| PDB FORMAT Version 2.3 |
REMARK 1
REMARK 1 lists important publications related to the structure presented in the entry. These citations are chosen by the depositor. They are listed in reverse-chronological order. Citations are not repeated from the JRNL records. After the first blank record and the REFERENCE sub-record, the sub-record types for REMARK 1 are the same as in the JRNL sub-record types. For details, see the JRNL section.
Record Format and DetailsAs with all other remarks, the first line is empty and is used as a spacer.
The following tables are used to describe the sub-record types of REMARK 1.
1. REFERENCE
Each reference is preceded by a line indicating the reference number in the entry.
COLUMNS DATA TYPE FIELD DEFINITION
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1 - 6 Record name "REMARK"
10 LString(1) "1"
12 - 20 LString(9) "REFERENCE"
22 - 70 Integer refNum Reference number. Starts with
1 and increments by 1.
2. AUTH
AUTH contains the list of authors of the reference.
COLUMNS DATA TYPE FIELD DEFINITION
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1 - 6 Record name "REMARK"
10 LString(1) "1"
13 - 16 LString(4) "AUTH" Appears on all continuation
records.
17 - 18 Continuation continuation Allows a long list of
authors.
20 - 70 List authorList List of the authors.
See JRNL AUTH for details.
3. TITL
TITL specifies the title of the reference.
COLUMNS DATA TYPE FIELD DEFINITION
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1 - 6 Record name "REMARK"
10 LString(1) "1"
13 - 16 LString(4) "TITL" Appears on all
continuation records.
17 - 18 Continuation continuation Permits long titles.
20 - 70 LString title Title of the article.
See JRNL TITL for details.
4. EDIT
EDIT appears if editors are associated with a non-journal reference.
COLUMNS DATA TYPE FIELD DEFINITION
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1 - 6 Record name "REMARK"
10 LString(1) "1"
13 - 16 LString(4) "TITL" Appears on all
continuation records.
17 - 18 Continuation continuation Permits long list of editors.
20 - 70 LString editorList List of the editors.
See JRNL EDIT for details.
5. REF
REF is a group of fields which contains the name of the publication.
COLUMNS DATA TYPE FIELD DEFINITION ----------------------------------------------------------- 1 - 6 Record name "REMARK" 10 LString(1) "1" 13 - 16 LString(3) "REF" 20 - 34 LString(15) "TO BE PUBLISHED"
At the present time, there is no formal mechanism in place for monitoring the subsequent publication of referenced papers. PDB relies upon the depositor to provide reference update information since preliminary information can change by the time of actual publication.
COLUMNS DATA TYPE FIELD DEFINITION
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1 - 6 Record name "REMARK"
10 LString(1) "1"
13 - 16 LString(3) "REF"
17 - 18 Continuation continuation Permits long publication
names.
20 - 47 LString pubName Name of the publication including
section or series designation.
This is the only field of this
record which may be continued
on successive records.
50 - 51 LString(2) "V." Appears in the first record only,
and only if column 55 is filled in.
52 - 55 String volume Right-justified blank-filled volume
information; appears in the first
sub-record only.
57 - 61 String page First page of the article; appears
in the first sub-record only.
63 - 66 Integer year First record year of publication.
See JRNL REF for details.
6. PUBL
PUBL contains the name of the publisher and place of publication if the reference is to a book or other non- journal publication. If the reference has not yet been published or released, this sub-record is absent.
COLUMNS DATA TYPE FIELD DEFINITION
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1 - 6 Record name "REMARK"
10 LString(1) "1"
13 - 16 LString(4) "PUBL"
17 - 18 Continuation continuation Permits long publisher and
city information.
20 - 70 LString pub Name of the publisher and
city of publication.
See JRNL PUBL for details.
7. REFN
REFN is a group of fields which contains encoded references to the citation.
COLUMNS DATA TYPE FIELD DEFINITION --------------------------------------------------- 1 - 6 Record name "REMARK" 10 LString(1) "1" 13 - 16 LString(4) "REFN"
COLUMNS DATA TYPE FIELD DEFINITION
-------------------------------------------------------
1 - 6 Record name "REMARK"
10 LString(1) "1"
13 - 16 LString(4) "REFN"
20 - 23 LString(4) "ASTM" Blank if reference is not
serialized.
25 - 30 LString astm Code from the ASTM file.
33 - 34 LString country 2-digit abbreviation for
country of publication.
36 - 39 LString(4) "ISBN"
"ISSN" or "ESSN"
41 - 65 LString isbn ISSN or ISBN number.
See JRNL REFN for details.
Verification/Validation/Value Authority ControlPDB verifies that this record is correctly formatted.
Citations appearing in REMARK 1 may not appear in JRNL.
Relationships to Other Record TypesCitations appearing in REMARK 1 may not appear in JRNL.
Example
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REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.M.BONVIN,J.A.RULLMANN,R.M.LAMERICHS,R.BOELENS,
REMARK 1 AUTH 2 R.KAPTEIN
REMARK 1 TITL "ENSEMBLE" ITERATIVE RELAXATION MATRIX APPROACH:
REMARK 1 TITL 2 A NEW NMR REFINEMENT PROTOCOL APPLIED TO THE
REMARK 1 TITL 3 SOLUTION STRUCTURE OF CRAMBIN
REMARK 1 REF PROTEINS: STRUCT.,FUNCT., V. 15 385 1993
REMARK 1 REF 2 GENET.
REMARK 1 REFN ASTM PSFGEY US ISSN 0887-3585
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.A.C.RULLMANN,A.M.J.J.BONVIN,R.BOELENS,R.KAPTEIN
REMARK 1 TITL STRUCTURE DETERMINATION BY NMR - APPLICATION TO
REMARK 1 TITL 2 CRAMBIN
REMARK 1 EDIT D.M.SOUMPASIS,T.M.JOVIN
REMARK 1 REF COMPUTATION OF BIOMOLECULAR 1 1992
REMARK 1 REF 2 STRUCTURES; ACHIEVEMENTS,
REMARK 1 REF 3 PROBLEMS, AND PERSPECTIVES
REMARK 1 PUBL BERLIN : SPRINGER-VERLAG
REMARK 1 REFN GW ISBN 3540559515
REMARK 1 REFERENCE 3
REMARK 1 AUTH R.M.J.M.LAMERICHS
REMARK 1 REF 2D NMR STUDIES OF 1989
REMARK 1 REF 2 BIOMOLECULES: PROTEIN
REMARK 1 REF 3 STRUCTURE AND PROTEIN-DNA
REMARK 1 REF 4 INTERACTIONS
REMARK 1 PUBL UTRECHT : UNIVERSITY OF UTRECHT (THESIS)
REMARK 1 REFN NE
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.FERMI,M.F.PERUTZ
REMARK 1 REF HAEMOGLOBIN AND MYOGLOBIN 1981
REMARK 1 REF 2 (IN: ATLAS OF MOLECULAR
REMARK 1 REF 3 STRUCTURES IN BIOLOGY, V.2)
REMARK 1 PUBL OXFORD : CLARENDON PRESS
REMARK 1 REFN ISBN 0-19-854706-4
Known Problems
See JRNL for a listing of problems associated with references.
REMARK 2
REMARK 2 states the highest resolution, in Angstroms, that was used in building the model. As with all the remarks, the first REMARK 2 record is empty and is used as a spacer.
Record Format and Details
COLUMNS DATA TYPE FIELD DEFINITION ------------------------------------------------------- 1 - 6 Record name "REMARK" 10 LString(1) "2" 12 - 22 LString(11) "RESOLUTION." 23 - 27 Real(5.2) resolution Resolution. 29 - 38 LString(10) "ANGSTROMS."
COLUMNS DATA TYPE FIELD DEFINITION ------------------------------------------------------------------- 1 - 6 Record name "REMARK" 10 LString(1) "2" 12 - 38 LString(28) "RESOLUTION. NOT APPLICABLE." 41 - 70 String comment Comment.
COLUMNS DATA TYPE FIELD DEFINITION ---------------------------------------------------------- 1 - 6 Record name "REMARK" 10 LString(1) "2" 12 - 22 LString(11) "RESOLUTION." 24 - 70 String comment Comment.Example
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REMARK 2
REMARK 2 RESOLUTION. 1.74 ANGSTROMS.
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 2 THIS EXPERIMENT WAS CARRIED OUT USING FLUORESCENCE TRANSFER
REMARK 2 AND THEREFORE NO RESOLUTION CAN BE CALCULATED.
REMARK 4-999
OverviewREMARKs following the refinement remark consist of free text annotation, predefined boilerplate remarks, and token: value pair styled templates. Presented here are examples of remark sections in PDB files
Record Format and Details
REMARK 4
Remark 4 indicates the version of the PDB file format used to generate the file.
Template
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REMARK 4
REMARK 4 XXXX COMPLIES WITH FORMAT V. 2.3, DD-MMM-YYYY
XXXX refers to the ID code of the entry.
N.M refers to the version number.
DD-MMM-YYYY refers to the release date of that version of the format. DD is a number 01 through
31, MMM is a 3 letter abbreviation for the month, and YYYY is the year.
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REMARK 4
REMARK 4 1ABC COMPLIES WITH FORMAT V. 2.3, 09-JUL-1998
REMARKs 5-99
REMARKs 5-99, Not in use
REMARK 100
REMARK 100, Deposition or Processing Site This remark indicates the processing site: RCSB, MSD-EBI, PDBj, or NDB.
Example
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REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-NOV-2006.
REMARK 100 THE RCSB ID CODE IS RCSB040554.
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 7-NOV-2005.
REMARK 100 THE EBI ID CODE IS EBI-26270.
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-DEC-2005.
REMARK 100 THE RCSB ID CODE IS RCSB025208.
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY THE NUCLEIC ACID DATABASE
REMARK 100 ON 08-DEC-2006.
REMARK 100 THE NDB ID CODE IS PH0029
REMARKs 102-199 Nucleic Acids
REMARK 102, For base mispairings
Remark 102 is mandatory if mispaired bases exist and Watson-Crick H-bonding is present.
Template
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REMARK 102
REMARK 102 BASES A B NN AND X Y ZZ ARE MISPAIRED.
REMARK 102 BASES A B NN AND X Y ZZ ARE MISPAIRED.
REMARK 102 ALL OTHER HYDROGEN BONDS BETWEEN BASE PAIRS IN THIS ENTRY
REMARK 102 FOLLOW THE CONVENTIONAL WATSON-CRICK HYDROGEN BONDING
REMARK 102 PATTERN AND THEY HAVE NOT BEEN PRESENTED ON *CONECT*
REMARK 102 RECORDS IN THIS ENTRY.
A is the residue name, B the chain identifier, and NN the sequence number of first base, X is the residue name, Y the chain id, and ZZ the sequence number of the second base.
Example
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REMARK 102
REMARK 102 BASES G A 4 AND A B 21 ARE MISPAIRED.
REMARK 102 BASES A A 9 AND G B 16 ARE MISPAIRED.
REMARK 102 ALL OTHER HYDROGEN BONDS BETWEEN BASE PAIRS IN THIS ENTRY
REMARK 102 FOLLOW THE CONVENTIONAL WATSON-CRICK HYDROGEN BONDING
REMARK 102 PATTERN AND THEY HAVE NOT BEEN PRESENTED ON *CONECT*
REMARK 102 RECORDS IN THIS ENTRY.
For structures containing inosine, Inosine is treated like a standard residue, however, entries containing inosine also include remarks 103 and 104.
REMARK 103
Remark 103 is mandatory if non-Watson-Crick H-bonding is present for specific interactions.
Template
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REMARK 103
REMARK 103 THERE ARE NON-WATSON-CRICK HYDROGEN BONDS BETWEEN THE
REMARK 103 FOLLOWING ATOMS:
REMARK 103 AB I X N AND AB Z X NN
REMARK 103 AB I X N AND AB Z X NN
REMARK 103 ALL OTHER HYDROGEN BONDS BETWEEN BASE PAIRS IN THIS ENTRY
REMARK 103 FOLLOW THE CONVENTIONAL WATSON-CRICK HYDROGEN BONDING
REMARK 103 PATTERN AND THEY HAVE NOT BEEN PRESENTED ON *CONECT*
REMARK 103 RECORDS IN THIS ENTRY.
AB is the atom name, I the residue name inosine, X the chain identifier, and N the sequence number of inosine, and AB is the atom name, Z the residue name, X the chain identifier, and NN the sequence number of the base that is paired with inosine.
REMARK 104
Remark 104 is mandatory if inosine exists.
Template
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REMARK 104
REMARK 104 RESIDUE I X N IS INOSINE.
REMARK 104 RESIDUE I X N IS INOSINE.
X is the chain identifier and N the sequence number.
Example
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REMARK 103
REMARK 103 THERE ARE NON-WATSON-CRICK HYDROGEN BONDS BETWEEN THE
REMARK 103 FOLLOWING ATOMS:
REMARK 103 N1 I A 1 AND N3 C B 16
REMARK 103 O6 I A 1 AND N4 C B 16
REMARK 103 N1 I A 3 AND N3 C B 14
REMARK 103 O6 I A 3 AND N4 C B 14
REMARK 103 ALL OTHER HYDROGEN BONDS BETWEEN BASE PAIRS IN THIS ENTRY
REMARK 103 FOLLOW THE CONVENTIONAL WATSON-CRICK HYDROGEN BONDING
REMARK 103 PATTERN AND THEY HAVE NOT BEEN PRESENTED ON CONECT
REMARK 103 RECORDS IN THIS ENTRY.
REMARK 104
REMARK 104 RESIDUE I A 1 IS INOSINE.
REMARK 104 RESIDUE I A 3 IS INOSINE.
REMARK 105
Remark 105 is mandatory if nucleic acids exist in an entry.
Template
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REMARK 105
REMARK 105 THE PROTEIN DATA BANK HAS ADOPTED THE SACCHARIDE CHEMISTS
REMARK 105 NOMENCLATURE FOR ATOMS OF THE DEOXYRIBOSE/RIBOSE MOIETY
REMARK 105 RATHER THAN THAT OF THE NUCLEOSIDE CHEMISTS. THE RING
REMARK 105 OXYGEN ATOM IS LABELLED O4* INSTEAD OF O1*.
REMARK 106
Remark 106 is mandatory if hydrogen bonding is Watson-Crick.
Template
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REMARK 106
REMARK 106 THE HYDROGEN BONDS BETWEEN BASE PAIRS IN THIS ENTRY FOLLOW
REMARK 106 THE CONVENTIONAL WATSON-CRICK HYDROGEN BONDING PATTERN.
REMARK 106 THEY HAVE NOT BEEN PRESENTED ON *CONECT* RECORDS IN THIS
REMARK 106 ENTRY.
REMARK 200-250, Experimental Details
Remarks in this range present the data collection details for the data which resulted in the refinement statistics of REMARK 3. They provide information on the structure determination experiment, which may have been done by diffraction, NMR, theoretical modeling, or some other technique.
The "NULL" value will be used if the data for a token is not supplied by the depositor.
REMARK 200, X-ray Diffraction Experimental Details
To be used for single crystal, fiber, or polycrystalline X-ray diffraction experiments.
Remark 200 is mandatory if x-ray.
Template
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REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION :
REMARK 200 TEMPERATURE (KELVIN) :
REMARK 200 PH :
REMARK 200 NUMBER OF CRYSTALS USED :
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) :
REMARK 200 RADIATION SOURCE :
REMARK 200 BEAMLINE :
REMARK 200 X-RAY GENERATOR MODEL :
REMARK 200 MONOCHROMATIC OR LAUE (M/L) :
REMARK 200 WAVELENGTH OR RANGE (A) :
REMARK 200 MONOCHROMATOR :
REMARK 200 OPTICS :
REMARK 200
REMARK 200 DETECTOR TYPE :
REMARK 200 DETECTOR MANUFACTURER :
REMARK 200 INTENSITY-INTEGRATION SOFTWARE :
REMARK 200 DATA SCALING SOFTWARE :
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS :
REMARK 200 RESOLUTION RANGE HIGH (A) :
REMARK 200 RESOLUTION RANGE LOW (A) :
REMARK 200 REJECTION CRITERIA (SIGMA(I)) :
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) :
REMARK 200 DATA REDUNDANCY :
REMARK 200 R MERGE (I) :
REMARK 200 R SYM (I) :
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET :
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) :
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) :
REMARK 200 COMPLETENESS FOR SHELL (%) :
REMARK 200 DATA REDUNDANCY IN SHELL :
REMARK 200 R MERGE FOR SHELL (I) :
REMARK 200 R SYM FOR SHELL (I) :
REMARK 200 <I/SIGMA(I)> FOR SHELL :
REMARK 200
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE:
REMARK 200 SOFTWARE USED:
REMARK 200 STARTING MODEL:
REMARK 200
REMARK 200 REMARK:
REMARK 205, Fiber Diffraction, Fiber Sample Experiment Details
Remark 205 is mandatory if fiber diffraction - non-crystalline sample.
Template
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REMARK 205
REMARK 205 THESE COORDINATES WERE GENERATED FROM FIBER DIFFRACTION
REMARK 205 DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT CRYST1
REMARK 205 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES OF THESE
REMARK 205 RECORDS ARE MEANINGLESS.
REMARKs 210 and 215, NMR Experiment Details
Remark 210 is mandatory if NMR.
Template
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REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) :
REMARK 210 PH :
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED :
REMARK 210 SPECTROMETER FIELD STRENGTH :
REMARK 210 SPECTROMETER MODEL :
REMARK 210 SPECTROMETER MANUFACTURER :
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED :
REMARK 210 METHOD USED :
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED :
REMARK 210 CONFORMERS, NUMBER SUBMITTED :
REMARK 210 CONFORMERS, SELECTION CRITERIA :
REMARK 210
REMARK 210 REMARK:
Remark 215 is mandatory if NMRTemplate
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REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
REMARK 217, Solid State NMR
This remark will appear in all solid state NMR entries.
REMARK 217 REMARK 217 SOLID STATE NMR STUDY REMARK 217 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLID REMARK 217 STATE NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT REMARK 217 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON REMARK 217 THESE RECORDS ARE MEANINGLESS.
REMARKs 220 and 225, Theoretical Modeling Experiment Details
Note: As of July 1, 2002, models are available from a directory separate from the main archive at https://ftp.rcsb.org/pub/pdb/data/structures/models/current/. As of October 15, 2006, theoretical models are no longer accepted for deposition.
Template
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REMARK 220
REMARK 220 EXPERIMENTAL DETAILS
REMARK 220 EXPERIMENT TYPE : THEORETICAL MODELLING
REMARK 220
REMARK 220 REMARK:
REMARK 225
Remark 225 is mandatory if theoretical model.
Template
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REMARK 225
REMARK 225 THEORETICAL MODEL
REMARK 225 THE COORDINATES IN THIS ENTRY REPRESENT A MODEL STRUCTURE.
REMARK 225 PROTEIN DATA BANK CONVENTIONS REQUIRE THAT CRYST1 AND
REMARK 225 SCALE RECORDS BE INCLUDED, BUT THE VALUES ON THESE
REMARK 225 RECORDS ARE MEANINGLESS.
REMARK 230, Neutron Diffraction Experiment Details
Remark 230 is mandatory if neutron diffraction study.
Template
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REMARK 230
REMARK 230 EXPERIMENTAL DETAILS
REMARK 230 EXPERIMENT TYPE : NEUTRON DIFFRACTION
REMARK 230 DATE OF DATA COLLECTION :
REMARK 230 TEMPERATURE (KELVIN) :
REMARK 230 PH :
REMARK 230 NUMBER OF CRYSTALS USED :
REMARK 230
REMARK 230 NEUTRON SOURCE :
REMARK 230 BEAMLINE :
REMARK 230 WAVELENGTH OR RANGE (A) :
REMARK 230 MONOCHROMATOR :
REMARK 230 OPTICS :
REMARK 230
REMARK 230 DETECTOR TYPE :
REMARK 230 DETECTOR MANUFACTURER :
REMARK 230 INTENSITY-INTEGRATION SOFTWARE :
REMARK 230 DATA SCALING SOFTWARE :
REMARK 230
REMARK 230 NUMBER OF UNIQUE REFLECTIONS :
REMARK 230 RESOLUTION RANGE HIGH (A) :
REMARK 230 RESOLUTION RANGE LOW (A) :
REMARK 230 REJECTION CRITERIA (SIGMA(I)) :
REMARK 230
REMARK 230 OVERALL.
REMARK 230 COMPLETENESS FOR RANGE (%) :
REMARK 230 DATA REDUNDANCY :
REMARK 230 R MERGE (I) :
REMARK 230 R SYM (I) :
REMARK 230 <I/SIGMA(I)> FOR THE DATA SET :
REMARK 230
REMARK 230 IN THE HIGHEST RESOLUTION SHELL.
REMARK 230 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) :
REMARK 230 HIGHEST RESOLUTION SHELL, RANGE LOW (A) :
REMARK 230 COMPLETENESS FOR SHELL (%) :
REMARK 230 DATA REDUNDANCY IN SHELL :
REMARK 230 R MERGE FOR SHELL (I) :
REMARK 230 R SYM FOR SHELL (I) :
REMARK 230 <I/SIGMA(I)> FOR SHELL :
REMARK 230
REMARK 230 METHOD USED TO DETERMINE THE STRUCTURE:
REMARK 230 SOFTWARE USED :
REMARK 230 STARTING MODEL:
REMARK 230
REMARK 230 REMARK:
REMARK 240, Electron Diffraction Experiment Details
Remark 240 is mandatory if electron diffraction study. Template
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REMARK 240
REMARK 240 EXPERIMENTAL DETAILS
REMARK 240 EXPERIMENT TYPE : ELECTRON DIFFRACTION
REMARK 240 DATE OF DATA COLLECTION :
REMARK 240
REMARK 240 REMARK:
REMARK 245, Cryo-Electron Microscopy Experiment Details
Remark 245 is mandatory if cryo-EM study.
Template
REMARK 245 REMARK 245 EXPERIMENTAL DETAILS REMARK 245 EXPERIMENT TYPE : CRYO-ELECTRON MICROSCOPY REMARK 245 REMARK 245 ELECTRON MICROSCOPE SAMPLE REMARK 245 SAMPLE AGGREGATION STATE : REMARK 245 REMARK 245 NAME OF SAMPLE : REMARK 245 REMARK 245 SAMPLE CONCENTRATION : REMARK 245 SAMPLE SUPPORT DETAILS : REMARK 245 REMARK 245 SAMPLE VITRIFICATION DETAILS : REMARK 245 REMARK 245 SAMPLE BUFFER : REMARK 245 REMARK 245 PH : REMARK 245 SAMPLE DETAILS: REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : REMARK 245 TEMPERATURE (KELVIN) : REMARK 245 MICROSCOPE MODEL : REMARK 245 DETECTOR TYPE : REMARK 245 MINIMUM DEFOCUS (NM) : REMARK 245 MAXIMUM DEFOCUS (NM) : REMARK 245 MINIMUM TILT ANGLE (DEGREES) : REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : REMARK 245 NOMINAL CS : REMARK 245 IMAGING MODE : REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : REMARK 245 ILLUMINATION MODE : REMARK 245 NOMINAL MAGNIFICATION : REMARK 245 CALIBRATED MAGNIFICATION : REMARK 245 SOURCE : REMARK 245 ACCELERATION VOLTAGE (KV) : REMARK 245 IMAGING DETAILS:Example
REMARK 245 REMARK 245 EXPERIMENTAL DETAILS REMARK 245 REMARK 245 EXPERIMENT TYPE : CRYO-ELECTRON MICROSCOPY REMARK 245 REMARK 245 ELECTRON MICROSCOPE SAMPLE REMARK 245 SAMPLE AGGREGATION STATE : ICOSAHEDRAL REMARK 245 NAME OF SAMPLE : BACTERIOPHAGE PRD1 SUS1 MUTANT REMARK 245 SAMPLE CONCENTRATION : NULL REMARK 245 SAMPLE SUPPORT DETAILS : HOLEY CARBON REMARK 245 SAMPLE VITRIFICATION DETAILS : PLUNGE VITRIFICATION REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.2 REMARK 245 SAMPLE DETAILS: THE SAMPLE CONSISTS OF THE ADENOVIRUS- REMARK 245 RELATED BACTERIOPHAGE PRD1. 400 MESH COPPER GLOW DISCHARGE REMARK 245 SAMPLES WERE PREPARED AS THIN LAYERS OF VITREOUS ICE. REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : 15 JUNE 1998 REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 29 REMARK 245 TEMPERATURE (KELVIN) : 95 REMARK 245 MICROSCOPE MODEL : PHILIPS CM200 FEG REMARK 245 DETECTOR TYPE : SO-163 FILM REMARK 245 MINIMUM DEFOCUS (NM) : 1300 REMARK 245 MAXIMUM DEFOCUS (NM) : 4100 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : 0 REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : 0 REMARK 245 NOMINAL CS : 2 REMARK 245 IMAGING MODE : LOW DOSE REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 1000 REMARK 245 ILLUMINATION MODE : BRIGHT FIELD REMARK 245 NOMINAL MAGNIFICATION : 36000 REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 200 REMARK 245 IMAGING DETAILS: SAMPLES WERE MAINTAINED AT LIQUID NITROGEN REMARK 245 TEMPERATURES IN THE ELECTRON MICROSCOPE WITH A GATAN 626-0300 REMARK 245 CRYOTRANSFER HOLDER.
REMARK 247, mandatory if Electron Microscopy
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REMARK 247
REMARK 247 ELECTRON MICROSCOPY
REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM
REMARK 247 ELECTRON MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS
REMARK 247 REQUIRE THAT CRYST1 AND SCALE RECORDS BE INCLUDED,
REMARK 247 BUT THE VALUES ON THESE RECORDS ARE MEANINGLESS
REMARK 247 EXCEPT FOR THE CALCULATION OF THE STRUCTURE FACTORS
REMARK 250, Other Type of Experiment Details
REMARK 250
Remark specific to other kinds of studies, not listed above. Remark 250 is mandatory if other than x-ray, NMR, theoretical model*, neutron, or electron study.
Note: As of July 1, 2002, models are available from a directory separate from the main archive at https://ftp.rcsb.org/pub/pdb/data/structures/models/current/. As of October 15, 2006, theoretical models are no longer accepted for deposition.
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REMARK 250
REMARK 250 EXPERIMENTAL DETAILS
REMARK 250 EXPERIMENT TYPE :
REMARK 250 DATE OF DATA COLLECTION :
REMARK 250
REMARK 250 REMARK:
REMARK 265, Solution Scatter Example Experiment Details
REMARK 265 REMARK 265 EXPERIMENTAL DETAILS REMARK 265 REMARK 265 EXPERIMENT TYPE : X-RAY SOLUTION SCATTERING REMARK 265 DATA ACQUISITION REMARK 265 RADIATION/NEUTRON SOURCE : SRS BEAMLINE 2.1 REMARK 265 SYNCHROTRON (Y/N) : Y REMARK 265 BEAMLINE : 2.1 REMARK 265 BEAMLINE INSTRUMENT : NULL REMARK 265 DETECTOR TYPE : 500-CHANNEL QUADRANT REMARK 265 DETECTOR MANUFACTURER DETAILS : NULL REMARK 265 TEMPERATURE (KELVIN) : 288 REMARK 265 PH : NULL REMARK 265 NUMBER OF TIME FRAMES USED : 10 REMARK 265 PROTEIN CONCENTRATION RANGE (MG/ML) : 0.7 - 14 REMARK 265 SAMPLE BUFFER : TRIS REMARK 265 DATA REDUCTION SOFTWARE : OTOKO REMARK 265 DATA ANALYSIS SOFTWARE : SCTPL5, GNOM REMARK 265 GUINIER MEAN RADIUS OF GYRATION (NM) : 11.1 REMARK 265 SIGMA MEAN RADIUS OF GYRATION : 0.4 REMARK 265 R(XS-1) MEAN CROSS SECTIONAL RADII (NM) : 4.4 REMARK 265 R(XS-1) SIGMA MEAN CROSS SECTIONAL RADII : 0.2 REMARK 265 R(XS-2) MEAN CROSS SECTIONAL RADII (NM) : 1.7 REMARK 265 R(XS-2) SIGMA MEAN CROSS SECTIONAL RADII : 0.1 REMARK 265 P(R) PROTEIN LENGTH (NM) : 40 REMARK 265 REMARK 265 EXPERIMENT TYPE : NEUTRON SOLUTION SCATTERING REMARK 265 DATA ACQUISITION REMARK 265 RADIATION/NEUTRON SOURCE : ILL REMARK 265 SYNCHROTRON (Y/N) : N REMARK 265 BEAMLINE : NULL REMARK 265 BEAMLINE INSTRUMENT : D11, D22 REMARK 265 DETECTOR TYPE : AREA REMARK 265 DETECTOR MANUFACTURER DETAILS : NULL REMARK 265 TEMPERATURE (KELVIN) : NULL REMARK 265 PH : NULL REMARK 265 NUMBER OF TIME FRAMES USED : NULL REMARK 265 PROTEIN CONCENTRATION RANGE (MG/ML) : 0.4 - 9.6 REMARK 265 SAMPLE BUFFER : PBS IN 99.9% D2O REMARK 265 DATA REDUCTION SOFTWARE : DETEC, RNILS, SPOLLY REMARK 265 DATA ANALYSIS SOFTWARE : SCTPL5, GNOM REMARK 265 GUINIER MEAN RADIUS OF GYRATION (NM) : 11.3 REMARK 265 SIGMA MEAN RADIUS OF GYRATION : 0.4 REMARK 265 R(XS-1) MEAN CROSS SECTIONAL RADII (NM) : 3.9 REMARK 265 R(XS-1) SIGMA MEAN CROSS SECTIONAL RADII : 0.2 REMARK 265 R(XS-2) MEAN CROSS SECTIONAL RADII (NM) : 1.51 REMARK 265 R(XS-2) SIGMA MEAN CROSS SECTIONAL RADII : 0.06 REMARK 265 P(R) PROTEIN LENGTH (NM) : 37 - 39 REMARK 265 REMARK 265 DATA ACQUISITION REMARK 265 RADIATION/NEUTRON SOURCE : ISIS REMARK 265 SYNCHROTRON (Y/N) : N REMARK 265 BEAMLINE : PULSED NEUTRON REMARK 265 BEAMLINE INSTRUMENT : LOQ REMARK 265 DETECTOR TYPE : AREA (TIME-OF-FLIGHT) REMARK 265 DETECTOR MANUFACTURER DETAILS : NULL REMARK 265 TEMPERATURE (KELVIN) : NULL REMARK 265 PH : NULL REMARK 265 NUMBER OF TIME FRAMES USED : NULL REMARK 265 PROTEIN CONCENTRATION RANGE (MG/ML) : 3.7, 6.1 REMARK 265 SAMPLE BUFFER : PBS IN 99.9% D2O REMARK 265 DATA REDUCTION SOFTWARE : COLLETTE REMARK 265 DATA ANALYSIS SOFTWARE : SCTPL5, GNOM REMARK 265 GUINIER MEAN RADIUS OF GYRATION (NM) : 11.7 REMARK 265 SIGMA MEAN RADIUS OF GYRATION : 0.5 REMARK 265 R(XS-1) MEAN CROSS SECTIONAL RADII (NM) : NULL REMARK 265 R(XS-1) SIGMA MEAN CROSS SECTIONAL RADII : NULL REMARK 265 R(XS-2) MEAN CROSS SECTIONAL RADII (NM) : NULL REMARK 265 R(XS-2) SIGMA MEAN CROSS SECTIONAL RADII : NULL REMARK 265 P(R) PROTEIN LENGTH (NM) : 40 REMARK 265 REMARK 265 EXPERIMENT TYPE: THEORETICAL MODELLING REMARK 265 METHOD USED TO DETERMINE THE STRUCTURE: CONSTRAINED SCATTERING REMARK 265 FITTING OF HOMOLOGY REMARK 265 MODELS REMARK 265 SOFTWARE USED : INSIGHT II, HOMOLOGY, DISCOVERY, REMARK 265 BIOPOLYMER, DELPHI REMARK 265 SOFTWARE AUTHORS : MSI REMARK 265 STARTING MODEL : PDB CODE 1HFI, 1HCC, 1HFH, 1VCC REMARK 265 REMARK 265 EXPERIMENTAL DETAILS: HOMOLOGY MODELS WERE BUILT FOR REMARK 265 THE 17 SCR DOMAINS AND ENERGY MINIMISATIONS WERE REMARK 265 PERFORMED TO IMPROVE THE CONNECTIVITY IN THE FH MODEL. REMARK 265 TRIANTENNARY COMPLEX-TYPE CARBOHYDRATE STRUCTURES REMARK 265 (MAN3GLCNAC6GAL3FUC3NEUNAC1) WERE ADDED TO EACH OF THE REMARK 265 N-LINKED GLYCOSYLATION SITES. A LIBRARY OF LINKER PEPTIDE REMARK 265 CONFORMATIONS WAS USED IN DOMAIN MODELLING CONSTRAINED REMARK 265 BY THE SOLUTION SCATTERING FITS. MODELLING WITH THE REMARK 265 SCATTERING DATA WAS ALSO CARRIED OUT BY ROTATIONAL REMARK 265 SEARCH METHODS. THE X-RAY AND NEUTRON SCATTERING CURVE REMARK 265 I(Q) WAS CALCULATED ASSUMING A UNIFORM SCATTERING DENSITY REMARK 265 FOR THE SPHERES USING THE DEBYE EQUATION AS ADAPTED TO REMARK 265 SPHERES. X-RAY CURVES WERE CALCULATED FROM THE HYDRATED REMARK 265 SPHERE MODELS WITHOUT CORRECTIONS FOR WAVELENGTH SPREAD OR REMARK 265 BEAM DIVERGENCE, WHILE THESE CORRECTIONS WERE APPLIED FOR REMARK 265 THE NEUTRON CURVES BUT NOW USING UNHYDRATED MODELS. REMARK 265 REMARK 265 CONFORMERS, NUMBER CALCULATED : 2010 REMARK 265 CONFORMERS, NUMBER SUBMITTED : 4 REMARK 265 CONFORMERS, SELECTION CRITERIA : THE MODELLED SCATTERING REMARK 265 CURVES WERE ASSESSED BY CALCULATION OF THE REMARK 265 RG, RSX-1 AND RXS-2 VALUES IN THE SAME Q RANGES REMARK 265 USED IN THE EXPERIMENTAL GUINIER FITS. MODELS WERE REMARK 265 THEN RANKED USING A GOODNESS-OF-FIT R-FACTOR REMARK 265 DEFINED BY ANALOGY WITH PROTEIN CRYSTALLOGRAPHY REMARK 265 AND BASED ON THE EXPERIMENTAL CURVES IN THE Q RANGE REMARK 265 EXTENDING TO 1.4 NM-1. REMARK 265
REMARK 280, Crystal
Remark 280 presents information on the crystal. The solvent content and Matthews coefficient are provided for protein and polypeptide crystals. Crystallization conditions are free text.
Remark 280 is mandatory if single crystal study.
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REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%):
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA):
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: FREE TEXT GOES HERE.
Example
REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 36.85 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.79 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4M SODIUM ACETATE, REMARK 280 0.1M MES PH 6.5
REMARK 285, CRYST1
Remark 285 presents information on the unit cell.
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REMARK 285
REMARK 285 CRYST1
REMARK 285 FREE TEXT GOES HERE.
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REMARK 285
REMARK 285 CRYST1
REMARK 285 TEXT TO EXPLAIN UNUSUAL UNIT-CELL DATA: THE DATA WAS
REMARK 285 COLLECTED ON TWO-DIMENSIONAL CRYSTALS AND HENCE THE
REMARK 285 C-AXIS REPEAT DOES NOT CORRESPOND TO A REAL REPEAT, BUT
REMARK 285 INSTEAD REFERS TO THE SAMPLING THAT IS USED TO DESCRIBE
REMARK 285 THE CONTINUOUS TRANSFORM. THE C VALUE OF 100.9 IS
REMARK 285 THEREFORE THE VALUE WHICH SHOULD BE USED IN
REMARK 285 INTERPRETING THE MEANING OF THE L INDEX.
REMARK 290, Crystallographic Symmetry
Remark 290 is mandatory for crystalline studies. The remark is generated by PDB.
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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 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-Z
REMARK 290 4555 1/2+X,1/2-Y,-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 36.30027
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 59.50256
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.45545
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 59.50256
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.30027
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 46.45545
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK:
REMARK 295, Non-Crystallographic Symmetry
Description of non-crystallographic symmetry. Mandatory when MTRIX records are present.
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REMARK 295
REMARK 295 NON-CRYSTALLOGRAPHIC SYMMETRY
REMARK 295 THE TRANSFORMATIONS PRESENTED ON THE MTRIX RECORDS BELOW
REMARK 295 DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG ATOMS
REMARK 295 IN THIS ENTRY. APPLYING THE APPROPRIATE MTRIX
REMARK 295 TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD
REMARK 295 APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND.
REMARK 295 CHAIN IDENTIFIERS GIVEN AS "?" REFER TO CHAINS FOR WHICH
REMARK 295 ATOMS ARE NOT FOUND IN THIS ENTRY.
REMARK 295
REMARK 295 APPLIED TO TRANSFORMED TO
REMARK 295 TRANSFORM CHAIN RESIDUES CHAIN RESIDUES RMSD
REMARK 295 SSS ? ? .. ? ? ? .. ? ?
REMARK 295
REMARK 295 WHERE SSS -> COLUMNS 8-10 OF MTRIX RECORDS
REMARK 295
REMARK 295 REMARK:
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REMARK 295
REMARK 295 NON-CRYSTALLOGRAPHIC SYMMETRY
REMARK 295 THE TRANSFORMATIONS PRESENTED ON THE MTRIX RECORDS BELOW
REMARK 295 DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG ATOMS
REMARK 295 IN THIS ENTRY. APPLYING THE APPROPRIATE MTRIX
REMARK 295 TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD
REMARK 295 APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND.
REMARK 295 CHAIN IDENTIFIERS GIVEN AS "?" REFER TO CHAINS FOR WHICH
REMARK 295 ATOMS ARE NOT FOUND IN THIS ENTRY.
REMARK 295
REMARK 295 APPLIED TO TRANSFORMED TO
REMARK 295 TRANSFORM CHAIN RESIDUES CHAIN RESIDUES RMSD
REMARK 295 SSS
REMARK 295 M 1 A 1 .. 374 C 1 .. 374 0.010
REMARK 295 M 2 B 1 .. 374 D 1 .. 374 0.010
REMARK 295
REMARK 295 WHERE SSS -> COLUMNS 8-10 OF MTRIX RECORDS
REMARK 295
REMARK 295 REMARK:
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