Solid-State NMR BMRB Deposition Content – Draft Specification(04/10/2005)
The outline below is a draft description of information unique primarily to a solid-state NMR
study of a biomolecular system that could be included in a BMRB deposition. The chemical structureof the system studied, a citation for the deposition, and other general information would also beincluded in a full deposition. Atomic coordinates and restraints for a structure determination could bepart of a deposition in the future and would be forwarded to the PDB. This draft is the result of thework of Dr. Matsuki and Professor Akutsu from Osaka University in collaboration with the BMRBstaff.
Input on these specifications from the solid-state NMR community is essential to developing acomplete and efficient archive of solid-state NMR data at BMRB. An electronic version of thisdocument will be available from the BMRB web site at this URL:
http://www.bmrb.wisc.edu/bmrb/features/
Please take the time to review this draft and send your comments and suggestions to Eldon Ulrich atBMRB (elu@bmrb.wisc.edu). Suggestions on the specific content of the archive and on which data
items should be required for a complete solid-state NMR entry are critical.

1. Kinds of experimental data or derived results archived
1.1. NMR parameters1.1.1. Assigned chemical shifts
1.1.2. Chemical shift referencing
1.1.2.1. Primary reference compound
1.1.2.2. Shift for secondary reference compound (hexamethyl benzene,adamantane, etc.)
1.1.2.3. Concentration and solvent for primary reference (DSS in water, TMS inchloroform, neat TMS, etc.)
1.1.2.4. ∆δ between primary and secondary reference used to report chemicalshifts
1.1.3. Dipolar coupling results
1.1.3.1 Scaling factor of the recoupling sequence
1.1.3.2. Fitting procedure
1.1.4. Quadrupolar coupling
1.1.5. Tensors
1.1.5.1. Chemical shift
CSA, asymmetry, principal components, Euler angles
1.1.5.2. Quadrupolar
1.1.5.3. Dipolar
1.2. Molecular geometries
1.2.1. Bond orientations with respect to Bo
1.2.2. Molecular axis with respect to Bo
1.2.3. Secondary structural elements (from chem. shifts)

2. Supporting data archived
2.1. Sample description
2.1.1. Type (lyophilized powder, polycrystalline powder, single crystal, fibrous protein,oriented glass plate/membrane film, precipitated microcrystal)
2.1.2. Content (weight and other characteristics of sample components)
2.1.2.1. Biopolymers (isotopic labeling pattern – single site, methyl group, otherside chain specific labeling, uniform, SAIL)
2.1.2.2. Excipients (salts, stabilizing agents, etc.)
2.1.3. Preparation
2.1.3.1. Crystallization (procedure followed, solution contents, etc.)
2.1.3.2. Cryo-protectant, if used
2.1.3.3. Oriented sample (procedure followed)2.2. Sample conditions
2.2.1. Temperature
2.2.1.1. Controller setting
2.2.1.2. Actual internal temperature
2.2.1.3. Calibration agent
2.3. Experimental parameters2.3.1. Spectrometer parameters2.3.1.1. Field strength
2.3.1.2. Rotor frequency
2.3.1.3. Rotor angle
2.3.1.4. Spectrometer manufacturer
2.3.1.5. Spectrometer model
2.3.2. Pulse programs (This information could be deposited for each NMR experimentthat was carried out.)
2.3.2.1. Overall experiment2.3.2.2. Recoupling sequence
2.3.2.2.1. Name (RFDR, SPC5, etc.)
2.3.2.2.2. Type (homonuclear or heteronuclear)
2.3.2.2.3. Nuclei
2.3.2.2.4. Time period for first mixing time
2.3.2.3. Decoupling sequence
2.3.2.3.1. Name
2.3.2.3.2. Nuclei
2.3.2.3.3. Time period
2.3.2.3.4. Decoupling strength (kHz)2.3.2.4. Citation for the pulse program
2.3.3. Probe parameters2.3.3.1. Rotor characteristics
2.3.3.1.1. Diameter2.3.3.1.2. Length
2.3.3.1.3. Volume (uL)
2.3.3.1.4. Composition (zirconium, etc.)
2.3.3.1.5. Spacer (yes/no)?
2.3.4. Probe characteristics
2.3.4.1. Type (transmission line, home built, triple/double resonance, inverse
coil, solenoid/saddle, etc.)