| 7wab-pdb | HEADER HYDROLASE 14-DEC-21 7WAB
TITLE CRYSTAL STRUCTURE OF THE PROLYL ENDOPROTEASE, PEP, FROM ASPERGILLUS
TITLE 2 NIGER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COMPASS (COMPLEX PROTEINS ASSOCIATED WITH SET1P) COMPONENT
COMPND 3 SHG1 FAMILY PROTEIN;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: PROLYL ENDOPROTEASE, PEP
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ASPERGILLUS NIGER;
SOURCE 3 ORGANISM_TAXID: 5061
KEYWDS PROTEASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.MIYAZONO,K.KUBOTA,K.TAKAHASHI,M.TANOKURA
REVDAT 1 12-JAN-22 7WAB 0
JRNL AUTH K.MIYAZONO,K.KUBOTA,K.TAKAHASHI,M.TANOKURA
JRNL TITL CRYSTAL STRUCTURE AND SUBSTATE RECOGNITION MECHANISM OF THE
JRNL TITL 2 PROLYL ENDOPROTEASE PEP FROM ASPERGILLUS NIGER
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. 2022
JRNL REFN ESSN 1090-2104
JRNL DOI 10.1016/J.BBRC.2021.12.114
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.19
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) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 17.14
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.040
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.1
REMARK 3 NUMBER OF REFLECTIONS : 107457
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.165
REMARK 3 R VALUE (WORKING SET) : 0.164
REMARK 3 FREE R VALUE : 0.193
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.110
REMARK 3 FREE R VALUE TEST SET COUNT : 5492
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 17.1400 - 5.3800 0.91 3330 181 0.1568 0.1593
REMARK 3 2 5.3800 - 4.2900 0.93 3373 197 0.1291 0.1452
REMARK 3 3 4.2900 - 3.7600 0.94 3385 216 0.1218 0.1409
REMARK 3 4 3.7600 - 3.4200 0.95 3456 192 0.1363 0.1663
REMARK 3 5 3.4200 - 3.1700 0.95 3444 193 0.1526 0.1631
REMARK 3 6 3.1700 - 2.9900 0.96 3517 171 0.1676 0.1931
REMARK 3 7 2.9900 - 2.8400 0.97 3580 153 0.1721 0.2071
REMARK 3 8 2.8400 - 2.7200 0.97 3544 179 0.1816 0.2304
REMARK 3 9 2.7200 - 2.6100 0.97 3548 229 0.1790 0.2233
REMARK 3 10 2.6100 - 2.5200 0.98 3575 182 0.1767 0.2204
REMARK 3 11 2.5200 - 2.4400 0.98 3548 222 0.1776 0.2224
REMARK 3 12 2.4400 - 2.3700 0.98 3607 169 0.1696 0.2342
REMARK 3 13 2.3700 - 2.3100 0.98 3579 202 0.1785 0.2138
REMARK 3 14 2.3100 - 2.2500 0.98 3554 174 0.1756 0.2313
REMARK 3 15 2.2500 - 2.2000 0.98 3615 185 0.1756 0.2254
REMARK 3 16 2.2000 - 2.1600 0.99 3565 213 0.1641 0.1963
REMARK 3 17 2.1600 - 2.1100 0.99 3649 164 0.1684 0.2526
REMARK 3 18 2.1100 - 2.0700 0.98 3557 186 0.1768 0.2076
REMARK 3 19 2.0700 - 2.0400 0.99 3566 229 0.1745 0.2237
REMARK 3 20 2.0400 - 2.0000 0.98 3646 156 0.1819 0.2174
REMARK 3 21 2.0000 - 1.9700 0.97 3597 151 0.1852 0.2162
REMARK 3 22 1.9700 - 1.9400 0.94 3398 208 0.2087 0.2644
REMARK 3 23 1.9400 - 1.9100 0.90 3257 190 0.2385 0.2866
REMARK 3 24 1.9100 - 1.8800 0.89 3205 209 0.2363 0.2282
REMARK 3 25 1.8800 - 1.8600 0.86 3200 142 0.2271 0.2661
REMARK 3 26 1.8600 - 1.8300 0.85 3083 154 0.2087 0.2343
REMARK 3 27 1.8300 - 1.8100 0.84 3068 157 0.2166 0.2649
REMARK 3 28 1.8100 - 1.7900 0.81 2948 194 0.2121 0.2611
REMARK 3 29 1.7900 - 1.7700 0.79 2845 153 0.2284 0.2536
REMARK 3 30 1.7700 - 1.7500 0.74 2726 141 0.2340 0.3116
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) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.970
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.14
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 : 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 43 THROUGH 102 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.1548 51.0784 -5.8928
REMARK 3 T TENSOR
REMARK 3 T11: 0.1831 T22: 0.2314
REMARK 3 T33: 0.3588 T12: 0.0059
REMARK 3 T13: 0.0236 T23: 0.0268
REMARK 3 L TENSOR
REMARK 3 L11: 5.7512 L22: 2.3303
REMARK 3 L33: 3.0206 L12: 1.6085
REMARK 3 L13: 3.3046 L23: 1.6344
REMARK 3 S TENSOR
REMARK 3 S11: 0.1125 S12: -0.5890 S13: 0.4005
REMARK 3 S21: 0.1368 S22: -0.1121 S23: 0.1196
REMARK 3 S31: 0.0603 S32: -0.4063 S33: 0.0154
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 103 THROUGH 172 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.8758 48.0256 -9.6322
REMARK 3 T TENSOR
REMARK 3 T11: 0.1719 T22: 0.1622
REMARK 3 T33: 0.2831 T12: 0.0183
REMARK 3 T13: -0.0355 T23: 0.0326
REMARK 3 L TENSOR
REMARK 3 L11: 3.2080 L22: 1.7582
REMARK 3 L33: 1.0070 L12: 1.5425
REMARK 3 L13: 0.5594 L23: 0.5298
REMARK 3 S TENSOR
REMARK 3 S11: -0.0445 S12: 0.1207 S13: 0.5174
REMARK 3 S21: -0.0590 S22: 0.0298 S23: 0.0505
REMARK 3 S31: -0.0647 S32: 0.0746 S33: 0.0032
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 173 THROUGH 526 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.9679 28.2560 6.7304
REMARK 3 T TENSOR
REMARK 3 T11: 0.1518 T22: 0.1933
REMARK 3 T33: 0.1659 T12: -0.0136
REMARK 3 T13: -0.0402 T23: 0.0188
REMARK 3 L TENSOR
REMARK 3 L11: 0.4486 L22: 0.4629
REMARK 3 L33: 0.9337 L12: 0.1125
REMARK 3 L13: -0.5360 L23: -0.2805
REMARK 3 S TENSOR
REMARK 3 S11: 0.0080 S12: -0.1419 S13: -0.0123
REMARK 3 S21: 0.0620 S22: -0.0699 S23: -0.0581
REMARK 3 S31: 0.0137 S32: 0.1130 S33: 0.0639
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 7WAB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-DEC-21.
REMARK 100 THE DEPOSITION ID IS D_1300026304.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-JUN-10
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : 2.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-1A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.17
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 107457
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 44.530
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.2
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : 0.06100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.78
REMARK 200 COMPLETENESS FOR SHELL (%) : 75.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.42200
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: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M GLYCINE BUFFER PH 2.5, 2.72M
REMARK 280 NACL, 3% ISOPROPANOL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 21 2
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 -Y+1/2,X+1/2,Z
REMARK 290 4555 Y+1/2,-X+1/2,Z
REMARK 290 5555 -X+1/2,Y+1/2,-Z
REMARK 290 6555 X+1/2,-Y+1/2,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 0.000000 -1.000000 0.000000 72.25850
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 72.25850
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 72.25850
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 72.25850
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 72.25850
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 72.25850
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 72.25850
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 72.25850
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
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 0.00000
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 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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 A1096 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1168 LIES ON A SPECIAL POSITION.
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 88 32.48 -75.11
REMARK 500 TYR A 122 -1.82 81.43
REMARK 500 SER A 179 -139.85 61.72
REMARK 500 THR A 195 -60.73 -100.59
REMARK 500 PHE A 384 -83.42 68.74
REMARK 500 PHE A 490 -137.36 -107.59
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 A1222 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH A1223 DISTANCE = 6.31 ANGSTROMS
DBREF1 7WAB A 43 526 UNP A0A3F3RXI7_ASPNG
DBREF2 7WAB A A0A3F3RXI7 43 526
SEQRES 1 A 484 THR THR GLY GLU ALA TYR PHE GLU GLN LEU LEU ASP HIS
SEQRES 2 A 484 HIS ASN PRO GLU LYS GLY THR PHE SER GLN ARG TYR TRP
SEQRES 3 A 484 TRP SER THR GLU TYR TRP GLY GLY PRO GLY SER PRO VAL
SEQRES 4 A 484 VAL LEU PHE ASN PRO GLY GLU VAL SER ALA ASP GLY TYR
SEQRES 5 A 484 GLU GLY TYR LEU THR ASN ASP THR LEU THR GLY VAL TYR
SEQRES 6 A 484 ALA GLN GLU ILE GLN GLY ALA VAL ILE LEU ILE GLU HIS
SEQRES 7 A 484 ARG TYR TRP GLY ASP SER SER PRO TYR GLU VAL LEU ASN
SEQRES 8 A 484 ALA GLU THR LEU GLN TYR LEU THR LEU ASP GLN SER ILE
SEQRES 9 A 484 LEU ASP MET THR TYR PHE ALA GLU THR VAL LYS LEU GLN
SEQRES 10 A 484 PHE ASP ASN SER SER ARG SER ASN ALA GLN ASN ALA PRO
SEQRES 11 A 484 TRP VAL MET VAL GLY GLY SER TYR SER GLY ALA LEU THR
SEQRES 12 A 484 ALA TRP THR GLU SER ILE ALA PRO GLY THR PHE TRP ALA
SEQRES 13 A 484 TYR HIS ALA THR SER ALA PRO VAL GLU ALA ILE TYR ASP
SEQRES 14 A 484 PHE TRP GLN TYR PHE TYR PRO ILE GLN GLN GLY MET ALA
SEQRES 15 A 484 GLN ASN CYS SER LYS ASP VAL SER LEU VAL ALA GLU TYR
SEQRES 16 A 484 VAL ASP LYS ILE GLY LYS ASN GLY THR ALA LYS GLU GLN
SEQRES 17 A 484 GLN GLU LEU LYS GLU LEU PHE GLY LEU GLY ALA VAL GLU
SEQRES 18 A 484 HIS TYR ASP ASP PHE ALA ALA VAL LEU PRO ASN GLY PRO
SEQRES 19 A 484 TYR LEU TRP GLN ASP ASN ASP PHE VAL THR GLY TYR SER
SEQRES 20 A 484 SER PHE PHE GLN PHE CYS ASP ALA VAL GLU GLY VAL GLU
SEQRES 21 A 484 ALA GLY ALA ALA VAL THR PRO GLY PRO GLU GLY VAL GLY
SEQRES 22 A 484 LEU GLU LYS ALA LEU ALA ASN TYR ALA ASN TRP PHE ASN
SEQRES 23 A 484 SER THR ILE LEU PRO ASN TYR CYS ALA SER TYR GLY TYR
SEQRES 24 A 484 TRP THR ASP GLU TRP SER VAL ALA CYS PHE ASP SER TYR
SEQRES 25 A 484 ASN ALA SER SER PRO ILE PHE THR ASP THR SER VAL GLY
SEQRES 26 A 484 ASN PRO VAL ASP ARG GLN TRP GLU TRP PHE LEU CYS ASN
SEQRES 27 A 484 GLU PRO PHE PHE TRP TRP GLN ASP GLY ALA PRO GLU GLY
SEQRES 28 A 484 THR SER THR ILE VAL PRO ARG LEU VAL SER ALA SER TYR
SEQRES 29 A 484 TRP GLN ARG GLN CYS PRO LEU TYR PHE PRO GLU VAL ASN
SEQRES 30 A 484 GLY TYR THR TYR GLY SER ALA LYS GLY LYS ASN SER ALA
SEQRES 31 A 484 THR VAL ASN SER TRP THR GLY GLY TRP ASP MET THR ARG
SEQRES 32 A 484 ASN THR THR ARG LEU ILE TRP THR ASN GLY GLN TYR ASP
SEQRES 33 A 484 PRO TRP ARG ASP SER GLY VAL SER SER THR PHE ARG PRO
SEQRES 34 A 484 GLY GLY PRO LEU VAL SER THR ALA ASN GLU PRO VAL GLN
SEQRES 35 A 484 ILE ILE PRO GLY GLY PHE HIS CYS SER ASP LEU TYR MET
SEQRES 36 A 484 GLU ASP TYR TYR ALA ASN GLU GLY VAL ARG LYS VAL VAL
SEQRES 37 A 484 ASP ASN GLU VAL LYS GLN ILE LYS GLU TRP VAL GLU GLU
SEQRES 38 A 484 TYR TYR ALA
HET NAG C 1 14
HET NAG C 2 14
HET BMA C 3 11
HET MAN C 4 11
HET MAN C 5 11
HET MAN C 6 11
HET NAG D 1 14
HET NAG D 2 14
HET NAG A 601 14
HET NAG A 602 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
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
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
FORMUL 2 NAG 6(C8 H15 N O6)
FORMUL 2 BMA C6 H12 O6
FORMUL 2 MAN 3(C6 H12 O6)
FORMUL 6 HOH *527(H2 O)
HELIX 1 AA1 ASN A 57 LYS A 60 5 4
HELIX 2 AA2 ALA A 91 THR A 99 5 9
HELIX 3 AA3 THR A 102 GLN A 112 1 11
HELIX 4 AA4 GLU A 135 LEU A 140 5 6
HELIX 5 AA5 THR A 141 VAL A 156 1 16
HELIX 6 AA6 SER A 179 ALA A 192 1 14
HELIX 7 AA7 TRP A 213 TYR A 215 5 3
HELIX 8 AA8 PHE A 216 MET A 223 1 8
HELIX 9 AA9 ALA A 224 GLY A 245 1 22
HELIX 10 AB1 THR A 246 PHE A 257 1 12
HELIX 11 AB2 HIS A 264 ALA A 270 1 7
HELIX 12 AB3 PRO A 273 LEU A 278 1 6
HELIX 13 AB4 TRP A 279 ASN A 282 5 4
HELIX 14 AB5 SER A 289 GLU A 299 1 11
HELIX 15 AB6 GLY A 315 ILE A 331 1 17
HELIX 16 AB7 CYS A 336 GLY A 340 5 5
HELIX 17 AB8 VAL A 348 ASP A 352 5 5
HELIX 18 AB9 SER A 358 ASP A 363 1 6
HELIX 19 AC1 ASP A 371 GLU A 381 1 11
HELIX 20 AC2 SER A 403 ARG A 409 1 7
HELIX 21 AC3 GLN A 410 PHE A 415 1 6
HELIX 22 AC4 TYR A 423 GLY A 428 5 6
HELIX 23 AC5 ASN A 430 GLY A 439 1 10
HELIX 24 AC6 GLY A 440 MET A 443 5 4
HELIX 25 AC7 TRP A 460 GLY A 464 5 5
HELIX 26 AC8 TYR A 496 ASN A 503 1 8
HELIX 27 AC9 ASN A 503 ALA A 526 1 24
SHEET 1 AA1 8 THR A 44 LEU A 52 0
SHEET 2 AA1 8 THR A 62 SER A 70 -1 O GLN A 65 N PHE A 49
SHEET 3 AA1 8 ALA A 114 ILE A 118 -1 O LEU A 117 N TRP A 68
SHEET 4 AA1 8 VAL A 81 PHE A 84 1 N VAL A 82 O ALA A 114
SHEET 5 AA1 8 TRP A 173 GLY A 178 1 O VAL A 174 N VAL A 81
SHEET 6 AA1 8 ALA A 198 THR A 202 1 O ALA A 198 N MET A 175
SHEET 7 AA1 8 LEU A 450 GLY A 455 1 O THR A 453 N ALA A 201
SHEET 8 AA1 8 VAL A 483 ILE A 486 1 O ILE A 486 N ASN A 454
SHEET 1 AA2 2 ILE A 209 ASP A 211 0
SHEET 2 AA2 2 PHE A 384 TRP A 386 1 O TRP A 385 N ILE A 209
SSBOND 1 CYS A 227 CYS A 295 1555 1555 2.04
SSBOND 2 CYS A 336 CYS A 350 1555 1555 2.07
SSBOND 3 CYS A 379 CYS A 411 1555 1555 2.05
LINK ND2 ASN A 100 C1 NAG A 601 1555 1555 1.44
LINK ND2 ASN A 226 C1 NAG C 1 1555 1555 1.44
LINK ND2 ASN A 328 C1 NAG D 1 1555 1555 1.46
LINK ND2 ASN A 355 C1 NAG A 602 1555 1555 1.44
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.42
LINK O4 NAG C 2 C1 BMA C 3 1555 1555 1.43
LINK O3 BMA C 3 C1 MAN C 4 1555 1555 1.44
LINK O2 MAN C 4 C1 MAN C 5 1555 1555 1.44
LINK O2 MAN C 5 C1 MAN C 6 1555 1555 1.44
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.43
CISPEP 1 GLU A 381 PRO A 382 0 -7.23
CRYST1 144.517 144.517 56.542 90.00 90.00 90.00 P 4 21 2 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 0.006920 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006920 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017686 0.00000
TER 3859 ALA A 526
MASTER 324 0 10 27 10 0 0 6 4513 1 138 38
END
|
|---|
