HEADER HYDROLASE 18-SEP-18 6MHM
TITLE CRYSTAL STRUCTURE OF HUMAN ACID CERAMIDASE IN COVALENT COMPLEX WITH
TITLE 2 CARMOFUR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACID CERAMIDASE SUBUNIT ALPHA;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: ACID CDASE,ACYLSPHINGOSINE DEACYLASE,N-ACYLSPHINGOSINE
COMPND 5 AMIDOHYDROLASE,PUTATIVE 32 KDA HEART PROTEIN,PHP32;
COMPND 6 EC: 3.5.1.23;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: ACID CERAMIDASE SUBUNIT BETA;
COMPND 10 CHAIN: B, D;
COMPND 11 SYNONYM: ACID CDASE,ACYLSPHINGOSINE DEACYLASE,N-ACYLSPHINGOSINE
COMPND 12 AMIDOHYDROLASE,PUTATIVE 32 KDA HEART PROTEIN,PHP32;
COMPND 13 EC: 3.5.1.23;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ASAH1, ASAH, HSD-33, HSD33;
SOURCE 6 EXPRESSION_SYSTEM: UNIDENTIFIED BACULOVIRUS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10469;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: ASAH1, ASAH, HSD-33, HSD33;
SOURCE 13 EXPRESSION_SYSTEM: UNIDENTIFIED BACULOVIRUS;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 10469
KEYWDS ACID CERAMIDASE, ACID CERAMIDASE INHIBITORS, BENZOXAZOLONE
KEYWDS 2 CARBOXAMIDES, CARMOFUR, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.DEMENTIEV,A.JOACHIMIAK,N.DOAN
REVDAT 4 11-OCT-23 6MHM 1 HETSYN
REVDAT 3 29-JUL-20 6MHM 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE ATOM
REVDAT 2 24-APR-19 6MHM 1 JRNL REMARK LINK
REVDAT 1 23-JAN-19 6MHM 0
JRNL AUTH A.DEMENTIEV,A.JOACHIMIAK,H.NGUYEN,A.GORELIK,K.ILLES,
JRNL AUTH 2 S.SHABANI,M.GELSOMINO,E.E.AHN,B.NAGAR,N.DOAN
JRNL TITL MOLECULAR MECHANISM OF INHIBITION OF ACID CERAMIDASE BY
JRNL TITL 2 CARMOFUR.
JRNL REF J. MED. CHEM. V. 62 987 2019
JRNL REFN ISSN 1520-4804
JRNL PMID 30525581
JRNL DOI 10.1021/ACS.JMEDCHEM.8B01723
REMARK 2
REMARK 2 RESOLUTION. 2.74 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.11.1_2575
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) : 2.74
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.65
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 23252
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.218
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.262
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.600
REMARK 3 FREE R VALUE TEST SET COUNT : 2000
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 48.6551 - 5.9074 1.00 2199 207 0.2237 0.2209
REMARK 3 2 5.9074 - 4.6901 1.00 2136 201 0.1929 0.2342
REMARK 3 3 4.6901 - 4.0976 1.00 2143 202 0.1774 0.2282
REMARK 3 4 4.0976 - 3.7231 1.00 2138 201 0.1875 0.2531
REMARK 3 5 3.7231 - 3.4563 1.00 2119 199 0.2138 0.2811
REMARK 3 6 3.4563 - 3.2526 1.00 2100 198 0.2201 0.3007
REMARK 3 7 3.2526 - 3.0897 1.00 2125 200 0.2376 0.2822
REMARK 3 8 3.0897 - 2.9553 1.00 2116 199 0.2807 0.3410
REMARK 3 9 2.9553 - 2.8415 1.00 2117 199 0.2673 0.3484
REMARK 3 10 2.8415 - 2.7435 0.98 2059 194 0.2957 0.3671
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) : 0.400
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.950
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 53.81
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.09
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 : 0.006 6288
REMARK 3 ANGLE : 1.006 8568
REMARK 3 CHIRALITY : 0.046 967
REMARK 3 PLANARITY : 0.004 1060
REMARK 3 DIHEDRAL : 5.684 3630
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 6MHM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-SEP-18.
REMARK 100 THE DEPOSITION ID IS D_1000236900.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-JUL-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23259
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.740
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 4.900
REMARK 200 R MERGE (I) : 0.11100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.74
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.79
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.68000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> 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: 5U7Z
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM-PHOSPHATE-CITRATE, PH
REMARK 280 4.3, 0.275 M LITHIUM SULFATE, AND 18% POLYETHYLENE GLYCOL 1000,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 76.85900
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.32500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 76.85900
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 34.32500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, G, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ASP A 12
REMARK 465 ARG A 13
REMARK 465 HIS A 14
REMARK 465 HIS A 15
REMARK 465 HIS A 16
REMARK 465 HIS A 17
REMARK 465 HIS A 18
REMARK 465 HIS A 19
REMARK 465 LYS A 20
REMARK 465 LEU A 21
REMARK 465 GLN A 22
REMARK 465 HIS A 23
REMARK 465 ALA A 24
REMARK 465 PRO A 25
REMARK 465 PRO A 26
REMARK 465 THR A 141
REMARK 465 ILE A 142
REMARK 465 ASP C 12
REMARK 465 ARG C 13
REMARK 465 HIS C 14
REMARK 465 HIS C 15
REMARK 465 HIS C 16
REMARK 465 HIS C 17
REMARK 465 HIS C 18
REMARK 465 HIS C 19
REMARK 465 LYS C 20
REMARK 465 LEU C 21
REMARK 465 GLN C 22
REMARK 465 HIS C 23
REMARK 465 ALA C 24
REMARK 465 PRO C 25
REMARK 465 PRO C 26
REMARK 465 THR C 141
REMARK 465 ILE C 142
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 LYS A 92 CG CD CE NZ
REMARK 470 LYS B 196 CG CD CE NZ
REMARK 470 GLN B 311 CG CD OE1 NE2
REMARK 470 LYS C 60 CG CD CE NZ
REMARK 470 LYS C 92 CG CD CE NZ
REMARK 470 LYS D 152 CG CD CE NZ
REMARK 470 LYS D 196 CG CD CE NZ
REMARK 470 LYS D 272 CG CD CE NZ
REMARK 470 LYS D 310 CG CD CE NZ
REMARK 470 GLN D 311 CG CD OE1 NE2
REMARK 470 ARG D 343 CG CD NE CZ NH1 NH2
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 D 274 O2 SO4 D 411 1.30
REMARK 500 NH1 ARG B 334 O HOH B 501 2.06
REMARK 500 OE1 GLN A 95 O4 SO4 A 203 2.09
REMARK 500 O MET B 210 OG1 THR B 253 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS B 143 CB CYS B 143 SG -0.166
REMARK 500 CYS D 143 CB CYS D 143 SG -0.111
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 PHE A 87 -66.77 -107.23
REMARK 500 ASP B 174 61.72 63.33
REMARK 500 LEU B 218 -78.42 -111.53
REMARK 500 ASP B 303 146.20 -173.45
REMARK 500 THR B 319 -107.12 -102.22
REMARK 500 SER B 345 153.39 77.50
REMARK 500 LEU D 218 -79.77 -115.28
REMARK 500 LYS D 243 94.97 -69.77
REMARK 500 THR D 319 -111.37 -105.66
REMARK 500 SER D 345 153.46 69.64
REMARK 500
REMARK 500 REMARK: NULL
REMARK 630
REMARK 630 MOLECULE TYPE: OLIGOSACCHARIDE INHIBITOR
REMARK 630 MOLECULE NAME: 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 630 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 630
REMARK 630 M RES C SSSEQI
REMARK 630 NAG B 406
REMARK 630 NAG D 404
REMARK 630 NAG D 407
REMARK 630 SOURCE: NULL
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP: NULL
REMARK 630 DETAILS: OLIGOSACCHARIDE
DBREF 6MHM A 22 142 UNP Q13510 ASAH1_HUMAN 22 142
DBREF 6MHM B 143 395 UNP Q13510 ASAH1_HUMAN 143 395
DBREF 6MHM C 22 142 UNP Q13510 ASAH1_HUMAN 22 142
DBREF 6MHM D 143 395 UNP Q13510 ASAH1_HUMAN 143 395
SEQADV 6MHM ASP A 12 UNP Q13510 EXPRESSION TAG
SEQADV 6MHM ARG A 13 UNP Q13510 EXPRESSION TAG
SEQADV 6MHM HIS A 14 UNP Q13510 EXPRESSION TAG
SEQADV 6MHM HIS A 15 UNP Q13510 EXPRESSION TAG
SEQADV 6MHM HIS A 16 UNP Q13510 EXPRESSION TAG
SEQADV 6MHM HIS A 17 UNP Q13510 EXPRESSION TAG
SEQADV 6MHM HIS A 18 UNP Q13510 EXPRESSION TAG
SEQADV 6MHM HIS A 19 UNP Q13510 EXPRESSION TAG
SEQADV 6MHM LYS A 20 UNP Q13510 EXPRESSION TAG
SEQADV 6MHM LEU A 21 UNP Q13510 EXPRESSION TAG
SEQADV 6MHM MET A 72 UNP Q13510 VAL 72 VARIANT
SEQADV 6MHM VAL A 93 UNP Q13510 ILE 93 VARIANT
SEQADV 6MHM ALA B 246 UNP Q13510 VAL 246 VARIANT
SEQADV 6MHM ASP C 12 UNP Q13510 EXPRESSION TAG
SEQADV 6MHM ARG C 13 UNP Q13510 EXPRESSION TAG
SEQADV 6MHM HIS C 14 UNP Q13510 EXPRESSION TAG
SEQADV 6MHM HIS C 15 UNP Q13510 EXPRESSION TAG
SEQADV 6MHM HIS C 16 UNP Q13510 EXPRESSION TAG
SEQADV 6MHM HIS C 17 UNP Q13510 EXPRESSION TAG
SEQADV 6MHM HIS C 18 UNP Q13510 EXPRESSION TAG
SEQADV 6MHM HIS C 19 UNP Q13510 EXPRESSION TAG
SEQADV 6MHM LYS C 20 UNP Q13510 EXPRESSION TAG
SEQADV 6MHM LEU C 21 UNP Q13510 EXPRESSION TAG
SEQADV 6MHM MET C 72 UNP Q13510 VAL 72 VARIANT
SEQADV 6MHM VAL C 93 UNP Q13510 ILE 93 VARIANT
SEQADV 6MHM ALA D 246 UNP Q13510 VAL 246 VARIANT
SEQRES 1 A 131 ASP ARG HIS HIS HIS HIS HIS HIS LYS LEU GLN HIS ALA
SEQRES 2 A 131 PRO PRO TRP THR GLU ASP CYS ARG LYS SER THR TYR PRO
SEQRES 3 A 131 PRO SER GLY PRO THR TYR ARG GLY ALA VAL PRO TRP TYR
SEQRES 4 A 131 THR ILE ASN LEU ASP LEU PRO PRO TYR LYS ARG TRP HIS
SEQRES 5 A 131 GLU LEU MET LEU ASP LYS ALA PRO MET LEU LYS VAL ILE
SEQRES 6 A 131 VAL ASN SER LEU LYS ASN MET ILE ASN THR PHE VAL PRO
SEQRES 7 A 131 SER GLY LYS VAL MET GLN VAL VAL ASP GLU LYS LEU PRO
SEQRES 8 A 131 GLY LEU LEU GLY ASN PHE PRO GLY PRO PHE GLU GLU GLU
SEQRES 9 A 131 MET LYS GLY ILE ALA ALA VAL THR ASP ILE PRO LEU GLY
SEQRES 10 A 131 GLU ILE ILE SER PHE ASN ILE PHE TYR GLU LEU PHE THR
SEQRES 11 A 131 ILE
SEQRES 1 B 253 CYS THR SER ILE VAL ALA GLU ASP LYS LYS GLY HIS LEU
SEQRES 2 B 253 ILE HIS GLY ARG ASN MET ASP PHE GLY VAL PHE LEU GLY
SEQRES 3 B 253 TRP ASN ILE ASN ASN ASP THR TRP VAL ILE THR GLU GLN
SEQRES 4 B 253 LEU LYS PRO LEU THR VAL ASN LEU ASP PHE GLN ARG ASN
SEQRES 5 B 253 ASN LYS THR VAL PHE LYS ALA SER SER PHE ALA GLY TYR
SEQRES 6 B 253 VAL GLY MET LEU THR GLY PHE LYS PRO GLY LEU PHE SER
SEQRES 7 B 253 LEU THR LEU ASN GLU ARG PHE SER ILE ASN GLY GLY TYR
SEQRES 8 B 253 LEU GLY ILE LEU GLU TRP ILE LEU GLY LYS LYS ASP ALA
SEQRES 9 B 253 MET TRP ILE GLY PHE LEU THR ARG THR VAL LEU GLU ASN
SEQRES 10 B 253 SER THR SER TYR GLU GLU ALA LYS ASN LEU LEU THR LYS
SEQRES 11 B 253 THR LYS ILE LEU ALA PRO ALA TYR PHE ILE LEU GLY GLY
SEQRES 12 B 253 ASN GLN SER GLY GLU GLY CYS VAL ILE THR ARG ASP ARG
SEQRES 13 B 253 LYS GLU SER LEU ASP VAL TYR GLU LEU ASP ALA LYS GLN
SEQRES 14 B 253 GLY ARG TRP TYR VAL VAL GLN THR ASN TYR ASP ARG TRP
SEQRES 15 B 253 LYS HIS PRO PHE PHE LEU ASP ASP ARG ARG THR PRO ALA
SEQRES 16 B 253 LYS MET CYS LEU ASN ARG THR SER GLN GLU ASN ILE SER
SEQRES 17 B 253 PHE GLU THR MET TYR ASP VAL LEU SER THR LYS PRO VAL
SEQRES 18 B 253 LEU ASN LYS LEU THR VAL TYR THR THR LEU ILE ASP VAL
SEQRES 19 B 253 THR LYS GLY GLN PHE GLU THR TYR LEU ARG ASP CYS PRO
SEQRES 20 B 253 ASP PRO CYS ILE GLY TRP
SEQRES 1 C 131 ASP ARG HIS HIS HIS HIS HIS HIS LYS LEU GLN HIS ALA
SEQRES 2 C 131 PRO PRO TRP THR GLU ASP CYS ARG LYS SER THR TYR PRO
SEQRES 3 C 131 PRO SER GLY PRO THR TYR ARG GLY ALA VAL PRO TRP TYR
SEQRES 4 C 131 THR ILE ASN LEU ASP LEU PRO PRO TYR LYS ARG TRP HIS
SEQRES 5 C 131 GLU LEU MET LEU ASP LYS ALA PRO MET LEU LYS VAL ILE
SEQRES 6 C 131 VAL ASN SER LEU LYS ASN MET ILE ASN THR PHE VAL PRO
SEQRES 7 C 131 SER GLY LYS VAL MET GLN VAL VAL ASP GLU LYS LEU PRO
SEQRES 8 C 131 GLY LEU LEU GLY ASN PHE PRO GLY PRO PHE GLU GLU GLU
SEQRES 9 C 131 MET LYS GLY ILE ALA ALA VAL THR ASP ILE PRO LEU GLY
SEQRES 10 C 131 GLU ILE ILE SER PHE ASN ILE PHE TYR GLU LEU PHE THR
SEQRES 11 C 131 ILE
SEQRES 1 D 253 CYS THR SER ILE VAL ALA GLU ASP LYS LYS GLY HIS LEU
SEQRES 2 D 253 ILE HIS GLY ARG ASN MET ASP PHE GLY VAL PHE LEU GLY
SEQRES 3 D 253 TRP ASN ILE ASN ASN ASP THR TRP VAL ILE THR GLU GLN
SEQRES 4 D 253 LEU LYS PRO LEU THR VAL ASN LEU ASP PHE GLN ARG ASN
SEQRES 5 D 253 ASN LYS THR VAL PHE LYS ALA SER SER PHE ALA GLY TYR
SEQRES 6 D 253 VAL GLY MET LEU THR GLY PHE LYS PRO GLY LEU PHE SER
SEQRES 7 D 253 LEU THR LEU ASN GLU ARG PHE SER ILE ASN GLY GLY TYR
SEQRES 8 D 253 LEU GLY ILE LEU GLU TRP ILE LEU GLY LYS LYS ASP ALA
SEQRES 9 D 253 MET TRP ILE GLY PHE LEU THR ARG THR VAL LEU GLU ASN
SEQRES 10 D 253 SER THR SER TYR GLU GLU ALA LYS ASN LEU LEU THR LYS
SEQRES 11 D 253 THR LYS ILE LEU ALA PRO ALA TYR PHE ILE LEU GLY GLY
SEQRES 12 D 253 ASN GLN SER GLY GLU GLY CYS VAL ILE THR ARG ASP ARG
SEQRES 13 D 253 LYS GLU SER LEU ASP VAL TYR GLU LEU ASP ALA LYS GLN
SEQRES 14 D 253 GLY ARG TRP TYR VAL VAL GLN THR ASN TYR ASP ARG TRP
SEQRES 15 D 253 LYS HIS PRO PHE PHE LEU ASP ASP ARG ARG THR PRO ALA
SEQRES 16 D 253 LYS MET CYS LEU ASN ARG THR SER GLN GLU ASN ILE SER
SEQRES 17 D 253 PHE GLU THR MET TYR ASP VAL LEU SER THR LYS PRO VAL
SEQRES 18 D 253 LEU ASN LYS LEU THR VAL TYR THR THR LEU ILE ASP VAL
SEQRES 19 D 253 THR LYS GLY GLN PHE GLU THR TYR LEU ARG ASP CYS PRO
SEQRES 20 D 253 ASP PRO CYS ILE GLY TRP
HET NAG E 1 14
HET NAG E 2 14
HET NAG E 3 14
HET NAG F 1 14
HET NAG F 2 14
HET NAG G 1 14
HET NAG G 2 14
HET NAG G 3 14
HET NAG H 1 14
HET NAG H 2 14
HET SO4 A 201 5
HET SO4 A 202 5
HET SO4 A 203 5
HET NAG B 406 14
HET JRY B 407 9
HET SO4 B 408 5
HET SO4 B 409 5
HET SO4 B 410 5
HET SO4 C 201 5
HET SO4 C 202 5
HET SO4 C 203 5
HET NAG D 404 14
HET NAG D 407 14
HET JRY D 408 9
HET SO4 D 409 5
HET SO4 D 410 5
HET SO4 D 411 5
HET SO4 D 412 5
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM SO4 SULFATE ION
HETNAM JRY HEXYLCARBAMIC ACID
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
FORMUL 5 NAG 13(C8 H15 N O6)
FORMUL 9 SO4 13(O4 S 2-)
FORMUL 13 JRY 2(C7 H15 N O2)
FORMUL 27 HOH *79(H2 O)
HELIX 1 AA1 PRO A 57 ARG A 61 5 5
HELIX 2 AA2 TRP A 62 THR A 86 1 25
HELIX 3 AA3 PRO A 89 LYS A 100 1 12
HELIX 4 AA4 LYS A 100 GLY A 106 1 7
HELIX 5 AA5 PRO A 111 ASP A 124 1 14
HELIX 6 AA6 PRO A 126 ILE A 135 1 10
HELIX 7 AA7 ILE A 135 PHE A 140 1 6
HELIX 8 AA8 VAL B 177 LYS B 183 1 7
HELIX 9 AA9 GLY B 231 GLY B 242 1 12
HELIX 10 AB1 TRP B 248 SER B 260 1 13
HELIX 11 AB2 SER B 262 THR B 273 1 12
HELIX 12 AB3 ASP B 308 GLY B 312 5 5
HELIX 13 AB4 ARG B 333 SER B 345 1 13
HELIX 14 AB5 GLN B 346 ILE B 349 5 4
HELIX 15 AB6 SER B 350 LEU B 358 1 9
HELIX 16 AB7 PRO C 57 ARG C 61 5 5
HELIX 17 AB8 TRP C 62 VAL C 88 1 27
HELIX 18 AB9 PRO C 89 LEU C 105 1 17
HELIX 19 AC1 PRO C 111 ASP C 124 1 14
HELIX 20 AC2 PRO C 126 ILE C 135 1 10
HELIX 21 AC3 ILE C 135 PHE C 140 1 6
HELIX 22 AC4 VAL D 177 LYS D 183 1 7
HELIX 23 AC5 GLY D 232 GLY D 242 1 11
HELIX 24 AC6 TRP D 248 SER D 260 1 13
HELIX 25 AC7 SER D 262 THR D 273 1 12
HELIX 26 AC8 ARG D 333 SER D 345 1 13
HELIX 27 AC9 GLN D 346 ILE D 349 5 4
HELIX 28 AD1 SER D 350 SER D 359 1 10
SHEET 1 AA1 6 TYR A 43 ALA A 46 0
SHEET 2 AA1 6 GLN B 380 ARG B 386 -1 O LEU B 385 N GLY A 45
SHEET 3 AA1 6 THR B 368 ASP B 375 -1 N LEU B 373 O GLU B 382
SHEET 4 AA1 6 LEU B 155 ASP B 162 -1 N HIS B 157 O ILE B 374
SHEET 5 AA1 6 THR B 144 GLU B 149 -1 N ILE B 146 O GLY B 158
SHEET 6 AA1 6 TYR B 315 GLN B 318 -1 O GLN B 318 N SER B 145
SHEET 1 AA2 8 TRP A 49 ASN A 53 0
SHEET 2 AA2 8 THR B 186 GLN B 192 1 O ASN B 188 N TYR A 50
SHEET 3 AA2 8 THR B 197 PHE B 204 -1 O VAL B 198 N PHE B 191
SHEET 4 AA2 8 THR B 212 LYS B 215 -1 O PHE B 214 N LYS B 200
SHEET 5 AA2 8 PHE B 219 GLU B 225 -1 O PHE B 219 N LYS B 215
SHEET 6 AA2 8 ALA B 279 GLY B 284 -1 O TYR B 280 N ASN B 224
SHEET 7 AA2 8 GLY B 291 ARG B 296 -1 O ILE B 294 N PHE B 281
SHEET 8 AA2 8 SER B 301 GLU B 306 -1 O TYR B 305 N VAL B 293
SHEET 1 AA3 2 TRP B 169 ASN B 170 0
SHEET 2 AA3 2 THR B 175 TRP B 176 -1 O THR B 175 N ASN B 170
SHEET 1 AA4 6 GLY C 45 ALA C 46 0
SHEET 2 AA4 6 GLN D 380 LEU D 385 -1 O LEU D 385 N GLY C 45
SHEET 3 AA4 6 THR D 368 ASP D 375 -1 N THR D 371 O TYR D 384
SHEET 4 AA4 6 LEU D 155 ASP D 162 -1 N MET D 161 O VAL D 369
SHEET 5 AA4 6 THR D 144 GLU D 149 -1 N ALA D 148 O ILE D 156
SHEET 6 AA4 6 TYR D 315 GLN D 318 -1 O VAL D 316 N VAL D 147
SHEET 1 AA5 8 TRP C 49 ASN C 53 0
SHEET 2 AA5 8 THR D 186 GLN D 192 1 O ASP D 190 N TYR C 50
SHEET 3 AA5 8 THR D 197 PHE D 204 -1 O VAL D 198 N PHE D 191
SHEET 4 AA5 8 THR D 212 LYS D 215 -1 O PHE D 214 N LYS D 200
SHEET 5 AA5 8 PHE D 219 GLU D 225 -1 O PHE D 219 N LYS D 215
SHEET 6 AA5 8 ALA D 279 GLY D 284 -1 O GLY D 284 N SER D 220
SHEET 7 AA5 8 GLY D 291 ARG D 296 -1 O ILE D 294 N PHE D 281
SHEET 8 AA5 8 SER D 301 GLU D 306 -1 O TYR D 305 N VAL D 293
SHEET 1 AA6 2 TRP D 169 ASN D 170 0
SHEET 2 AA6 2 THR D 175 TRP D 176 -1 O THR D 175 N ASN D 170
SSBOND 1 CYS A 31 CYS B 340 1555 1555 2.03
SSBOND 2 CYS B 388 CYS B 392 1555 1555 2.03
SSBOND 3 CYS C 31 CYS D 340 1555 1555 2.03
SSBOND 4 CYS D 388 CYS D 392 1555 1555 2.03
LINK SG CYS B 143 C07 JRY B 407 1555 1555 1.80
LINK ND2 ASN B 173 C1 NAG E 1 1555 1555 1.45
LINK ND2 ASN B 259 C1 NAG F 1 1555 1555 1.44
LINK ND2 ASN B 286 C1 NAG B 406 1555 1555 1.44
LINK SG CYS D 143 C07 JRY D 408 1555 1555 1.80
LINK ND2 ASN D 173 C1 NAG G 1 1555 1555 1.45
LINK ND2 ASN D 259 C1 NAG H 1 1555 1555 1.44
LINK ND2 ASN D 286 C1 NAG D 404 1555 1555 1.44
LINK ND2 ASN D 342 C1 NAG D 407 1555 1555 1.46
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.45
LINK O4 NAG E 2 C1 NAG E 3 1555 1555 1.47
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.44
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.45
LINK O4 NAG G 2 C1 NAG G 3 1555 1555 1.47
LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.43
CISPEP 1 TYR A 36 PRO A 37 0 -3.03
CISPEP 2 LYS B 361 PRO B 362 0 5.62
CISPEP 3 ASP B 390 PRO B 391 0 0.92
CISPEP 4 TYR C 36 PRO C 37 0 -2.42
CISPEP 5 LYS D 361 PRO D 362 0 4.38
CISPEP 6 ASP D 390 PRO D 391 0 1.04
CRYST1 153.718 68.650 98.386 90.00 120.73 90.00 C 1 2 1 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 0.006505 0.000000 0.003867 0.00000
SCALE2 0.000000 0.014567 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011824 0.00000
(ATOM LINES ARE NOT SHOWN.)
END