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HEADER HYDROLASE 14-OCT-22 8BBX
TITLE STRUCTURE OF PROLYL ENDOPROTEASE FROM ASPERGILLUS NIGER CBS 109712 IN
TITLE 2 SPACE GROUP C222(1)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDOPROTEASE ENDO-PRO;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ASPERGILLUS NIGER;
SOURCE 3 ORGANISM_TAXID: 5061;
SOURCE 4 GENE: ATWU_08740;
SOURCE 5 EXPRESSION_SYSTEM: ASPERGILLUS NIGER;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 5061;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: CBS 109712
KEYWDS ENDOPROTEASE, PROLINE-SPECIFIC, S28 PEPTIDASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.PIJNING,A.VUJICIC-ZAGAR,J.M.VAN DER LAAN,R.M.DE JONG,B.W.DIJKSTRA
REVDAT 1 20-DEC-23 8BBX 0
JRNL AUTH T.PIJNING,A.VUJICIC-ZAGAR,J.M.V.D.LAAN,R.M.D.JONG,
JRNL AUTH 2 C.RAMIREZ-PALACIOS,A.VENTE,L.EDENS,B.W.DIJKSTRA
JRNL TITL STRUCTURAL AND TIME-RESOLVED MECHANISTIC INVESTIGATIONS OF
JRNL TITL 2 PROTEIN HYDROLYSIS BY THE ACIDIC PROLINE-SPECIFIC
JRNL TITL 3 ENDOPROTEASE FROM ASPERGILLUS NIGER
JRNL REF PROTEIN SCI. 2023
JRNL REFN ESSN 1469-896X
JRNL DOI 10.1002/PRO.4856
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.17.1_3660
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.39
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 42704
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 2144
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 49.3900 - 6.6500 1.00 2868 138 0.1856 0.2297
REMARK 3 2 6.6500 - 5.2800 1.00 2763 158 0.1712 0.1899
REMARK 3 3 5.2800 - 4.6200 1.00 2727 142 0.1525 0.2211
REMARK 3 4 4.6200 - 4.1900 1.00 2715 151 0.1513 0.1874
REMARK 3 5 4.1900 - 3.8900 1.00 2684 154 0.1790 0.2442
REMARK 3 6 3.8900 - 3.6600 1.00 2731 136 0.1928 0.2588
REMARK 3 7 3.6600 - 3.4800 1.00 2710 125 0.2098 0.2786
REMARK 3 8 3.4800 - 3.3300 1.00 2691 152 0.2272 0.2791
REMARK 3 9 3.3300 - 3.2000 1.00 2685 145 0.2491 0.3099
REMARK 3 10 3.2000 - 3.0900 1.00 2689 130 0.2517 0.2671
REMARK 3 11 3.0900 - 2.9900 1.00 2682 141 0.2491 0.3416
REMARK 3 12 2.9900 - 2.9100 1.00 2655 150 0.2597 0.3103
REMARK 3 13 2.9100 - 2.8300 0.99 2665 123 0.2700 0.3598
REMARK 3 14 2.8300 - 2.7600 0.99 2648 161 0.3143 0.3520
REMARK 3 15 2.7600 - 2.7000 0.99 2647 138 0.3442 0.3996
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) : 0.442
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.464
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 49.49
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.82
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 : 0.010 8362
REMARK 3 ANGLE : 1.163 11447
REMARK 3 CHIRALITY : 0.059 1268
REMARK 3 PLANARITY : 0.008 1435
REMARK 3 DIHEDRAL : 9.916 1325
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 : 3
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'A'
REMARK 3 SELECTION : (CHAIN 'B' AND RESID 43 THROUGH 525)
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'C'
REMARK 3 SELECTION : CHAIN 'E'
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN 'C'
REMARK 3 SELECTION : CHAIN 'F'
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN 'C'
REMARK 3 SELECTION : CHAIN 'G'
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 4
REMARK 3 REFERENCE SELECTION: CHAIN 'C'
REMARK 3 SELECTION : CHAIN 'H'
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 5
REMARK 3 REFERENCE SELECTION: CHAIN 'C'
REMARK 3 SELECTION : CHAIN 'I'
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 6
REMARK 3 REFERENCE SELECTION: CHAIN 'C'
REMARK 3 SELECTION : CHAIN 'K'
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 3
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: (CHAIN 'D' AND (RESID 2 OR RESID 5
REMARK 3 THROUGH 10))
REMARK 3 SELECTION : (CHAIN 'J' AND (RESID 1 OR RESID 4
REMARK 3 THROUGH 9))
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 8BBX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-OCT-22.
REMARK 100 THE DEPOSITION ID IS D_1292125952.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-NOV-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8726
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 : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42923
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.690
REMARK 200 RESOLUTION RANGE LOW (A) : 49.390
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 4.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.69
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.79
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.400
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: 8B57
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.56
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 28-32% (W/V) PEG 3000, 0.1 M SODIUM
REMARK 280 CITRATE BUFFER PH 5.25, PH 6.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 96.70000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 96.70000
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 51.08500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 78.10300
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 51.08500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 78.10300
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 96.70000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 51.08500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 78.10300
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 96.70000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 51.08500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 78.10300
REMARK 290 SMTRY3 8 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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, D, 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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, G, H, I, J, K
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 ALA A 42
REMARK 465 ALA A 526
REMARK 465 ALA B 526
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 ND2 ASN B 446 O5 NAG I 1 2.17
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 GLU A 59 CA - CB - CG ANGL. DEV. = -14.7 DEGREES
REMARK 500 GLU A 101 CA - CB - CG ANGL. DEV. = -24.1 DEGREES
REMARK 500 ARG B 121 NE - CZ - NH1 ANGL. DEV. = 3.4 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 PRO A 58 -9.80 -59.61
REMARK 500 GLU A 88 39.77 -72.37
REMARK 500 THR A 155 -18.22 -141.96
REMARK 500 ASP A 161 87.82 -168.20
REMARK 500 SER A 179 -131.51 55.10
REMARK 500 THR A 195 -60.82 -100.74
REMARK 500 TYR A 212 58.66 -95.54
REMARK 500 ASP A 266 -65.72 -22.51
REMARK 500 ASP A 283 156.57 176.94
REMARK 500 VAL A 348 18.35 -142.01
REMARK 500 PHE A 384 -80.35 62.47
REMARK 500 PRO A 391 -177.82 -64.37
REMARK 500 VAL A 402 92.78 -68.40
REMARK 500 LEU A 475 131.64 -39.76
REMARK 500 PHE A 490 -148.72 -110.60
REMARK 500 CYS A 492 54.78 30.90
REMARK 500 GLU B 88 38.11 -72.29
REMARK 500 ASP B 161 86.99 -168.69
REMARK 500 SER B 179 -129.20 51.08
REMARK 500 TYR B 212 59.57 -94.48
REMARK 500 ASP B 266 -68.00 -19.88
REMARK 500 ASP B 283 158.53 179.03
REMARK 500 VAL B 348 20.57 -140.81
REMARK 500 PHE B 384 -82.44 62.35
REMARK 500 VAL B 402 90.44 -64.32
REMARK 500 PHE B 490 -149.09 -105.90
REMARK 500 CYS B 492 54.79 35.59
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 8B57 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN CRYSTALLIZED IN A DIFFERENT SPACE GROUP
DBREF1 8BBX A 42 526 UNP A0A8H3Y1T9_ASPTU
DBREF2 8BBX A A0A8H3Y1T9 42 526
DBREF1 8BBX B 42 526 UNP A0A8H3Y1T9_ASPTU
DBREF2 8BBX B A0A8H3Y1T9 42 526
SEQRES 1 A 485 ALA THR THR GLY GLU ALA TYR PHE GLU GLN LEU LEU ASP
SEQRES 2 A 485 HIS HIS ASN PRO GLU LYS GLY THR PHE SER GLN ARG TYR
SEQRES 3 A 485 TRP TRP SER THR GLU TYR TRP GLY GLY PRO GLY SER PRO
SEQRES 4 A 485 VAL VAL LEU PHE THR PRO GLY GLU VAL SER ALA ASP GLY
SEQRES 5 A 485 TYR GLU GLY TYR LEU THR ASN GLU THR LEU THR GLY VAL
SEQRES 6 A 485 TYR ALA GLN GLU ILE GLN GLY ALA VAL ILE LEU ILE GLU
SEQRES 7 A 485 HIS ARG TYR TRP GLY ASP SER SER PRO TYR GLU VAL LEU
SEQRES 8 A 485 ASN ALA GLU THR LEU GLN TYR LEU THR LEU ASP GLN ALA
SEQRES 9 A 485 ILE LEU ASP MET THR TYR PHE ALA GLU THR VAL LYS LEU
SEQRES 10 A 485 GLN PHE ASP ASN SER THR ARG SER ASN ALA GLN ASN ALA
SEQRES 11 A 485 PRO TRP VAL MET VAL GLY GLY SER TYR SER GLY ALA LEU
SEQRES 12 A 485 THR ALA TRP THR GLU SER VAL ALA PRO GLY THR PHE TRP
SEQRES 13 A 485 ALA TYR HIS ALA THR SER ALA PRO VAL GLU ALA ILE TYR
SEQRES 14 A 485 ASP TYR TRP GLN TYR PHE TYR PRO ILE GLN GLN GLY MET
SEQRES 15 A 485 ALA GLN ASN CYS SER LYS ASP VAL SER LEU VAL ALA GLU
SEQRES 16 A 485 TYR VAL ASP LYS ILE GLY LYS ASN GLY THR ALA LYS GLU
SEQRES 17 A 485 GLN GLN ALA LEU LYS GLU LEU PHE GLY LEU GLY ALA VAL
SEQRES 18 A 485 GLU HIS PHE ASP ASP PHE ALA ALA VAL LEU PRO ASN GLY
SEQRES 19 A 485 PRO TYR LEU TRP GLN ASP ASN ASP PHE ALA THR GLY TYR
SEQRES 20 A 485 SER SER PHE PHE GLN PHE CYS ASP ALA VAL GLU GLY VAL
SEQRES 21 A 485 GLU ALA GLY ALA ALA VAL THR PRO GLY PRO GLU GLY VAL
SEQRES 22 A 485 GLY LEU GLU LYS ALA LEU ALA ASN TYR ALA ASN TRP PHE
SEQRES 23 A 485 ASN SER THR ILE LEU PRO ASP TYR CYS ALA SER TYR GLY
SEQRES 24 A 485 TYR TRP THR ASP GLU TRP SER VAL ALA CYS PHE ASP SER
SEQRES 25 A 485 TYR ASN ALA SER SER PRO ILE TYR THR ASP THR SER VAL
SEQRES 26 A 485 GLY ASN ALA VAL ASP ARG GLN TRP GLU TRP PHE LEU CYS
SEQRES 27 A 485 ASN GLU PRO PHE PHE TYR TRP GLN ASP GLY ALA PRO GLU
SEQRES 28 A 485 GLY THR SER THR ILE VAL PRO ARG LEU VAL SER ALA SER
SEQRES 29 A 485 TYR TRP GLN ARG GLN CYS PRO LEU TYR PHE PRO GLU THR
SEQRES 30 A 485 ASN GLY TYR THR TYR GLY SER ALA LYS GLY LYS ASN ALA
SEQRES 31 A 485 ALA THR VAL ASN SER TRP THR GLY GLY TRP ASP MET THR
SEQRES 32 A 485 ARG ASN THR THR ARG LEU ILE TRP THR ASN GLY GLN TYR
SEQRES 33 A 485 ASP PRO TRP ARG ASP SER GLY VAL SER SER THR PHE ARG
SEQRES 34 A 485 PRO GLY GLY PRO LEU ALA SER THR ALA ASN GLU PRO VAL
SEQRES 35 A 485 GLN ILE ILE PRO GLY GLY PHE HIS CYS SER ASP LEU TYR
SEQRES 36 A 485 MET ALA ASP TYR TYR ALA ASN GLU GLY VAL LYS LYS VAL
SEQRES 37 A 485 VAL ASP ASN GLU VAL LYS GLN ILE LYS GLU TRP VAL GLU
SEQRES 38 A 485 GLU TYR TYR ALA
SEQRES 1 B 485 ALA THR THR GLY GLU ALA TYR PHE GLU GLN LEU LEU ASP
SEQRES 2 B 485 HIS HIS ASN PRO GLU LYS GLY THR PHE SER GLN ARG TYR
SEQRES 3 B 485 TRP TRP SER THR GLU TYR TRP GLY GLY PRO GLY SER PRO
SEQRES 4 B 485 VAL VAL LEU PHE THR PRO GLY GLU VAL SER ALA ASP GLY
SEQRES 5 B 485 TYR GLU GLY TYR LEU THR ASN GLU THR LEU THR GLY VAL
SEQRES 6 B 485 TYR ALA GLN GLU ILE GLN GLY ALA VAL ILE LEU ILE GLU
SEQRES 7 B 485 HIS ARG TYR TRP GLY ASP SER SER PRO TYR GLU VAL LEU
SEQRES 8 B 485 ASN ALA GLU THR LEU GLN TYR LEU THR LEU ASP GLN ALA
SEQRES 9 B 485 ILE LEU ASP MET THR TYR PHE ALA GLU THR VAL LYS LEU
SEQRES 10 B 485 GLN PHE ASP ASN SER THR ARG SER ASN ALA GLN ASN ALA
SEQRES 11 B 485 PRO TRP VAL MET VAL GLY GLY SER TYR SER GLY ALA LEU
SEQRES 12 B 485 THR ALA TRP THR GLU SER VAL ALA PRO GLY THR PHE TRP
SEQRES 13 B 485 ALA TYR HIS ALA THR SER ALA PRO VAL GLU ALA ILE TYR
SEQRES 14 B 485 ASP TYR TRP GLN TYR PHE TYR PRO ILE GLN GLN GLY MET
SEQRES 15 B 485 ALA GLN ASN CYS SER LYS ASP VAL SER LEU VAL ALA GLU
SEQRES 16 B 485 TYR VAL ASP LYS ILE GLY LYS ASN GLY THR ALA LYS GLU
SEQRES 17 B 485 GLN GLN ALA LEU LYS GLU LEU PHE GLY LEU GLY ALA VAL
SEQRES 18 B 485 GLU HIS PHE ASP ASP PHE ALA ALA VAL LEU PRO ASN GLY
SEQRES 19 B 485 PRO TYR LEU TRP GLN ASP ASN ASP PHE ALA THR GLY TYR
SEQRES 20 B 485 SER SER PHE PHE GLN PHE CYS ASP ALA VAL GLU GLY VAL
SEQRES 21 B 485 GLU ALA GLY ALA ALA VAL THR PRO GLY PRO GLU GLY VAL
SEQRES 22 B 485 GLY LEU GLU LYS ALA LEU ALA ASN TYR ALA ASN TRP PHE
SEQRES 23 B 485 ASN SER THR ILE LEU PRO ASP TYR CYS ALA SER TYR GLY
SEQRES 24 B 485 TYR TRP THR ASP GLU TRP SER VAL ALA CYS PHE ASP SER
SEQRES 25 B 485 TYR ASN ALA SER SER PRO ILE TYR THR ASP THR SER VAL
SEQRES 26 B 485 GLY ASN ALA VAL ASP ARG GLN TRP GLU TRP PHE LEU CYS
SEQRES 27 B 485 ASN GLU PRO PHE PHE TYR TRP GLN ASP GLY ALA PRO GLU
SEQRES 28 B 485 GLY THR SER THR ILE VAL PRO ARG LEU VAL SER ALA SER
SEQRES 29 B 485 TYR TRP GLN ARG GLN CYS PRO LEU TYR PHE PRO GLU THR
SEQRES 30 B 485 ASN GLY TYR THR TYR GLY SER ALA LYS GLY LYS ASN ALA
SEQRES 31 B 485 ALA THR VAL ASN SER TRP THR GLY GLY TRP ASP MET THR
SEQRES 32 B 485 ARG ASN THR THR ARG LEU ILE TRP THR ASN GLY GLN TYR
SEQRES 33 B 485 ASP PRO TRP ARG ASP SER GLY VAL SER SER THR PHE ARG
SEQRES 34 B 485 PRO GLY GLY PRO LEU ALA SER THR ALA ASN GLU PRO VAL
SEQRES 35 B 485 GLN ILE ILE PRO GLY GLY PHE HIS CYS SER ASP LEU TYR
SEQRES 36 B 485 MET ALA ASP TYR TYR ALA ASN GLU GLY VAL LYS LYS VAL
SEQRES 37 B 485 VAL ASP ASN GLU VAL LYS GLN ILE LYS GLU TRP VAL GLU
SEQRES 38 B 485 GLU TYR TYR ALA
HET NAG C 1 14
HET NAG C 2 14
HET NAG D 1 14
HET NAG D 2 14
HET BMA D 3 11
HET MAN D 4 11
HET MAN D 5 11
HET MAN D 6 11
HET MAN D 7 11
HET MAN D 8 11
HET MAN D 9 11
HET MAN D 10 11
HET NAG E 1 14
HET NAG E 2 14
HET NAG F 1 14
HET NAG F 2 14
HET NAG G 1 14
HET NAG G 2 14
HET NAG H 1 14
HET NAG H 2 14
HET NAG I 1 14
HET NAG I 2 14
HET NAG J 1 14
HET NAG J 2 14
HET BMA J 3 11
HET MAN J 4 11
HET MAN J 5 11
HET MAN J 6 11
HET MAN J 7 11
HET MAN J 8 11
HET MAN J 9 11
HET NAG K 1 14
HET NAG K 2 14
HET PG4 B 601 13
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM PG4 TETRAETHYLENE GLYCOL
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 3 NAG 18(C8 H15 N O6)
FORMUL 4 BMA 2(C6 H12 O6)
FORMUL 4 MAN 13(C6 H12 O6)
FORMUL 12 PG4 C8 H18 O5
FORMUL 13 HOH *16(H2 O)
HELIX 1 AA1 TYR A 94 THR A 99 5 6
HELIX 2 AA2 THR A 102 GLN A 112 1 11
HELIX 3 AA3 GLU A 135 LEU A 140 5 6
HELIX 4 AA4 THR A 141 VAL A 156 1 16
HELIX 5 AA5 SER A 163 ASN A 167 5 5
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 TYR A 335 GLY A 340 5 6
HELIX 17 AB8 SER A 358 ASP A 363 1 6
HELIX 18 AB9 ASP A 371 GLU A 381 1 11
HELIX 19 AC1 SER A 403 ARG A 409 1 7
HELIX 20 AC2 GLN A 410 PHE A 415 1 6
HELIX 21 AC3 TYR A 423 LYS A 427 5 5
HELIX 22 AC4 ASN A 430 GLY A 439 1 10
HELIX 23 AC5 GLY A 440 ASN A 446 5 7
HELIX 24 AC6 TRP A 460 GLY A 464 5 5
HELIX 25 AC7 TYR A 496 ASN A 503 1 8
HELIX 26 AC8 ASN A 503 GLU A 523 1 21
HELIX 27 AC9 ASN B 57 LYS B 60 5 4
HELIX 28 AD1 TYR B 94 THR B 99 5 6
HELIX 29 AD2 THR B 102 GLN B 112 1 11
HELIX 30 AD3 GLU B 135 LEU B 140 5 6
HELIX 31 AD4 THR B 141 VAL B 156 1 16
HELIX 32 AD5 SER B 179 ALA B 192 1 14
HELIX 33 AD6 TRP B 213 TYR B 215 5 3
HELIX 34 AD7 PHE B 216 MET B 223 1 8
HELIX 35 AD8 ALA B 224 ASN B 244 1 21
HELIX 36 AD9 THR B 246 LEU B 256 1 11
HELIX 37 AE1 HIS B 264 ALA B 270 1 7
HELIX 38 AE2 PRO B 273 LEU B 278 1 6
HELIX 39 AE3 TRP B 279 ASN B 282 5 4
HELIX 40 AE4 SER B 289 GLU B 299 1 11
HELIX 41 AE5 GLY B 315 ILE B 331 1 17
HELIX 42 AE6 TYR B 335 GLY B 340 5 6
HELIX 43 AE7 SER B 358 ASP B 363 1 6
HELIX 44 AE8 ASP B 371 GLU B 381 1 11
HELIX 45 AE9 SER B 403 ARG B 409 1 7
HELIX 46 AF1 GLN B 410 PHE B 415 1 6
HELIX 47 AF2 TYR B 423 LYS B 427 5 5
HELIX 48 AF3 ASN B 430 GLY B 439 1 10
HELIX 49 AF4 GLY B 440 ASN B 446 5 7
HELIX 50 AF5 TRP B 460 GLY B 464 5 5
HELIX 51 AF6 TYR B 496 ASN B 503 1 8
HELIX 52 AF7 ASN B 503 GLU B 523 1 21
SHEET 1 AA1 8 THR A 44 LEU A 52 0
SHEET 2 AA1 8 THR A 62 SER A 70 -1 O TYR A 67 N ALA A 47
SHEET 3 AA1 8 ALA A 114 ILE A 118 -1 O VAL A 115 N SER A 70
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 HIS A 200 N MET A 175
SHEET 7 AA1 8 LEU A 450 GLY A 455 1 O ILE A 451 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 TYR A 385 N ILE A 209
SHEET 1 AA3 8 THR B 44 LEU B 52 0
SHEET 2 AA3 8 THR B 62 SER B 70 -1 O GLN B 65 N PHE B 49
SHEET 3 AA3 8 ALA B 114 ILE B 118 -1 O LEU B 117 N TRP B 68
SHEET 4 AA3 8 VAL B 81 PHE B 84 1 N VAL B 82 O ALA B 114
SHEET 5 AA3 8 TRP B 173 GLY B 178 1 O VAL B 174 N VAL B 81
SHEET 6 AA3 8 ALA B 198 THR B 202 1 O HIS B 200 N MET B 175
SHEET 7 AA3 8 LEU B 450 GLY B 455 1 O ILE B 451 N TYR B 199
SHEET 8 AA3 8 VAL B 483 ILE B 486 1 O ILE B 486 N ASN B 454
SHEET 1 AA4 2 ILE B 209 ASP B 211 0
SHEET 2 AA4 2 PHE B 384 TRP B 386 1 O TYR B 385 N ILE B 209
SSBOND 1 CYS A 227 CYS A 295 1555 1555 2.09
SSBOND 2 CYS A 336 CYS A 350 1555 1555 2.08
SSBOND 3 CYS A 379 CYS A 411 1555 1555 2.06
SSBOND 4 CYS B 227 CYS B 295 1555 1555 2.02
SSBOND 5 CYS B 336 CYS B 350 1555 1555 2.07
SSBOND 6 CYS B 379 CYS B 411 1555 1555 2.07
LINK ND2 ASN A 100 C1 NAG C 1 1555 1555 1.46
LINK ND2 ASN A 226 C1 NAG D 1 1555 1555 1.46
LINK ND2 ASN A 355 C1 NAG E 1 1555 1555 1.45
LINK ND2 ASN A 446 C1 NAG F 1 1555 1555 1.44
LINK ND2 ASN B 100 C1 NAG G 1 1555 1555 1.45
LINK ND2 ASN B 226 C1 NAG J 1 1555 1555 1.44
LINK ND2 ASN B 328 C1 NAG K 1 1555 1555 1.45
LINK ND2 ASN B 355 C1 NAG H 1 1555 1555 1.45
LINK ND2 ASN B 446 C1 NAG I 1 1555 1555 1.44
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.45
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.43
LINK O4 NAG D 2 C1 BMA D 3 1555 1555 1.43
LINK O3 BMA D 3 C1 MAN D 4 1555 1555 1.43
LINK O6 BMA D 3 C1 MAN D 7 1555 1555 1.44
LINK O2 MAN D 4 C1 MAN D 5 1555 1555 1.45
LINK O2 MAN D 5 C1 MAN D 6 1555 1555 1.44
LINK O3 MAN D 7 C1 MAN D 8 1555 1555 1.45
LINK O6 MAN D 7 C1 MAN D 10 1555 1555 1.44
LINK O3 MAN D 8 C1 MAN D 9 1555 1555 1.45
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.45
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.48
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.45
LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.45
LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.45
LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.43
LINK O4 NAG J 2 C1 BMA J 3 1555 1555 1.44
LINK O3 BMA J 3 C1 MAN J 4 1555 1555 1.45
LINK O6 BMA J 3 C1 MAN J 7 1555 1555 1.45
LINK O2 MAN J 4 C1 MAN J 5 1555 1555 1.44
LINK O2 MAN J 5 C1 MAN J 6 1555 1555 1.44
LINK O3 MAN J 7 C1 MAN J 8 1555 1555 1.44
LINK O6 MAN J 7 C1 MAN J 9 1555 1555 1.45
LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.45
CISPEP 1 GLU A 381 PRO A 382 0 -7.21
CISPEP 2 GLU B 381 PRO B 382 0 -8.49
CRYST1 102.170 156.206 193.400 90.00 90.00 90.00 C 2 2 21 16
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 0.009788 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006402 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005171 0.00000
TER 3835 TYR A 525
TER 7675 TYR B 525
MASTER 359 0 34 52 20 0 0 6 8119 2 451 76
END |