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HEADER HYDROLASE 19-MAY-10 3N2Z
TITLE THE STRUCTURE OF HUMAN PROLYLCARBOXYPEPTIDASE AT 2.80 ANGSTROMS
TITLE 2 RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYSOSOMAL PRO-X CARBOXYPEPTIDASE;
COMPND 3 CHAIN: B;
COMPND 4 SYNONYM: PROLYLCARBOXYPEPTIDASE, PRCP, PROLINE CARBOXYPEPTIDASE,
COMPND 5 ANGIOTENSINASE C, LYSOSOMAL CARBOXYPEPTIDASE C;
COMPND 6 EC: 3.4.16.2;
COMPND 7 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: PRCP, PCP;
SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 9 EXPRESSION_SYSTEM_CELL: CHO CELLS
KEYWDS ALPHA/BETA HYDROLASE, PRCP, SERINE CARBOXYPEPTIDASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.M.SOISSON,S.B.PATEL,K.J.LUMB,S.SHARMA
REVDAT 1 07-JUL-10 3N2Z 0
JRNL AUTH S.M.SOISSON,S.B.PATEL,P.D.ABEYWICKREMA,N.J.BRYNE,R.E.DIEHL,
JRNL AUTH 2 D.L.HALL,R.E.FORD,J.C.REID,K.W.RICKERT,J.M.SHIPMAN,S.SHARMA,
JRNL AUTH 3 K.J.LUMB
JRNL TITL STRUCTURAL DEFINITION AND SUBSTRATE SPECIFICITY OF THE S28
JRNL TITL 2 PROTEASE FAMILY: THE CRYSTAL STRUCTURE OF HUMAN
JRNL TITL 3 PROLYLCARBOXYPEPTIDASE.
JRNL REF BMC STRUCT.BIOL. V. 10 16 2010
JRNL REFN ESSN 1472-6807
JRNL PMID 20540760
JRNL DOI 10.1186/1472-6807-10-16
REMARK 2
REMARK 2 RESOLUTION. 2.79 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.9.4
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,
REMARK 3 : MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.79
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.67
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 37540
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.218
REMARK 3 R VALUE (WORKING SET) : 0.216
REMARK 3 FREE R VALUE : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 1875
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 19
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.79
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.87
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.19
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2839
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.3170
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2703
REMARK 3 BIN R VALUE (WORKING SET) : 0.3150
REMARK 3 BIN FREE R VALUE : 0.3520
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.79
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 136
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3539
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 89
REMARK 3 SOLVENT ATOMS : 76
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 64.57
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -16.02700
REMARK 3 B22 (A**2) : -16.02700
REMARK 3 B33 (A**2) : 32.05500
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.43
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.894
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.878
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : NULL ; NULL ; NULL
REMARK 3 BOND ANGLES : NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES : NULL ; NULL ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS : NULL ; NULL ; NULL
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : NULL ; NULL ; NULL
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : NULL ; NULL ; NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : NULL
REMARK 3 OTHER TORSION ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3N2Z COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JUN-10.
REMARK 100 THE RCSB ID CODE IS RCSB059314.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-MAY-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL
REMARK 200 DATA SCALING SOFTWARE : HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37814
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.790
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 10.900
REMARK 200 R MERGE (I) : 0.09800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.79
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.87
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.90
REMARK 200 R MERGE FOR SHELL (I) : 0.59400
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: MIRAS
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8M AMMONIUM SULFATE, 0.1M HEPES, 1-
REMARK 280 2% PEG400 MIXED IN A 2:1 RATIO, PH 7.5, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 90.57000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 52.29061
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 80.04333
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 90.57000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 52.29061
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 80.04333
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 90.57000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 52.29061
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 80.04333
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 90.57000
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 52.29061
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 80.04333
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 90.57000
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 52.29061
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 80.04333
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 90.57000
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 52.29061
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 80.04333
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 104.58123
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 160.08667
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 104.58123
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 160.08667
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 104.58123
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 160.08667
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 104.58123
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 160.08667
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 104.58123
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 160.08667
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 104.58123
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 160.08667
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: 6950 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 104.58123
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 160.08667
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 THR B 349
REMARK 465 ALA B 350
REMARK 465 THR B 351
REMARK 465 SER B 352
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 101 O5 NAG B 1 2.19
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 TYR B 78 -19.27 85.39
REMARK 500 ASN B 92 -163.45 -117.99
REMARK 500 GLU B 93 58.06 -55.62
REMARK 500 TYR B 124 4.99 81.03
REMARK 500 SER B 128 55.91 -96.89
REMARK 500 LYS B 137 -70.17 -51.79
REMARK 500 GLU B 169 -48.96 -22.55
REMARK 500 SER B 179 -111.74 59.48
REMARK 500 TYR B 192 62.44 -117.24
REMARK 500 GLN B 208 49.48 -74.73
REMARK 500 GLU B 210 -127.72 45.25
REMARK 500 VAL B 217 -54.71 -29.81
REMARK 500 PHE B 297 -78.46 -74.88
REMARK 500 LEU B 313 -101.06 -87.04
REMARK 500 LYS B 314 -41.20 50.99
REMARK 500 ASN B 317 72.11 -67.71
REMARK 500 ASN B 336 26.41 -140.94
REMARK 500 THR B 365 -79.54 -109.26
REMARK 500 GLU B 452 10.00 80.77
REMARK 500 ALA B 454 -132.73 -87.98
REMARK 500 HIS B 456 58.56 39.81
REMARK 500 ALA B 464 -40.66 125.65
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 ASP B 76 23.8 L L OUTSIDE RANGE
REMARK 500 GLU B 93 24.5 L L OUTSIDE RANGE
REMARK 500 ASN B 102 24.0 L L OUTSIDE RANGE
REMARK 500 VAL B 217 22.5 L L OUTSIDE RANGE
REMARK 500 ILE B 272 24.6 L L OUTSIDE RANGE
REMARK 500 LYS B 314 23.1 L L OUTSIDE RANGE
REMARK 500 VAL B 333 23.2 L L OUTSIDE RANGE
REMARK 500 TRP B 406 25.0 L L OUTSIDE RANGE
REMARK 500 VAL B 437 24.7 L L OUTSIDE RANGE
REMARK 500 HIS B 456 24.8 L L OUTSIDE RANGE
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 B 495 DISTANCE = 5.92 ANGSTROMS
REMARK 525 HOH B 500 DISTANCE = 6.34 ANGSTROMS
REMARK 525 HOH B 519 DISTANCE = 5.14 ANGSTROMS
REMARK 525 HOH B 521 DISTANCE = 5.08 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 492
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3JYH RELATED DB: PDB
DBREF 3N2Z B 46 491 UNP P42785 PCP_HUMAN 46 491
SEQRES 1 B 446 LYS ASN TYR SER VAL LEU TYR PHE GLN GLN LYS VAL ASP
SEQRES 2 B 446 HIS PHE GLY PHE ASN THR VAL LYS THR PHE ASN GLN ARG
SEQRES 3 B 446 TYR LEU VAL ALA ASP LYS TYR TRP LYS LYS ASN GLY GLY
SEQRES 4 B 446 SER ILE LEU PHE TYR THR GLY ASN GLU GLY ASP ILE ILE
SEQRES 5 B 446 TRP PHE CYS ASN ASN THR GLY PHE MET TRP ASP VAL ALA
SEQRES 6 B 446 GLU GLU LEU LYS ALA MET LEU VAL PHE ALA GLU HIS ARG
SEQRES 7 B 446 TYR TYR GLY GLU SER LEU PRO PHE GLY ASP ASN SER PHE
SEQRES 8 B 446 LYS ASP SER ARG HIS LEU ASN PHE LEU THR SER GLU GLN
SEQRES 9 B 446 ALA LEU ALA ASP PHE ALA GLU LEU ILE LYS HIS LEU LYS
SEQRES 10 B 446 ARG THR ILE PRO GLY ALA GLU ASN GLN PRO VAL ILE ALA
SEQRES 11 B 446 ILE GLY GLY SER TYR GLY GLY MET LEU ALA ALA TRP PHE
SEQRES 12 B 446 ARG MET LYS TYR PRO HIS MET VAL VAL GLY ALA LEU ALA
SEQRES 13 B 446 ALA SER ALA PRO ILE TRP GLN PHE GLU ASP LEU VAL PRO
SEQRES 14 B 446 CYS GLY VAL PHE MET LYS ILE VAL THR THR ASP PHE ARG
SEQRES 15 B 446 LYS SER GLY PRO HIS CYS SER GLU SER ILE HIS ARG SER
SEQRES 16 B 446 TRP ASP ALA ILE ASN ARG LEU SER ASN THR GLY SER GLY
SEQRES 17 B 446 LEU GLN TRP LEU THR GLY ALA LEU HIS LEU CYS SER PRO
SEQRES 18 B 446 LEU THR SER GLN ASP ILE GLN HIS LEU LYS ASP TRP ILE
SEQRES 19 B 446 SER GLU THR TRP VAL ASN LEU ALA MET VAL ASP TYR PRO
SEQRES 20 B 446 TYR ALA SER ASN PHE LEU GLN PRO LEU PRO ALA TRP PRO
SEQRES 21 B 446 ILE LYS VAL VAL CYS GLN TYR LEU LYS ASN PRO ASN VAL
SEQRES 22 B 446 SER ASP SER LEU LEU LEU GLN ASN ILE PHE GLN ALA LEU
SEQRES 23 B 446 ASN VAL TYR TYR ASN TYR SER GLY GLN VAL LYS CYS LEU
SEQRES 24 B 446 ASN ILE SER GLU THR ALA THR SER SER LEU GLY THR LEU
SEQRES 25 B 446 GLY TRP SER TYR GLN ALA CYS THR GLU VAL VAL MET PRO
SEQRES 26 B 446 PHE CYS THR ASN GLY VAL ASP ASP MET PHE GLU PRO HIS
SEQRES 27 B 446 SER TRP ASN LEU LYS GLU LEU SER ASP ASP CYS PHE GLN
SEQRES 28 B 446 GLN TRP GLY VAL ARG PRO ARG PRO SER TRP ILE THR THR
SEQRES 29 B 446 MET TYR GLY GLY LYS ASN ILE SER SER HIS THR ASN ILE
SEQRES 30 B 446 VAL PHE SER ASN GLY GLU LEU ASP PRO TRP SER GLY GLY
SEQRES 31 B 446 GLY VAL THR LYS ASP ILE THR ASP THR LEU VAL ALA VAL
SEQRES 32 B 446 THR ILE SER GLU GLY ALA HIS HIS LEU ASP LEU ARG THR
SEQRES 33 B 446 LYS ASN ALA LEU ASP PRO MET SER VAL LEU LEU ALA ARG
SEQRES 34 B 446 SER LEU GLU VAL ARG HIS MET LYS ASN TRP ILE ARG ASP
SEQRES 35 B 446 PHE TYR ASP SER
MODRES 3N2Z ASN B 336 ASN GLYCOSYLATION SITE
MODRES 3N2Z ASN B 415 ASN GLYCOSYLATION SITE
MODRES 3N2Z ASN B 101 ASN GLYCOSYLATION SITE
MODRES 3N2Z ASN B 345 ASN GLYCOSYLATION SITE
MODRES 3N2Z ASN B 317 ASN GLYCOSYLATION SITE
HET NAG B 1 14
HET NAG B 2 14
HET NAG B 3 14
HET NAG B 4 14
HET NAG B 5 14
HET NAG B 6 14
HET SO4 B 492 5
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM SO4 SULFATE ION
FORMUL 2 NAG 6(C8 H15 N O6)
FORMUL 7 SO4 O4 S 2-
FORMUL 8 HOH *76(H2 O)
HELIX 1 1 ASP B 95 THR B 103 1 9
HELIX 2 2 THR B 103 LYS B 114 1 12
HELIX 3 3 PHE B 131 LYS B 137 5 7
HELIX 4 4 THR B 146 ILE B 165 1 20
HELIX 5 5 GLY B 167 GLN B 171 5 5
HELIX 6 6 SER B 179 TYR B 192 1 14
HELIX 7 7 GLY B 216 LYS B 228 1 13
HELIX 8 8 HIS B 232 SER B 248 1 17
HELIX 9 9 THR B 250 LEU B 261 1 12
HELIX 10 10 ASP B 271 VAL B 289 1 19
HELIX 11 11 TRP B 304 LEU B 313 1 10
HELIX 12 12 SER B 319 TYR B 337 1 19
HELIX 13 13 SER B 353 GLU B 366 1 14
HELIX 14 14 ASN B 386 GLY B 399 1 14
HELIX 15 15 SER B 405 GLY B 412 1 8
HELIX 16 16 ASP B 430 GLY B 436 5 7
HELIX 17 17 HIS B 456 ARG B 460 5 5
HELIX 18 18 PRO B 467 ASP B 490 1 24
SHEET 1 A 8 SER B 49 LYS B 56 0
SHEET 2 A 8 THR B 67 ALA B 75 -1 O TYR B 72 N LEU B 51
SHEET 3 A 8 ALA B 115 ALA B 120 -1 O LEU B 117 N ALA B 75
SHEET 4 A 8 SER B 85 THR B 90 1 N TYR B 89 O VAL B 118
SHEET 5 A 8 VAL B 173 GLY B 178 1 O ILE B 174 N ILE B 86
SHEET 6 A 8 GLY B 198 ALA B 202 1 O LEU B 200 N ALA B 175
SHEET 7 A 8 ILE B 422 GLY B 427 1 O VAL B 423 N ALA B 199
SHEET 8 A 8 LEU B 445 ILE B 450 1 O VAL B 446 N PHE B 424
SHEET 1 B 2 SER B 295 ASN B 296 0
SHEET 2 B 2 PRO B 300 LEU B 301 -1 O LEU B 301 N SER B 295
SSBOND 1 CYS B 215 CYS B 372 1555 1555 2.09
SSBOND 2 CYS B 233 CYS B 310 1555 1555 2.05
SSBOND 3 CYS B 264 CYS B 343 1555 1555 2.06
SSBOND 4 CYS B 364 CYS B 394 1555 1555 2.05
LINK ND2 ASN B 336 C1 NAG B 3 1555 1555 1.42
LINK ND2 ASN B 415 C1 NAG B 6 1555 1555 1.44
LINK ND2 ASN B 101 C1 NAG B 1 1555 1555 1.45
LINK O4 NAG B 3 C1 NAG B 4 1555 1555 1.45
LINK ND2 ASN B 345 C1 NAG B 5 1555 1555 1.49
LINK ND2 ASN B 317 C1 NAG B 2 1555 1555 1.49
SITE 1 AC1 3 HOH B 21 ASN B 101 HOH B 517
SITE 1 AC2 3 ASN B 315 PRO B 316 ASN B 317
SITE 1 AC3 8 NAG B 4 HIS B 262 PHE B 328 ASN B 332
SITE 2 AC3 8 ASN B 336 GLY B 339 VAL B 341 LYS B 342
SITE 1 AC4 1 NAG B 3
SITE 1 AC5 3 ASN B 345 SER B 347 HOH B 520
SITE 1 AC6 4 HOH B 9 LYS B 162 ASN B 170 ASN B 415
SITE 1 AC7 4 LYS B 56 ARG B 403 PRO B 404 SER B 405
CRYST1 181.140 181.140 240.130 90.00 90.00 120.00 H 3 2 18
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 0.005521 0.003187 0.000000 0.00000
SCALE2 0.000000 0.006375 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004164 0.00000
TER 3540 SER B 491
MASTER 411 0 7 18 10 0 8 6 3704 1 102 35
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