ARG PRO HIS SER TYR GLY
SEQRES 27 A 756 ARG VAL ALA PHE ASP ILE GLY ASP SER ARG SER ALA GLY
SEQRES 28 A 756 TRP LYS ARG SER ARG ASP GLY LYS ARG VAL VAL ILE GLY
SEQRES 29 A 756 THR ARG GLY LEU GLY ASP ALA ARG TYR GLY LEU ALA LEU
SEQRES 30 A 756 ILE ASP LYS THR GLY VAL ARG GLU LEU ARG ALA ASP ALA
SEQRES 31 A 756 SER LEU THR ARG CYS GLY PHE ASP GLY MSE LEU ARG SER
SEQRES 32 A 756 ALA ILE CYS VAL GLU GLU GLY MSE SER ARG PRO PRO ARG
SEQRES 33 A 756 LEU VAL ARG VAL ASP LEU GLY THR ASP LYS ILE THR ASP
SEQRES 34 A 756 LEU GLY PRO ILE SER PRO ARG HIS GLU GLU ILE GLU PRO
SEQRES 35 A 756 LEU GLN THR ILE ALA ARG THR PHE VAL SER ARG ASP GLY
SEQRES 36 A 756 TYR TRP SER SER GLY TYR VAL LEU LEU PRO ARG GLY HIS
SEQRES 37 A 756 ARG ALA ALA ASP ARG HIS PRO ALA VAL VAL VAL THR HIS
SEQRES 38 A 756 GLY THR ASP ALA ASP ASP ARG PHE ALA GLU PRO ALA ASN
SEQRES 39 A 756 GLN TRP ASN TYR PRO VAL GLN LEU LEU ALA GLU ARG GLY
SEQRES 40 A 756 TYR VAL VAL LEU LEU LEU ASN ASP PRO SER PRO GLY GLN
SEQRES 41 A 756 SER LYS ASP LEU MSE ASP ALA MSE HIS ALA TRP LEU ARG
SEQRES 42 A 756 GLY LYS GLY PRO PRO ASP PRO GLU THR VAL GLN GLN LYS
SEQRES 43 A 756 LEU TRP LEU THR GLY VAL HIS SER PHE GLU ASP ALA VAL
SEQRES 44 A 756 THR GLU LEU ALA ALA GLU GLY LEU ILE ASP PRO ALA ARG
SEQRES 45 A 756 VAL GLY ILE ALA GLY TYR SER ARG GLY SER GLN MSE VAL
SEQRES 46 A 756 ASN VAL THR VAL THR ASN SER LYS MSE PHE ARG ALA ALA
SEQRES 47 A 756 SER SER GLY ASP GLY GLY PHE LEU GLU PRO ALA GLY TYR
SEQRES 48 A 756 ALA THR GLY ARG SER SER TYR ASP ALA VAL TYR GLY GLY
SEQRES 49 A 756 ALA PRO LEU SER ASP ASN ILE GLU ARG TRP ARG ARG PHE
SEQRES 50 A 756 ALA PRO SER LEU ASN ALA ASP LYS VAL CYS ALA ALA VAL
SEQRES 51 A 756 LEU GLN GLN VAL ALA SER ALA SER PRO SER GLN ILE GLU
SEQRES 52 A 756 LEU PHE GLU ALA LEU ARG ALA ALA GLY VAL ALA THR GLN
SEQRES 53 A 756 ILE SER TYR TYR PRO GLY ALA THR ALA ALA SER ASP GLU
SEQRES 54 A 756 THR HIS VAL PHE TYR LEU THR THR ASN ARG LEU ARG ALA
SEQRES 55 A 756 MSE ARG GLU ASN ILE ALA TRP PHE ASP TYR TRP LEU LEU
SEQRES 56 A 756 ASP LYS ARG ASP ALA ASP ALA PRO PHE PRO ASP HIS VAL
SEQRES 57 A 756 VAL LYS TRP ASP ARG LEU LYS LYS ASN LEU PRO ASP ARG
SEQRES 58 A 756 CYS ALA ALA ALA PRO SER ALA TRP SER HIS PRO GLN PHE
SEQRES 59 A 756 GLU LYS
SEQRES 1 B 756 MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 756 LEU VAL PRO ARG GLY SER HIS MSE LYS ILE ALA LEU ARG
SEQRES 3 B 756 SER GLY LEU PRO ALA VAL ALA LEU LEU ALA ALA ALA ALA
SEQRES 4 B 756 LEU SER PRO ALA ALA GLN ALA GLY GLU SER LYS GLY ARG
SEQRES 5 B 756 PRO TRP THR LEU GLU ASP ILE LEU THR VAL PRO GLU VAL
SEQRES 6 B 756 ASN GLU ILE ALA LEU SER ASP ASN GLY ARG LEU ALA ILE
SEQRES 7 B 756 TYR ALA ALA GLU ILE ALA ASP LEU ASP ALA GLY LYS PRO
SEQRES 8 B 756 ARG SER HIS ILE ARG ILE VAL ASP VAL GLU THR GLY ARG
SEQRES 9 B 756 THR LYS GLU LEU LEU THR VAL ASP THR ILE LYS SER LEU
SEQRES 10 B 756 ARG SER VAL PRO GLY THR GLN ASP TRP SER ALA LEU VAL
SEQRES 11 B 756 ASP LEU GLY GLU GLY GLN GLN LEU TYR ARG ILE ASP THR
SEQRES 12 B 756 GLU GLY LYS LEU LEU PRO LEU ILE VAL ASN PRO ASN PRO
SEQRES 13 B 756 VAL PRO VAL GLY LYS ALA ASP MSE SER PHE PRO LEU GLY
SEQRES 14 B 756 GLY GLY ILE ARG PRO SER HIS ILE GLY ILE LEU ASP TYR
SEQRES 15 B 756 ASP TRP SER PRO ASP GLY LYS TRP LEU TRP TYR SER GLN
SEQRES 16 B 756 LEU ARG ALA LYS SER ASP GLY PRO ARG VAL ARG PHE ASP
SEQRES 17 B 756 GLU GLU VAL THR ALA LEU LEU GLY ARG ARG ARG SER THR
SEQRES 18 B 756 ILE ASP VAL GLU VAL ASP PHE PHE LEU ARG ASN PRO GLU
SEQRES 19 B 756 GLY ASP THR THR ARG ILE MSE ALA ARG PRO SER THR ASP
SEQRES 20 B 756 ARG VAL ALA THR ARG GLY GLY GLY ARG VAL LEU TRP ARG
SEQRES 21 B 756 GLY ASN GLU VAL GLN PHE ARG ILE GLU THR SER ASP GLY
SEQRES 22 B 756 THR LEU GLY GLY ALA PHE GLU PHE VAL ALA TRP ASN ARG
SEQRES 23 B 756 VAL ASN ARG THR VAL ARG THR LEU ALA LYS GLN ARG ASP
SEQRES 24 B 756 LEU LEU SER MSE SER ILE LEU VAL GLY PRO ARG GLY GLY
SEQRES 25 B 756 GLN LEU SER THR SER GLY LEU GLY SER ASP ARG GLU LEU
SEQRES 26 B 756 ILE GLU THR SER ALA GLU GLY ARG PRO HIS SER TYR GLY
SEQRES 27 B 756 ARG VAL ALA PHE ASP ILE GLY ASP SER ARG SER ALA GLY
SEQRES 28 B 756 TRP LYS ARG SER ARG ASP GLY LYS ARG VAL VAL ILE GLY
SEQRES 29 B 756 THR ARG GLY LEU GLY ASP ALA ARG TYR GLY LEU ALA LEU
SEQRES 30 B 756 ILE ASP LYS THR GLY VAL ARG GLU LEU ARG ALA ASP ALA
SEQRES 31 B 756 SER LEU THR ARG CYS GLY PHE ASP GLY MSE LEU ARG SER
SEQRES 32 B 756 ALA ILE CYS VAL GLU GLU GLY MSE SER ARG PRO PRO ARG
SEQRES 33 B 756 LEU VAL ARG VAL ASP LEU GLY THR ASP LYS ILE THR ASP
SEQRES 34 B 756 LEU GLY PRO ILE SER PRO ARG HIS GLU GLU ILE GLU PRO
SEQRES 35 B 756 LEU GLN THR ILE ALA ARG THR PHE VAL SER ARG ASP GLY
SEQRES 36 B 756 TYR TRP SER SER GLY TYR VAL LEU LEU PRO ARG GLY HIS
SEQRES 37 B 756 ARG ALA ALA ASP ARG HIS PRO ALA VAL VAL VAL THR HIS
SEQRES 38 B 756 GLY THR ASP ALA ASP ASP ARG PHE ALA GLU PRO ALA ASN
SEQRES 39 B 756 GLN TRP ASN TYR PRO VAL GLN LEU LEU ALA GLU ARG GLY
SEQRES 40 B 756 TYR VAL VAL LEU LEU LEU ASN ASP PRO SER PRO GLY GLN
SEQRES 41 B 756 SER LYS ASP LEU MSE ASP ALA MSE HIS ALA TRP LEU ARG
SEQRES 42 B 756 GLY LYS GLY PRO PRO ASP PRO GLU THR VAL GLN GLN LYS
SEQRES 43 B 756 LEU TRP LEU THR GLY VAL HIS SER PHE GLU ASP ALA VAL
SEQRES 44 B 756 THR GLU LEU ALA ALA GLU GLY LEU ILE ASP PRO ALA ARG
SEQRES 45 B 756 VAL GLY ILE ALA GLY TYR SER ARG GLY SER GLN MSE VAL
SEQRES 46 B 756 ASN VAL THR VAL THR ASN SER LYS MSE PHE ARG ALA ALA
SEQRES 47 B 756 SER SER GLY ASP GLY GLY PHE LEU GLU PRO ALA GLY TYR
SEQRES 48 B 756 ALA THR GLY ARG SER SER TYR ASP ALA VAL TYR GLY GLY
SEQRES 49 B 756 ALA PRO LEU SER ASP ASN ILE GLU ARG TRP ARG ARG PHE
SEQRES 50 B 756 ALA PRO SER LEU ASN ALA ASP LYS VAL CYS ALA ALA VAL
SEQRES 51 B 756 LEU GLN GLN VAL ALA SER ALA SER PRO SER GLN ILE GLU
SEQRES 52 B 756 LEU PHE GLU ALA LEU ARG ALA ALA GLY VAL ALA THR GLN
SEQRES 53 B 756 ILE SER TYR TYR PRO GLY ALA THR ALA ALA SER ASP GLU
SEQRES 54 B 756 THR HIS VAL PHE TYR LEU THR THR ASN ARG LEU ARG ALA
SEQRES 55 B 756 MSE ARG GLU ASN ILE ALA TRP PHE ASP TYR TRP LEU LEU
SEQRES 56 B 756 ASP LYS ARG ASP ALA ASP ALA PRO PHE PRO ASP HIS VAL
SEQRES 57 B 756 VAL LYS TRP ASP ARG LEU LYS LYS ASN LEU PRO ASP ARG
SEQRES 58 B 756 CYS ALA ALA ALA PRO SER ALA TRP SER HIS PRO GLN PHE
SEQRES 59 B 756 GLU LYS
MODRES 5JRK MSE A 144 MET MODIFIED RESIDUE
MODRES 5JRK MSE A 221 MET MODIFIED RESIDUE
MODRES 5JRK MSE A 283 MET MODIFIED RESIDUE
MODRES 5JRK MSE A 380 MET MODIFIED RESIDUE
MODRES 5JRK MSE A 391 MET MODIFIED RESIDUE
MODRES 5JRK MSE A 505 MET MODIFIED RESIDUE
MODRES 5JRK MSE A 508 MET MODIFIED RESIDUE
MODRES 5JRK MSE A 564 MET MODIFIED RESIDUE
MODRES 5JRK MSE A 574 MET MODIFIED RESIDUE
MODRES 5JRK MSE A 683 MET MODIFIED RESIDUE
MODRES 5JRK MSE B 144 MET MODIFIED RESIDUE
MODRES 5JRK MSE B 221 MET MODIFIED RESIDUE
MODRES 5JRK MSE B 380 MET MODIFIED RESIDUE
MODRES 5JRK MSE B 391 MET MODIFIED RESIDUE
MODRES 5JRK MSE B 505 MET MODIFIED RESIDUE
MODRES 5JRK MSE B 508 MET MODIFIED RESIDUE
MODRES 5JRK MSE B 564 MET MODIFIED RESIDUE
MODRES 5JRK MSE B 574 MET MODIFIED RESIDUE
MODRES 5JRK MSE B 683 MET MODIFIED RESIDUE
HET MSE A 144 8
HET MSE A 221 8
HET MSE A 283 8
HET MSE A 380 8
HET MSE A 391 8
HET MSE A 505 8
HET MSE A 508 8
HET MSE A 564 8
HET MSE A 574 8
HET MSE A 683 8
HET MSE B 144 8
HET MSE B 221 8
HET MSE B 380 8
HET MSE B 391 8
HET MSE B 505 8
HET MSE B 508 8
HET MSE B 564 8
HET MSE B 574 8
HET MSE B 683 8
HET BGC A 801 12
HET BGC B 801 12
HETNAM MSE SELENOMETHIONINE
HETNAM BGC BETA-D-GLUCOSE
FORMUL 1 MSE 19(C5 H11 N O2 SE)
FORMUL 3 BGC 2(C6 H12 O6)
HELIX 1 AA1 THR A 35 THR A 41 1 7
HELIX 2 AA2 PHE A 187 ALA A 193 1 7
HELIX 3 AA3 ASP A 227 GLY A 233 1 7
HELIX 4 AA4 SER A 414 GLU A 419 1 6
HELIX 5 AA5 GLU A 471 TRP A 476 1 6
HELIX 6 AA6 PRO A 479 ARG A 486 1 8
HELIX 7 AA7 SER A 497 GLN A 500 5 4
HELIX 8 AA8 SER A 501 GLY A 514 1 14
HELIX 9 AA9 ASP A 519 TRP A 528 1 10
HELIX 10 AB1 TRP A 528 GLU A 545 1 18
HELIX 11 AB2 SER A 559 SER A 572 1 14
HELIX 12 AB3 GLU A 587 ALA A 589 5 3
HELIX 13 AB4 GLY A 590 GLY A 603 1 14
HELIX 14 AB5 ASN A 610 ALA A 618 1 9
HELIX 15 AB6 ASN A 622 VAL A 626 5 5
HELIX 16 AB7 SER A 638 ALA A 651 1 14
HELIX 17 AB8 LEU A 675 LEU A 694 1 20
HELIX 18 AB9 ASP A 706 ASN A 717 1 12
HELIX 19 AC1 PRO A 719 ALA A 723 5 5
HELIX 20 AC2 THR B 35 THR B 41 1 7
HELIX 21 AC3 PHE B 187 THR B 192 1 6
HELIX 22 AC4 ALA B 193 LEU B 195 5 3
HELIX 23 AC5 SER B 414 ILE B 420 1 7
HELIX 24 AC6 GLU B 471 TRP B 476 1 6
HELIX 25 AC7 PRO B 479 ARG B 486 1 8
HELIX 26 AC8 SER B 497 GLN B 500 5 4
HELIX 27 AC9 SER B 501 GLY B 514 1 14
HELIX 28 AD1 ASP B 519 TRP B 528 1 10
HELIX 29 AD2 TRP B 528 GLU B 545 1 18
HELIX 30 AD3 SER B 559 SER B 572 1 14
HELIX 31 AD4 GLU B 587 ALA B 589 5 3
HELIX 32 AD5 GLY B 590 GLY B 603 1 14
HELIX 33 AD6 ASN B 610 ALA B 618 1 9
HELIX 34 AD7 ASN B 622 VAL B 626 5 5
HELIX 35 AD8 SER B 638 ALA B 651 1 14
HELIX 36 AD9 LEU B 675 LEU B 694 1 20
HELIX 37 AE1 PRO B 705 ASN B 717 1 13
SHEET 1 AA1 4 GLU A 44 LEU A 50 0
SHEET 2 AA1 4 LEU A 56 ALA A 64 -1 O GLU A 62 N GLU A 44
SHEET 3 AA1 4 PRO A 71 ASP A 79 -1 O ARG A 72 N ILE A 63
SHEET 4 AA1 4 THR A 85 VAL A 91 -1 O LYS A 86 N ILE A 77
SHEET 1 AA2 4 THR A 93 SER A 99 0
SHEET 2 AA2 4 TRP A 106 ASP A 111 -1 O LEU A 109 N LYS A 95
SHEET 3 AA2 4 GLN A 116 ILE A 121 -1 O ILE A 121 N TRP A 106
SHEET 4 AA2 4 LEU A 127 ILE A 131 -1 O LEU A 128 N ARG A 120
SHEET 1 AA3 2 VAL A 137 VAL A 139 0
SHEET 2 AA3 2 SER A 155 ILE A 157 -1 O SER A 155 N VAL A 139
SHEET 1 AA4 4 ASP A 161 TRP A 164 0
SHEET 2 AA4 4 LEU A 171 ALA A 178 -1 O TRP A 172 N ASP A 163
SHEET 3 AA4 4 VAL A 204 ARG A 211 -1 O PHE A 209 N TYR A 173
SHEET 4 AA4 4 THR A 217 ARG A 223 -1 O ILE A 220 N PHE A 208
SHEET 1 AA5 4 VAL A 237 ARG A 240 0
SHEET 2 AA5 4 GLU A 243 ILE A 248 -1 O GLN A 245 N LEU A 238
SHEET 3 AA5 4 PHE A 259 ASN A 265 -1 O TRP A 264 N VAL A 244
SHEET 4 AA5 4 VAL A 271 LYS A 276 -1 O LEU A 274 N PHE A 261
SHEET 1 AA6 3 GLN A 293 SER A 297 0
SHEET 2 AA6 3 ARG A 303 THR A 308 -1 O THR A 308 N GLN A 293
SHEET 3 AA6 3 PRO A 314 VAL A 320 -1 O HIS A 315 N GLU A 307
SHEET 1 AA7 3 PHE A 322 ILE A 324 0
SHEET 2 AA7 3 VAL A 341 GLY A 347 -1 O ARG A 346 N ASP A 323
SHEET 3 AA7 3 TRP A 332 ARG A 334 -1 N LYS A 333 O VAL A 342
SHEET 1 AA8 4 PHE A 322 ILE A 324 0
SHEET 2 AA8 4 VAL A 341 GLY A 347 -1 O ARG A 346 N ASP A 323
SHEET 3 AA8 4 TYR A 353 ILE A 358 -1 O GLY A 354 N THR A 345
SHEET 4 AA8 4 VAL A 363 GLU A 365 -1 O ARG A 364 N LEU A 357
SHEET 1 AA9 4 SER A 371 PHE A 377 0
SHEET 2 AA9 4 SER A 383 GLU A 389 -1 O GLU A 389 N SER A 371
SHEET 3 AA9 4 ARG A 396 ASP A 401 -1 O VAL A 400 N ALA A 384
SHEET 4 AA9 4 LYS A 406 PRO A 412 -1 O LYS A 406 N ASP A 401
SHEET 1 AB1 8 GLN A 424 ALA A 427 0
SHEET 2 AB1 8 GLY A 440 LEU A 444 -1 O VAL A 442 N ILE A 426
SHEET 3 AB1 8 VAL A 489 LEU A 493 -1 O VAL A 490 N LEU A 443
SHEET 4 AB1 8 HIS A 454 VAL A 459 1 N VAL A 457 O LEU A 491
SHEET 5 AB1 8 ILE A 548 TYR A 558 1 O GLY A 554 N VAL A 458
SHEET 6 AB1 8 ALA A 577 GLY A 581 1 O GLY A 581 N GLY A 557
SHEET 7 AB1 8 ALA A 629 VAL A 634 1 O ALA A 629 N ALA A 578
SHEET 8 AB1 8 ALA A 654 TYR A 659 1 O SER A 658 N VAL A 634
SHEET 1 AB2 2 PHE A 430 VAL A 431 0
SHEET 2 AB2 2 TRP A 437 SER A 438 -1 O SER A 438 N PHE A 430
SHEET 1 AB3 4 GLU B 44 LEU B 50 0
SHEET 2 AB3 4 LEU B 56 ALA B 64 -1 O ILE B 58 N ALA B 49
SHEET 3 AB3 4 PRO B 71 ASP B 79 -1 O VAL B 78 N ALA B 57
SHEET 4 AB3 4 THR B 85 VAL B 91 -1 O VAL B 91 N SER B 73
SHEET 1 AB4 4 THR B 93 SER B 99 0
SHEET 2 AB4 4 TRP B 106 ASP B 111 -1 O LEU B 109 N LYS B 95
SHEET 3 AB4 4 GLN B 116 ILE B 121 -1 O ILE B 121 N TRP B 106
SHEET 4 AB4 4 LEU B 127 ILE B 131 -1 O LEU B 128 N ARG B 120
SHEET 1 AB5 2 VAL B 137 VAL B 139 0
SHEET 2 AB5 2 SER B 155 ILE B 157 -1 O SER B 155 N VAL B 139
SHEET 1 AB6 4 ILE B 159 TRP B 164 0
SHEET 2 AB6 4 LEU B 171 ALA B 178 -1 O SER B 174 N ASP B 161
SHEET 3 AB6 4 VAL B 204 ARG B 211 -1 O ARG B 211 N LEU B 171
SHEET 4 AB6 4 THR B 217 ARG B 223 -1 O ILE B 220 N PHE B 208
SHEET 1 AB7 4 VAL B 237 ARG B 240 0
SHEET 2 AB7 4 GLU B 243 PHE B 246 -1 O GLN B 245 N LEU B 238
SHEET 3 AB7 4 VAL B 262 ASN B 265 -1 O TRP B 264 N VAL B 244
SHEET 4 AB7 4 THR B 270 ARG B 272 -1 O ARG B 272 N ALA B 263
SHEET 1 AB8 3 GLN B 293 SER B 297 0
SHEET 2 AB8 3 ARG B 303 THR B 308 -1 O ILE B 306 N SER B 295
SHEET 3 AB8 3 PRO B 314 VAL B 320 -1 O VAL B 320 N ARG B 303
SHEET 1 AB9 3 PHE B 322 ASP B 323 0
SHEET 2 AB9 3 ARG B 340 GLY B 347 -1 O ARG B 346 N ASP B 323
SHEET 3 AB9 3 TRP B 332 ARG B 334 -1 N LYS B 333 O VAL B 342
SHEET 1 AC1 4 PHE B 322 ASP B 323 0
SHEET 2 AC1 4 ARG B 340 GLY B 347 -1 O ARG B 346 N ASP B 323
SHEET 3 AC1 4 TYR B 353 ASP B 359 -1 O ILE B 358 N VAL B 341
SHEET 4 AC1 4 VAL B 363 GLU B 365 -1 O ARG B 364 N LEU B 357
SHEET 1 AC2 4 SER B 371 PHE B 377 0
SHEET 2 AC2 4 SER B 383 GLU B 389 -1 O ILE B 385 N GLY B 376
SHEET 3 AC2 4 ARG B 396 ASP B 401 -1 O VAL B 400 N ALA B 384
SHEET 4 AC2 4 LYS B 406 PRO B 412 -1 O LEU B 410 N LEU B 397
SHEET 1 AC3 8 THR B 425 VAL B 431 0
SHEET 2 AC3 8 TRP B 437 LEU B 443 -1 O VAL B 442 N ILE B 426
SHEET 3 AC3 8 VAL B 489 LEU B 493 -1 O VAL B 490 N LEU B 443
SHEET 4 AC3 8 HIS B 454 VAL B 459 1 N VAL B 457 O LEU B 491
SHEET 5 AC3 8 ILE B 548 TYR B 558 1 O ALA B 556 N VAL B 458
SHEET 6 AC3 8 ALA B 577 GLY B 581 1 O GLY B 581 N GLY B 557
SHEET 7 AC3 8 ALA B 629 VAL B 634 1 O ALA B 629 N ALA B 578
SHEET 8 AC3 8 THR B 655 TYR B 659 1 O SER B 658 N GLN B 632
SSBOND 1 CYS A 375 CYS A 386 1555 1555 2.03
SSBOND 2 CYS A 627 CYS A 722 1555 1555 2.03
SSBOND 3 CYS B 375 CYS B 386 1555 1555 2.03
SSBOND 4 CYS B 627 CYS B 722 1555 1555 2.03
LINK C ASP A 143 N MSE A 144 1555 1555 1.33
LINK C MSE A 144 N SER A 145 1555 1555 1.33
LINK C ILE A 220 N MSE A 221 1555 1555 1.33
LINK C MSE A 221 N ALA A 222 1555 1555 1.33
LINK C SER A 282 N MSE A 283 1555 1555 1.33
LINK C MSE A 283 N SER A 284 1555 1555 1.33
LINK C GLY A 379 N MSE A 380 1555 1555 1.33
LINK C MSE A 380 N LEU A 381 1555 1555 1.33
LINK C GLY A 390 N MSE A 391 1555 1555 1.33
LINK C MSE A 391 N SER A 392 1555 1555 1.33
LINK C LEU A 504 N MSE A 505 1555 1555 1.33
LINK C MSE A 505 N ASP A 506 1555 1555 1.34
LINK C ALA A 507 N MSE A 508 1555 1555 1.33
LINK C MSE A 508 N HIS A 509 1555 1555 1.33
LINK C GLN A 563 N MSE A 564 1555 1555 1.33
LINK C MSE A 564 N VAL A 565 1555 1555 1.33
LINK C LYS A 573 N MSE A 574 1555 1555 1.33
LINK C MSE A 574 N PHE A 575 1555 1555 1.33
LINK C ALA A 682 N MSE A 683 1555 1555 1.33
LINK C MSE A 683 N ARG A 684 1555 1555 1.33
LINK C ASP B 143 N MSE B 144 1555 1555 1.33
LINK C MSE B 144 N SER B 145 1555 1555 1.33
LINK C ILE B 220 N MSE B 221 1555 1555 1.33
LINK C MSE B 221 N ALA B 222 1555 1555 1.33
LINK C GLY B 379 N MSE B 380 1555 1555 1.33
LINK C MSE B 380 N LEU B 381 1555 1555 1.33
LINK C GLY B 390 N MSE B 391 1555 1555 1.33
LINK C MSE B 391 N SER B 392 1555 1555 1.33
LINK C LEU B 504 N MSE B 505 1555 1555 1.33
LINK C MSE B 505 N ASP B 506 1555 1555 1.33
LINK C ALA B 507 N MSE B 508 1555 1555 1.33
LINK C MSE B 508 N HIS B 509 1555 1555 1.33
LINK C GLN B 563 N MSE B 564 1555 1555 1.33
LINK C MSE B 564 N VAL B 565 1555 1555 1.33
LINK C LYS B 573 N MSE B 574 1555 1555 1.33
LINK C MSE B 574 N PHE B 575 1555 1555 1.33
LINK C ALA B 682 N MSE B 683 1555 1555 1.33
LINK C MSE B 683 N ARG B 684 1555 1555 1.34
CISPEP 1 GLY A 516 PRO A 517 0 -3.33
CISPEP 2 PRO A 517 PRO A 518 0 -0.51
CISPEP 3 GLY B 516 PRO B 517 0 0.26
CISPEP 4 PRO B 517 PRO B 518 0 1.30
SITE 1 AC1 6 ALA A 49 LEU A 50 SER A 99 LYS A 333
SITE 2 AC1 6 GLY A 376 PHE A 377
SITE 1 AC2 4 ASP B 369 GLU B 388 ILE B 407 ASP B 409
CRYST1 111.105 133.501 169.070 90.00 90.00 90.00 P 21 21 21 8
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 0.009000 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007491 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005915 0.00000
TER 5394 PRO A 726
TER 10659 ALA B 723
MASTER 443 0 21 37 82 0 3 610681 2 222 118
END |