Mass: 34564.723 Da / Num. of mol.: 2 / Fragment: ALPHA/BETA-HYDROLASE DOMAIN, RESIDUES 114-421 Source method: isolated from a genetically manipulated source Details: N-GLYCOSYLATION AT ASN148 IN BOTH COPIES PRESENT. / Source: (gene. exp.) HOMO SAPIENS (human) Description: CDNA PROVIDED BY DRS.HUANG AND SMITH, MAYO CLINIC, ROCHESTER, MN. Plasmid: PPIC9 / Production host: PICHIA PASTORIS (fungus) / References: UniProt: Q9UI42
#2: Protein
HUMANLATEXIN / MUM
Mass: 25797.164 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PGAT2 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q9BS40
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
Wavelength: 1.0067 Å / Relative weight: 1
Reflection
Resolution: 1.6→48.3 Å / Num. obs: 179401 / % possible obs: 99.8 % / Observed criterion σ(I): 0 / Redundancy: 3.8 % / Biso Wilson estimate: 13.5 Å2 / Rmerge(I) obs: 0.07 / Net I/σ(I): 11.8
Reflection shell
Resolution: 1.6→1.69 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.26 / Mean I/σ(I) obs: 4.8 / % possible all: 99.3
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Processing
Software
Name
Version
Classification
DM
modelbuilding
SCALA
datascaling
AMoRE
phasing
MLPHARE
phasing
SIGMAA
phasing
DM
phasing
REFMAC
5.1.9999
refinement
Refinement
Method to determine structure: MOLECULAR REPLACEMENT Starting model: CPA4 WITHIN PCPA4 Resolution: 1.6→50 Å / Cor.coef. Fo:Fc: 0.968 / Cor.coef. Fo:Fc free: 0.96 / SU B: 2.467 / SU ML: 0.04 / Cross valid method: THROUGHOUT / ESU R: 0.063 / ESU R Free: 0.066 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. THERE IS NCS BETWEEN THE COMPLEX FORMED BY MOLECULES A-C AND COMPLEX B-D. IN MOLECULES B AND D, RESIDUES 218-222 ARE DISORDERED. THE ...Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. THERE IS NCS BETWEEN THE COMPLEX FORMED BY MOLECULES A-C AND COMPLEX B-D. IN MOLECULES B AND D, RESIDUES 218-222 ARE DISORDERED. THE COORDINATES OF HUMAN PROCARBOXYPEPTIDASE A4 EMPLOYED FOR THE MR CORRESPOND TO PDB ENTRY 2BOA.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.176
678
0.4 %
RANDOM
Rwork
0.149
-
-
-
obs
0.15
178706
99.8 %
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Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK