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HEADER HYDROLASE 05-NOV-10 3PIC
TITLE GLUCURONOYL ESTERASE CATALYTIC DOMAIN (CIP2_GE) FROM HYPOCREA JECORINA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CIP2;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN (UNP RESIDUES 90-460)
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HYPOCREA JECORINA;
SOURCE 3 ORGANISM_COMMON: TRICHODERMA REESEI;
SOURCE 4 ORGANISM_TAXID: 51453
KEYWDS ALPHA/BETA HYDROLASE FOLD, GLUCURONOYL ESTERASE, CARBOHYDRATE
KEYWDS 2 ESTERASE FAMILY 15 (CE-15), N-LINKED GLYCOSYLATION, SECRETED,
KEYWDS 3 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.R.POKKULURI
REVDAT 3 20-JUL-11 3PIC 1 JRNL
REVDAT 2 22-JUN-11 3PIC 1 JRNL
REVDAT 1 01-JUN-11 3PIC 0
JRNL AUTH P.R.POKKULURI,N.E.DUKE,S.J.WOOD,M.A.COTTA,X.L.LI,P.BIELY,
JRNL AUTH 2 M.SCHIFFER
JRNL TITL STRUCTURE OF THE CATALYTIC DOMAIN OF GLUCURONOYL ESTERASE
JRNL TITL 2 CIP2 FROM HYPOCREA JECORINA.
JRNL REF PROTEINS V. 79 2588 2011
JRNL REFN ISSN 0887-3585
JRNL PMID 21661060
JRNL DOI 10.1002/PROT.23088
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.20
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 58390.550
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 90.1
REMARK 3 NUMBER OF REFLECTIONS : 87710
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 SET) : 0.195
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 8748
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.02
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 12321
REMARK 3 BIN R VALUE (WORKING SET) : 0.2470
REMARK 3 BIN FREE R VALUE : 0.2920
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 1340
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.008
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8066
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 42
REMARK 3 SOLVENT ATOMS : 1113
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 9.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.67000
REMARK 3 B22 (A**2) : -3.51000
REMARK 3 B33 (A**2) : 1.85000
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) : 0.21
REMARK 3 ESD FROM SIGMAA (A) : 0.17
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.26
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.22
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.20
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.76
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.040 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.470 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.690 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.180 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 36.62
REMARK 3
REMARK 3 NCS MODEL : NONE
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : CARB.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 3PIC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-NOV-10.
REMARK 100 THE RCSB ID CODE IS RCSB062406.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-JUN-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.9
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) : 0.91946
REMARK 200 MONOCHROMATOR : MONOCHROMATIC
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : CUSTOM-MADE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 91361
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.0
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.08500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.30500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: HKL-3000
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: QUIK SCREEN C4 (1.4 M SODIUM/POTASSIUM
REMARK 280 PHOSPHATE, PH 6.9), VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 40.13000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 92.94500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.00500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 92.94500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 40.13000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.00500
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, 3
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 300 REMARK: MONOMER
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 GLN A 86
REMARK 465 GLN A 87
REMARK 465 THR A 88
REMARK 465 SER A 89
REMARK 465 GLY A 90
REMARK 465 ALA A 91
REMARK 465 GLY A 92
REMARK 465 GLY A 93
REMARK 465 ALA A 94
REMARK 465 THR A 95
REMARK 465 CYS A 96
REMARK 465 SER A 97
REMARK 465 ALA A 98
REMARK 465 GLN B 86
REMARK 465 GLN B 87
REMARK 465 THR B 88
REMARK 465 SER B 89
REMARK 465 GLY B 90
REMARK 465 ALA B 91
REMARK 465 GLY B 92
REMARK 465 GLY B 93
REMARK 465 ALA B 94
REMARK 465 GLN C 86
REMARK 465 GLN C 87
REMARK 465 THR C 88
REMARK 465 SER C 89
REMARK 465 GLY C 90
REMARK 465 ALA C 91
REMARK 465 GLY C 92
REMARK 465 GLY C 93
REMARK 465 ALA C 94
REMARK 465 THR C 95
REMARK 465 CYS C 96
REMARK 465 SER C 97
REMARK 465 ALA C 98
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 SER A 102 OG
REMARK 470 LYS A 122 CG CD CE NZ
REMARK 470 LYS A 173 CG CD CE NZ
REMARK 470 LYS A 292 CG CD CE NZ
REMARK 470 LYS A 317 CG CD CE NZ
REMARK 470 GLN A 393 CG CD OE1 NE2
REMARK 470 SER A 460 OG
REMARK 470 THR B 95 OG1 CG2
REMARK 470 LYS B 173 CG CD CE NZ
REMARK 470 THR B 188 OG1 CG2
REMARK 470 ARG C 106 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 126 CG CD CE NZ
REMARK 470 ASP C 127 CG OD1 OD2
REMARK 470 LYS C 128 CG CD CE NZ
REMARK 470 THR C 156 OG1 CG2
REMARK 470 LYS C 173 CG CD CE NZ
REMARK 470 SER C 174 OG
REMARK 470 ILE C 181 CG1 CG2 CD1
REMARK 470 VAL C 208 CG1 CG2
REMARK 470 ASN C 212 CG OD1
REMARK 470 LEU C 261 CG CD1 CD2
REMARK 470 ARG C 266 CZ NH1 NH2
REMARK 470 LYS C 271 CG CD CE NZ
REMARK 470 LYS C 292 CG CD CE NZ
REMARK 470 ASP C 399 CG OD1 OD2
REMARK 470 HIS C 400 CG ND1 CD2 CE1 NE2
REMARK 470 LEU C 431 CG CD1 CD2
REMARK 470 GLN C 433 CG CD OE1 NE2
REMARK 470 SER C 434 OG
REMARK 470 GLN C 441 CG CD OE1 NE2
REMARK 470 GLN C 448 CG CD OE1 NE2
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 144 -51.75 -121.93
REMARK 500 GLN A 221 46.03 -143.76
REMARK 500 SER A 278 -126.53 57.24
REMARK 500 PRO A 334 42.68 -83.96
REMARK 500 GLN A 346 45.46 -151.91
REMARK 500 PRO A 351 30.09 -77.68
REMARK 500 SER B 278 -127.57 58.21
REMARK 500 PRO B 334 41.67 -81.69
REMARK 500 GLN B 346 41.11 -142.33
REMARK 500 PRO B 351 27.01 -75.09
REMARK 500 PHE B 440 100.41 -162.92
REMARK 500 GLU C 144 -52.82 -120.36
REMARK 500 GLN C 221 53.28 -144.75
REMARK 500 SER C 278 -121.27 57.06
REMARK 500 PRO C 334 41.86 -81.07
REMARK 500 GLN C 346 49.77 -143.64
REMARK 500 PRO C 351 26.79 -78.07
REMARK 500 SER C 434 75.02 -110.35
REMARK 500 PHE C 440 81.11 -166.77
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 A 724 DISTANCE = 5.10 ANGSTROMS
REMARK 525 HOH A 728 DISTANCE = 6.25 ANGSTROMS
REMARK 525 HOH A 923 DISTANCE = 5.04 ANGSTROMS
REMARK 525 HOH B 693 DISTANCE = 5.05 ANGSTROMS
REMARK 525 HOH B 973 DISTANCE = 5.36 ANGSTROMS
REMARK 525 HOH B1017 DISTANCE = 6.98 ANGSTROMS
REMARK 525 HOH B1023 DISTANCE = 5.02 ANGSTROMS
REMARK 525 HOH B1100 DISTANCE = 5.26 ANGSTROMS
REMARK 525 HOH B1108 DISTANCE = 6.59 ANGSTROMS
REMARK 525 HOH B1112 DISTANCE = 5.33 ANGSTROMS
REMARK 525 HOH C 717 DISTANCE = 5.06 ANGSTROMS
REMARK 525 HOH C 725 DISTANCE = 7.39 ANGSTROMS
REMARK 525 HOH C 726 DISTANCE = 6.58 ANGSTROMS
REMARK 525 HOH C 729 DISTANCE = 5.30 ANGSTROMS
REMARK 525 HOH C 865 DISTANCE = 6.31 ANGSTROMS
REMARK 525 HOH C 968 DISTANCE = 5.22 ANGSTROMS
REMARK 525 HOH C1101 DISTANCE = 5.66 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 NAG A 500
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 500
DBREF 3PIC A 90 460 UNP Q7Z9N1 Q7Z9N1_TRIRE 90 460
DBREF 3PIC B 90 460 UNP Q7Z9N1 Q7Z9N1_TRIRE 90 460
DBREF 3PIC C 90 460 UNP Q7Z9N1 Q7Z9N1_TRIRE 90 460
SEQADV 3PIC GLN A 86 UNP Q7Z9N1 CLONING ARTIFACT
SEQADV 3PIC GLN A 87 UNP Q7Z9N1 CLONING ARTIFACT
SEQADV 3PIC THR A 88 UNP Q7Z9N1 CLONING ARTIFACT
SEQADV 3PIC SER A 89 UNP Q7Z9N1 CLONING ARTIFACT
SEQADV 3PIC GLN B 86 UNP Q7Z9N1 CLONING ARTIFACT
SEQADV 3PIC GLN B 87 UNP Q7Z9N1 CLONING ARTIFACT
SEQADV 3PIC THR B 88 UNP Q7Z9N1 CLONING ARTIFACT
SEQADV 3PIC SER B 89 UNP Q7Z9N1 CLONING ARTIFACT
SEQADV 3PIC GLN C 86 UNP Q7Z9N1 CLONING ARTIFACT
SEQADV 3PIC GLN C 87 UNP Q7Z9N1 CLONING ARTIFACT
SEQADV 3PIC THR C 88 UNP Q7Z9N1 CLONING ARTIFACT
SEQADV 3PIC SER C 89 UNP Q7Z9N1 CLONING ARTIFACT
SEQRES 1 A 375 GLN GLN THR SER GLY ALA GLY GLY ALA THR CYS SER ALA
SEQRES 2 A 375 LEU PRO GLY SER ILE THR LEU ARG SER ASN ALA LYS LEU
SEQRES 3 A 375 ASN ASP LEU PHE THR MET PHE ASN GLY ASP LYS VAL THR
SEQRES 4 A 375 THR LYS ASP LYS PHE SER CYS ARG GLN ALA GLU MET SER
SEQRES 5 A 375 GLU LEU ILE GLN ARG TYR GLU LEU GLY THR LEU PRO GLY
SEQRES 6 A 375 ARG PRO SER THR LEU THR ALA SER PHE SER GLY ASN THR
SEQRES 7 A 375 LEU THR ILE ASN CYS GLY GLU ALA GLY LYS SER ILE SER
SEQRES 8 A 375 PHE THR VAL THR ILE THR TYR PRO SER SER GLY THR ALA
SEQRES 9 A 375 PRO TYR PRO ALA ILE ILE GLY TYR GLY GLY GLY SER LEU
SEQRES 10 A 375 PRO ALA PRO ALA GLY VAL ALA MET ILE ASN PHE ASN ASN
SEQRES 11 A 375 ASP ASN ILE ALA ALA GLN VAL ASN THR GLY SER ARG GLY
SEQRES 12 A 375 GLN GLY LYS PHE TYR ASP LEU TYR GLY SER SER HIS SER
SEQRES 13 A 375 ALA GLY ALA MET THR ALA TRP ALA TRP GLY VAL SER ARG
SEQRES 14 A 375 VAL ILE ASP ALA LEU GLU LEU VAL PRO GLY ALA ARG ILE
SEQRES 15 A 375 ASP THR THR LYS ILE GLY VAL THR GLY CYS SER ARG ASN
SEQRES 16 A 375 GLY LYS GLY ALA MET VAL ALA GLY ALA PHE GLU LYS ARG
SEQRES 17 A 375 ILE VAL LEU THR LEU PRO GLN GLU SER GLY ALA GLY GLY
SEQRES 18 A 375 SER ALA CYS TRP ARG ILE SER ASP TYR LEU LYS SER GLN
SEQRES 19 A 375 GLY ALA ASN ILE GLN THR ALA SER GLU ILE ILE GLY GLU
SEQRES 20 A 375 ASP PRO TRP PHE SER THR THR PHE ASN SER TYR VAL ASN
SEQRES 21 A 375 GLN VAL PRO VAL LEU PRO PHE ASP HIS HIS SER LEU ALA
SEQRES 22 A 375 ALA LEU ILE ALA PRO ARG GLY LEU PHE VAL ILE ASP ASN
SEQRES 23 A 375 ASN ILE ASP TRP LEU GLY PRO GLN SER CYS PHE GLY CYS
SEQRES 24 A 375 MET THR ALA ALA HIS MET ALA TRP GLN ALA LEU GLY VAL
SEQRES 25 A 375 SER ASP HIS MET GLY TYR SER GLN ILE GLY ALA HIS ALA
SEQRES 26 A 375 HIS CYS ALA PHE PRO SER ASN GLN GLN SER GLN LEU THR
SEQRES 27 A 375 ALA PHE VAL GLN LYS PHE LEU LEU GLY GLN SER THR ASN
SEQRES 28 A 375 THR ALA ILE PHE GLN SER ASP PHE SER ALA ASN GLN SER
SEQRES 29 A 375 GLN TRP ILE ASP TRP THR THR PRO THR LEU SER
SEQRES 1 B 375 GLN GLN THR SER GLY ALA GLY GLY ALA THR CYS SER ALA
SEQRES 2 B 375 LEU PRO GLY SER ILE THR LEU ARG SER ASN ALA LYS LEU
SEQRES 3 B 375 ASN ASP LEU PHE THR MET PHE ASN GLY ASP LYS VAL THR
SEQRES 4 B 375 THR LYS ASP LYS PHE SER CYS ARG GLN ALA GLU MET SER
SEQRES 5 B 375 GLU LEU ILE GLN ARG TYR GLU LEU GLY THR LEU PRO GLY
SEQRES 6 B 375 ARG PRO SER THR LEU THR ALA SER PHE SER GLY ASN THR
SEQRES 7 B 375 LEU THR ILE ASN CYS GLY GLU ALA GLY LYS SER ILE SER
SEQRES 8 B 375 PHE THR VAL THR ILE THR TYR PRO SER SER GLY THR ALA
SEQRES 9 B 375 PRO TYR PRO ALA ILE ILE GLY TYR GLY GLY GLY SER LEU
SEQRES 10 B 375 PRO ALA PRO ALA GLY VAL ALA MET ILE ASN PHE ASN ASN
SEQRES 11 B 375 ASP ASN ILE ALA ALA GLN VAL ASN THR GLY SER ARG GLY
SEQRES 12 B 375 GLN GLY LYS PHE TYR ASP LEU TYR GLY SER SER HIS SER
SEQRES 13 B 375 ALA GLY ALA MET THR ALA TRP ALA TRP GLY VAL SER ARG
SEQRES 14 B 375 VAL ILE ASP ALA LEU GLU LEU VAL PRO GLY ALA ARG ILE
SEQRES 15 B 375 ASP THR THR LYS ILE GLY VAL THR GLY CYS SER ARG ASN
SEQRES 16 B 375 GLY LYS GLY ALA MET VAL ALA GLY ALA PHE GLU LYS ARG
SEQRES 17 B 375 ILE VAL LEU THR LEU PRO GLN GLU SER GLY ALA GLY GLY
SEQRES 18 B 375 SER ALA CYS TRP ARG ILE SER ASP TYR LEU LYS SER GLN
SEQRES 19 B 375 GLY ALA ASN ILE GLN THR ALA SER GLU ILE ILE GLY GLU
SEQRES 20 B 375 ASP PRO TRP PHE SER THR THR PHE ASN SER TYR VAL ASN
SEQRES 21 B 375 GLN VAL PRO VAL LEU PRO PHE ASP HIS HIS SER LEU ALA
SEQRES 22 B 375 ALA LEU ILE ALA PRO ARG GLY LEU PHE VAL ILE ASP ASN
SEQRES 23 B 375 ASN ILE ASP TRP LEU GLY PRO GLN SER CYS PHE GLY CYS
SEQRES 24 B 375 MET THR ALA ALA HIS MET ALA TRP GLN ALA LEU GLY VAL
SEQRES 25 B 375 SER ASP HIS MET GLY TYR SER GLN ILE GLY ALA HIS ALA
SEQRES 26 B 375 HIS CYS ALA PHE PRO SER ASN GLN GLN SER GLN LEU THR
SEQRES 27 B 375 ALA PHE VAL GLN LYS PHE LEU LEU GLY GLN SER THR ASN
SEQRES 28 B 375 THR ALA ILE PHE GLN SER ASP PHE SER ALA ASN GLN SER
SEQRES 29 B 375 GLN TRP ILE ASP TRP THR THR PRO THR LEU SER
SEQRES 1 C 375 GLN GLN THR SER GLY ALA GLY GLY ALA THR CYS SER ALA
SEQRES 2 C 375 LEU PRO GLY SER ILE THR LEU ARG SER ASN ALA LYS LEU
SEQRES 3 C 375 ASN ASP LEU PHE THR MET PHE ASN GLY ASP LYS VAL THR
SEQRES 4 C 375 THR LYS ASP LYS PHE SER CYS ARG GLN ALA GLU MET SER
SEQRES 5 C 375 GLU LEU ILE GLN ARG TYR GLU LEU GLY THR LEU PRO GLY
SEQRES 6 C 375 ARG PRO SER THR LEU THR ALA SER PHE SER GLY ASN THR
SEQRES 7 C 375 LEU THR ILE ASN CYS GLY GLU ALA GLY LYS SER ILE SER
SEQRES 8 C 375 PHE THR VAL THR ILE THR TYR PRO SER SER GLY THR ALA
SEQRES 9 C 375 PRO TYR PRO ALA ILE ILE GLY TYR GLY GLY GLY SER LEU
SEQRES 10 C 375 PRO ALA PRO ALA GLY VAL ALA MET ILE ASN PHE ASN ASN
SEQRES 11 C 375 ASP ASN ILE ALA ALA GLN VAL ASN THR GLY SER ARG GLY
SEQRES 12 C 375 GLN GLY LYS PHE TYR ASP LEU TYR GLY SER SER HIS SER
SEQRES 13 C 375 ALA GLY ALA MET THR ALA TRP ALA TRP GLY VAL SER ARG
SEQRES 14 C 375 VAL ILE ASP ALA LEU GLU LEU VAL PRO GLY ALA ARG ILE
SEQRES 15 C 375 ASP THR THR LYS ILE GLY VAL THR GLY CYS SER ARG ASN
SEQRES 16 C 375 GLY LYS GLY ALA MET VAL ALA GLY ALA PHE GLU LYS ARG
SEQRES 17 C 375 ILE VAL LEU THR LEU PRO GLN GLU SER GLY ALA GLY GLY
SEQRES 18 C 375 SER ALA CYS TRP ARG ILE SER ASP TYR LEU LYS SER GLN
SEQRES 19 C 375 GLY ALA ASN ILE GLN THR ALA SER GLU ILE ILE GLY GLU
SEQRES 20 C 375 ASP PRO TRP PHE SER THR THR PHE ASN SER TYR VAL ASN
SEQRES 21 C 375 GLN VAL PRO VAL LEU PRO PHE ASP HIS HIS SER LEU ALA
SEQRES 22 C 375 ALA LEU ILE ALA PRO ARG GLY LEU PHE VAL ILE ASP ASN
SEQRES 23 C 375 ASN ILE ASP TRP LEU GLY PRO GLN SER CYS PHE GLY CYS
SEQRES 24 C 375 MET THR ALA ALA HIS MET ALA TRP GLN ALA LEU GLY VAL
SEQRES 25 C 375 SER ASP HIS MET GLY TYR SER GLN ILE GLY ALA HIS ALA
SEQRES 26 C 375 HIS CYS ALA PHE PRO SER ASN GLN GLN SER GLN LEU THR
SEQRES 27 C 375 ALA PHE VAL GLN LYS PHE LEU LEU GLY GLN SER THR ASN
SEQRES 28 C 375 THR ALA ILE PHE GLN SER ASP PHE SER ALA ASN GLN SER
SEQRES 29 C 375 GLN TRP ILE ASP TRP THR THR PRO THR LEU SER
MODRES 3PIC ASN C 447 ASN GLYCOSYLATION SITE
MODRES 3PIC ASN B 447 ASN GLYCOSYLATION SITE
HET NAG A 500 14
HET NAG B 500 14
HET NAG C 500 14
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
FORMUL 4 NAG 3(C8 H15 N O6)
FORMUL 7 HOH *1113(H2 O)
HELIX 1 1 THR A 125 GLU A 144 1 20
HELIX 2 2 ASN A 214 ALA A 219 1 6
HELIX 3 3 ASN A 223 ARG A 227 5 5
HELIX 4 4 GLY A 230 GLY A 237 1 8
HELIX 5 5 GLY A 243 VAL A 262 1 20
HELIX 6 6 PRO A 263 ALA A 265 5 3
HELIX 7 7 SER A 278 GLU A 291 1 14
HELIX 8 8 CYS A 309 GLN A 319 1 11
HELIX 9 9 THR A 325 ILE A 330 1 6
HELIX 10 10 SER A 337 TYR A 343 5 7
HELIX 11 11 GLN A 346 LEU A 350 5 5
HELIX 12 12 ASP A 353 LEU A 360 1 8
HELIX 13 13 ILE A 373 LEU A 376 5 4
HELIX 14 14 GLY A 377 LEU A 395 1 19
HELIX 15 15 VAL A 397 ASP A 399 5 3
HELIX 16 16 PRO A 415 ASN A 417 5 3
HELIX 17 17 GLN A 418 LEU A 430 1 13
HELIX 18 18 ASN A 447 ILE A 452 1 6
HELIX 19 19 THR B 125 GLU B 144 1 20
HELIX 20 20 ASN B 214 ALA B 219 1 6
HELIX 21 21 ASN B 223 ARG B 227 5 5
HELIX 22 22 GLY B 230 GLY B 237 1 8
HELIX 23 23 GLY B 243 VAL B 262 1 20
HELIX 24 24 PRO B 263 ALA B 265 5 3
HELIX 25 25 ASN B 280 GLU B 291 1 12
HELIX 26 26 CYS B 309 GLN B 319 1 11
HELIX 27 27 THR B 325 ILE B 330 1 6
HELIX 28 28 SER B 337 TYR B 343 5 7
HELIX 29 29 GLN B 346 LEU B 350 5 5
HELIX 30 30 ASP B 353 LEU B 360 1 8
HELIX 31 31 ILE B 373 LEU B 376 5 4
HELIX 32 32 GLY B 377 LEU B 395 1 19
HELIX 33 33 VAL B 397 ASP B 399 5 3
HELIX 34 34 PRO B 415 ASN B 417 5 3
HELIX 35 35 GLN B 418 LEU B 430 1 13
HELIX 36 36 ASN B 447 ILE B 452 1 6
HELIX 37 37 THR C 125 GLU C 144 1 20
HELIX 38 38 ASN C 214 ALA C 219 1 6
HELIX 39 39 ASN C 223 ARG C 227 5 5
HELIX 40 40 GLY C 230 GLY C 237 1 8
HELIX 41 41 GLY C 243 VAL C 262 1 20
HELIX 42 42 PRO C 263 ALA C 265 5 3
HELIX 43 43 SER C 278 GLU C 291 1 14
HELIX 44 44 CYS C 309 GLY C 320 1 12
HELIX 45 45 THR C 325 ILE C 330 1 6
HELIX 46 46 SER C 337 TYR C 343 5 7
HELIX 47 47 GLN C 346 LEU C 350 5 5
HELIX 48 48 ASP C 353 LEU C 360 1 8
HELIX 49 49 ILE C 373 LEU C 376 5 4
HELIX 50 50 GLY C 377 LEU C 395 1 19
HELIX 51 51 VAL C 397 ASP C 399 5 3
HELIX 52 52 PRO C 415 ASN C 417 5 3
HELIX 53 53 GLN C 418 LEU C 430 1 13
HELIX 54 54 ASN C 447 ILE C 452 1 6
SHEET 1 A10 THR A 154 SER A 160 0
SHEET 2 A10 THR A 163 GLU A 170 -1 O ASN A 167 N THR A 156
SHEET 3 A10 LYS A 173 THR A 182 -1 O PHE A 177 N ILE A 166
SHEET 4 A10 ALA A 209 PHE A 213 -1 O ASN A 212 N THR A 180
SHEET 5 A10 TYR A 191 TYR A 197 1 N GLY A 196 O ILE A 211
SHEET 6 A10 ILE A 267 CYS A 277 1 O ASP A 268 N TYR A 191
SHEET 7 A10 ILE A 294 GLN A 300 1 O LEU A 298 N VAL A 274
SHEET 8 A10 GLY A 365 ILE A 369 1 O PHE A 367 N THR A 297
SHEET 9 A10 MET A 401 SER A 404 1 O GLY A 402 N LEU A 366
SHEET 10 A10 PHE A 440 GLN A 441 1 O GLN A 441 N TYR A 403
SHEET 1 B10 THR B 154 SER B 160 0
SHEET 2 B10 THR B 163 GLU B 170 -1 O ASN B 167 N THR B 156
SHEET 3 B10 LYS B 173 THR B 182 -1 O VAL B 179 N LEU B 164
SHEET 4 B10 ALA B 209 PHE B 213 -1 O MET B 210 N THR B 182
SHEET 5 B10 TYR B 191 TYR B 197 1 N PRO B 192 O ALA B 209
SHEET 6 B10 ILE B 267 CYS B 277 1 O GLY B 273 N ALA B 193
SHEET 7 B10 ILE B 294 GLN B 300 1 O LEU B 298 N VAL B 274
SHEET 8 B10 GLY B 365 ILE B 369 1 O PHE B 367 N THR B 297
SHEET 9 B10 MET B 401 SER B 404 1 O GLY B 402 N LEU B 366
SHEET 10 B10 PHE B 440 GLN B 441 1 O GLN B 441 N TYR B 403
SHEET 1 C10 THR C 154 SER C 160 0
SHEET 2 C10 THR C 163 GLU C 170 -1 O GLY C 169 N THR C 154
SHEET 3 C10 LYS C 173 THR C 182 -1 O LYS C 173 N GLU C 170
SHEET 4 C10 ALA C 209 PHE C 213 -1 O ASN C 212 N THR C 180
SHEET 5 C10 TYR C 191 TYR C 197 1 N GLY C 196 O ILE C 211
SHEET 6 C10 ILE C 267 CYS C 277 1 O ASP C 268 N TYR C 191
SHEET 7 C10 ILE C 294 GLN C 300 1 O LEU C 298 N VAL C 274
SHEET 8 C10 GLY C 365 ASP C 370 1 O GLY C 365 N THR C 297
SHEET 9 C10 MET C 401 GLN C 405 1 O GLY C 402 N LEU C 366
SHEET 10 C10 PHE C 440 GLN C 441 1 O GLN C 441 N TYR C 403
SSBOND 1 CYS A 277 CYS A 412 1555 1555 2.04
SSBOND 2 CYS A 309 CYS A 384 1555 1555 2.03
SSBOND 3 CYS B 96 CYS B 131 1555 1555 2.03
SSBOND 4 CYS B 277 CYS B 412 1555 1555 2.04
SSBOND 5 CYS B 309 CYS B 384 1555 1555 2.03
SSBOND 6 CYS C 277 CYS C 412 1555 1555 2.04
SSBOND 7 CYS C 309 CYS C 384 1555 1555 2.03
LINK ND2 ASN C 447 C1 NAG C 500 1555 1555 1.45
LINK ND2 ASN B 447 C1 NAG B 500 1555 1555 1.45
CISPEP 1 ALA A 189 PRO A 190 0 0.32
CISPEP 2 ALA A 362 PRO A 363 0 0.65
CISPEP 3 ALA B 189 PRO B 190 0 -2.17
CISPEP 4 ALA B 362 PRO B 363 0 1.09
CISPEP 5 ALA C 189 PRO C 190 0 0.26
CISPEP 6 ALA C 362 PRO C 363 0 0.08
SITE 1 AC1 7 TYR A 315 GLN A 379 ASN A 447 GLN A 450
SITE 2 AC1 7 TRP A 451 HOH A 751 HOH A 815
SITE 1 AC2 7 TYR B 315 GLN B 379 ASN B 447 GLN B 450
SITE 2 AC2 7 TRP B 451 HOH B 748 HOH B 845
SITE 1 AC3 6 TYR C 315 GLN C 379 ASN C 447 GLN C 450
SITE 2 AC3 6 TRP C 451 HOH C 850
CRYST1 80.260 82.010 185.890 90.00 90.00 90.00 P 21 21 21 12
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 0.012460 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012194 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005380 0.00000
TER 2693 SER A 460
TER 5424 SER B 460
TER 8069 SER C 460
MASTER 400 0 3 54 30 0 6 6 9221 3 58 87
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