wwPDB
PDB FORMAT Version 2.3
Main Index
REMARK 300
REMARK 350
REMARK 375
REMARK 400
REMARK 450
REMARK 465
REMARK 470
REMARK 500
REMARK 525
REMARK 550
REMARK 600
REMARK 650
REMARK 700
REMARK 750
REMARK 800
REMARK 860
REMARK 900
REMARK 999


REMARK 300, Biomolecule

Description of the biologically functional molecule (biomolecule) in free text.

Remark 300 is mandatory if Remark 350 is provided.

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REMARK 300
REMARK 300 BIOMOLECULE:
REMARK 300 THIS ENTRY CONTAINS THE UNIQUE NON-CRYSTALLOGRAPHIC VIRAL
REMARK 300 REPEAT UNIT, WHICH CONSISTS OF ? CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 300
REMARK 300  free text

Example (for Cryo-Electron Microscopy)

REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE UNIQUE NON-CRYSTALLOGRAPHIC VIRAL
REMARK 300 REPEAT UNIT, WHICH CONSISTS OF 12 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 300
REMARK 300 ASSEMBLY COMPONENTS
REMARK 300   COM_ID: 1;
REMARK 300    NAME: ENTEROBACTERIA PHAGE PRD1 SUS1 MUTANT;
REMARK 300    OTHER_DETAILS: VIRUS;
REMARK 300
REMARK 300 VIRUS PARTICULARS
REMARK 300   COM_ID: 1;
REMARK 300    VIRUS_HOST_CATEGORY:  BACTERIA ;
REMARK 300    VIRUS_HOST_SPECIES: ENTEROBACTERIA ;
REMARK 300    VIRUS_HOST_GROWTH_CELL: NULL ;
REMARK 300    VIRUS_TYPE: VIRUS;
REMARK 300    VIRUS_ISOLATE: SPECIES ;
REMARK 300    ICTVDB_ID: 68.0.1.0.001
REMARK 300
REMARK 300 THE VIRUS PARTICLE HAS AN ICOSAHEDRALLY ARRANGED OUTER PROTEIN
REMARK 300 COAT. EACH CAPSID ICOSAHEDRAL ASYMMETRIC UNIT CONTAINS FOUR
REMARK 300 INDEPENDENT COPIES OF THE P3 TRIMER.
REMARK 300

REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF   2 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 300
REMARK 300 QUATERNARY STRUCTURE FOR THIS ENTRY: DIMERIC
REMARK 300
REMARK 300 FOR THE HOMO-ASSEMBLY DESCRIBED BY REMARK 350
REMARK 300 THE DIFFERENCE IN ACCESSIBLE SURFACE AREA PER
REMARK 300 CHAIN BETWEEN THE ISOLATED CHAIN AND THAT FOR
REMARK 300 THE CHAIN IN THE COMPLEX IS     2498.4 ANGSTROM**2

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REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 6 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 300
REMARK 300 THE CATALYTIC SUBUNIT OF LIVER ALCOHOL DEHYDROGENASE FROM
REMARK 300 EQUUS CABALLUS IS A HOMO DIMER.


REMARK 350, Generating the Biomolecule

Remark 350 presents all transformations, both crystallographic and non-crystallographic, needed to generate the biomolecule. These transformations operate on the coordinates in the entry.

Remark 350 is mandatory if Remark 300 is provided.

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REMARK 350  
REMARK 350 GENERATING THE BIOMOLECULE
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: ?
REMARK 350 APPLY THE FOLLOWING TO CHAINS: ?, ?...
REMARK 350   BIOMT1   N  N.NNNNNN  N.NNNNNN  N.NNNNNN        N.NNNNN
REMARK 350   BIOMT2   N  N.NNNNNN  N.NNNNNN  N.NNNNNN        N.NNNNN
REMARK 350   BIOMT3   N  N.NNNNNN  N.NNNNNN  N.NNNNNN        N.NNNNN 

Example

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REMARK 350  
REMARK 350 GENERATING THE BIOMOLECULE
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 APPLY THE FOLLOWING TO CHAINS: A, B, 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 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000       60.00000
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000     -120.00000
REMARK 350   BIOMT3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F
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   4  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000       60.00000
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   5 -1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   5  0.000000 -1.000000  0.000000     -120.00000
REMARK 350   BIOMT3   5  0.000000  0.000000  1.000000        0.00000

(NOTE Identity matrix in BIOMT is mandatory)

REMARK 350  
REMARK 350 GENERATING THE BIOMOLECULE
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 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J, K, L
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 -0.500000 -0.865983  0.000000        0.00000
REMARK 350   BIOMT2   2  0.866068 -0.500000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000


REMARK 375, Special Position

Remark 375 specifies atoms that are known to lie in particular locations, related by the symmetry elements, at which objects may be placed if and only if they possess symmetry which coincides with that of the cell.

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REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 FREE TEXT GOES HERE. 

Example

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REMARK 375                                                            
REMARK 375 SPECIAL POSITION                                           
REMARK 375      HOH   301  LIES ON A SPECIAL POSITION.                 
REMARK 375      HOH    77  LIES ON A SPECIAL POSITION.                 
REMARK 375                                                         
REMARK 375 SPECIAL POSITION                                        
REMARK 375 MG   MO4 A  10  LIES ON A SPECIAL POSITION.              
REMARK 375      HOH A  13  LIES ON A SPECIAL POSITION.              
REMARK 375      HOH A  28  LIES ON A SPECIAL POSITION.              
REMARK 375      HOH A  36  LIES ON A SPECIAL POSITION.              


REMARK 400, Compound

Further details on the macromolecular contents of the entry.

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REMARK 400
REMARK 400 COMPOUND
REMARK 400 FREE TEXT GOES HERE.

Example

REMARK 400
REMARK 400 COMPOUND
REMARK 400 THE PRD1 SUS1 MUTANT LACKS THE PACKAGING PROTEIN P9
REMARK 400 AND PRODUCES ONLY EMPTY PARTICLES, WHICH REPRESENT
REMARK 400 AN ASSEMBLY INTERMEDIATE (MINDICH, L. ET AL.,
REMARK 400 J. VIROL 44, 1013-1020 (1982); MINDICH, L. ET AL.,
REMARK 400 J. VIROL 44, 1021-1030 (1982)).

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REMARK 400
REMARK 400 COMPOUND
REMARK 400  COMPONENT OF NAPHTHALENE DIOXYGENASE (NDO)
REMARK 400  MULTICOMPONENT ENZYME SYSTEM WHICH CATALYZES THE INCORPORATION 
REMARK 400  OF BOTH ATOMS OF MOLECULAR OXYGEN INTO NAPHTHALENE TO FORM
REMARK 400  CIS-NAPHTHALENE DIHYDRODIOL.
REMARK 400
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ARG 270 TO GLY


REMARK 450, Source

Further details on the biological source of the macromolecular contents of the entry.

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REMARK 450
REMARK 450 SOURCE
REMARK 450 FREE TEXT GOES HERE.


REMARK 465, Missing residues

Remark 465 lists the residues that are present in the SEQRES records but are not present in the coordinates section.

Template

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 470, Missing Atom

Non-hydrogen atoms of standard residues which are missing from the coordinates are listed. Missing HETATMS are not listed here.

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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                                       

Example

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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     ARG A 412    CG   CD   NE   CZ   NH1  NH2               
REMARK 470     ARG A 456    CG   CD   NE   CZ   NH1  NH2               
REMARK 470     GLU A 486    CG   CD   OE1  OE2                         
REMARK 470     GLU A 547    CG   CD   OE1  OE2                         
REMARK 470     GLU A 548    CG   CD   OE1  OE2                         
REMARK 470     LYS A 606    CG   CD   CE   NZ                          
REMARK 470     ARG B 456    CG   CD   NE   CZ   NH1  NH2               
REMARK 470     ASP B 484    CG   OD1  OD2                              
REMARK 470     GLN B 485    CG   CD   OE1  NE2                         
REMARK 470     GLU B 486    CG   CD   OE1  OE2                         
REMARK 470     ARG B 490    CG   CD   NE   CZ   NH1  NH2               
REMARK 470     GLU B 522    CG   CD   OE1  OE2                         
REMARK 470     ARG B 576    CG   CD   NE   CZ   NH1  NH2               
REMARK 470     ASP B 599    CG   OD1  OD2


REMARK 500, Geometry and Stereochemistry

Further details on the stereochemistry of the structure. This remark is generated by PDB, but may also be provided by the depositor. Additional subtopics may be added as needed.

Subtopic: Close Contacts
Subtopic: Close Contacts In Same Asymmetric Unit
Subtopic: Chiral Centers
Subtopic: Covalent Bond Angles
Subtopic: Torsion Angles
Subtopic: Covalent Bond Lengths

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REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY 
REMARK 500 SUBTOPIC: 
REMARK 500 
REMARK 500 FREE TEXT GOES HERE.

Subtopic: Close Contacts

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REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC 
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  SOME OF THESE MAY BE ATOMS
REMARK 500 LOCATED ON SPECIAL POSITIONS IN THE CELL.
REMARK 500
REMARK 500 DISTANCE CUTOFF: 2.2 ANGSTROMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   CB   LEU D    68  -  CE   LYS E    76     1656     2.10
REMARK 500   CB   THR D   173  -  O    HOH    1151     4455     1.73
REMARK 500   O    HOH    1151  -  CB   THR D   173     4566     1.73
REMARK 500   CZ   ARG D    64  -  O    HOH    1422     3656     1.75 

Subtopic: Close Contacts In Same Asymmetric Unit

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   O    HOH     761  -  O    ARG      17              1.89
REMARK 500   O    HOH     806  -  N    ARG      88              1.46

Subtopic: Non-Cis, Non-Trans

 
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REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 VAL A  123    GLN A  124          0       221.48
REMARK 500 VAL B  123    GLN B  124          0       222.43

Subtopic: Chiral Centers

 
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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) (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,A12)
REMARK 500
REMARK 500    M RES CSSEQI
REMARK 500    0 GLU       1       
REMARK 500    0 GLU       1       
REMARK 500    0 GLU       1       

Subtopic: Covalent Bond Angles

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REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES 
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (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,A1,3(2X,A4,17X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500  0 ASP     3   C-1 -  N   -  CA  ANGL. DEV. =  21.7 DEGREES

Subtopic: Torsion Angles

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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  M RES CSSEQI        PSI       PHI
REMARK 500  0 VAL    26     -174.85   -134.80
REMARK 500  0 MET    61       46.11   -176.53

Subtopic: Covalent Bond Lengths

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REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD AND BY MORE THAN 0.150 ANGSTROMS (M=MODEL                
REMARK 500 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE          
REMARK 500 NUMBER; I=INSERTION CODE).                                           
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,1X,2(A4,A1,3X),12X,F5.3)           
REMARK 500                                                                      
REMARK 500 EXPECTED VALUESS: ENGH AND HUBER, 1991                               
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    LYS A  24  CB     LYS A  24  CG       0.269                       
REMARK 500    LYS A 109  CD     LYS A 109  CE      -0.251                       
REMARK 500    GLU B  39  CG     GLU B  39  CD       0.158                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL


REMARK 525, Solvent

Remarks specific to the solvent molecules of the entry.

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REMARK 525
REMARK 525 SOLVENT
REMARK 525 FREE TEXT GOES HERE. 

Example

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REMARK 525
REMARK 525 SOLVENT
REMARK 525 MANY OF THE WATER MOLECULES APPEAR TO BE ASSOCIATED WITH
REMARK 525 A SYMMETRY-RELATED MOLECULE. 

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REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES ARE GIVEN CHAIN IDENTIFIERS TO
REMARK 525 INDICATE THE PROTEIN CHAIN TO WHICH THEY ARE MOST CLOSELY
REMARK 525 ASSOCIATED WITH:
REMARK 525   PROTEIN CHAIN  SOLVENT CHAIN
REMARK 525     A              Z
REMARK 525     B              Y
REMARK 525
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 THESE MOLECULES CAN BE PLACED WITHIN  5.00 ANGSTROM OF THE
REMARK 525 OBSERVED OLIGOMER BY APPLYING THE SYMMETRY TRANSFORMATION
REMARK 525 INDICATED.
REMARK 525
REMARK 525  M RES CSSEQI     ORIGINAL COORDINATES   SYMMETRY TRANS.    DIST.
REMARK 525                    X       Y       Z
REMARK 525  1 HOH Z 197   -23.309 -18.431  27.821    002      456      2.85
REMARK 525  1 HOH Z  64   -18.204 -18.469   0.503    002      455      2.91
REMARK 525  1 HOH Z 236   -18.883 -15.861  -2.863    002      455      2.13
REMARK 525  1 HOH Z 185   -28.011   5.875  32.170    001      554      2.60

REMARK 525
REMARK 525 SOLVENT
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525 
REMARK 525  M RES CSSEQI                                            
REMARK 525  0 HOH    561      DISTANCE =  5.07 ANGSTROMS            
REMARK 525  0 HOH    791      DISTANCE =  5.08 ANGSTROMS

REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES ARE GIVEN CHAIN IDENTIFIERS TO
REMARK 525 INDICATE THE PROTEIN CHAIN TO WHICH THEY ARE MOST CLOSELY
REMARK 525 ASSOCIATED WITH:
REMARK 525   PROTEIN CHAIN  SOLVENT CHAIN
REMARK 525     A              Z
REMARK 525     B              Y


REMARK 550, SEGID (deprecated)

This record has been deprecated.


REMARK 600, Heterogen

Further details on the heterogens in the entry.

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REMARK 600
REMARK 600 HETEROGEN
REMARK 600 FREE TEXT GOES HERE.

Example

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REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600
REMARK 600 FOR METAL ATOM MG    MG A1192  THE COORDINATION ANGLES ARE:
REMARK 600  1 HOH    157Z  O
REMARK 600  2 ASP    144A  OD2       87.3
REMARK 600  3 ADP   1190A  O3B       94.6  87.9
REMARK 600  4 ASP    173A  OD1       88.0  90.6 176.9
REMARK 600  5 HOH    199Z  O         85.1 172.1  90.7  91.2
REMARK 600  6 ADP   1190A  O1A      167.1 105.4  88.0  89.8  82.3
REMARK 600                             1     2     3     4     5
REMARK 600
REMARK 600 HETGROUPS RENAMED OR RENUMBERED
REMARK 600 PRIMARY PUBLICATION            THIS ENTRY
REMARK 600        CA 1 W                   CA B2326
REMARK 600       GOL 2 W                  GOL A1327
REMARK 600       GOL 3 W                  GOL A1328
REMARK 600       GOL 4 W                  GOL B1326
REMARK 600       GOL 5 W                  GOL B1327


REMARK 650, Helix

Further details on the helix contents of the entry.

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REMARK 650
REMARK 650 HELIX
REMARK 650 FREE TEXT GOES HERE.

Example

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REMARK 650                                                            
REMARK 650 HELIX                                                      
REMARK 650 DETERMINATION METHOD: KDSSP                                
REMARK 650 THE MAJOR DOMAINS ARE: "N" FOR N-TERMINAL DOMAIN, "B" FOR  
REMARK 650 BETA-BARREL DOMAIN, AND "C" FOR C-TERMINAL DOMAIN. "F"     
REMARK 650 REFERS TO THE ACTIVE SITE FLAP.  ALPHA HELICES ARE NAMED   
REMARK 650 WITH TWO CHARACTERS, THE FIRST REFERRING TO THE DOMAIN     
REMARK 650 IN WHICH THEY OCCUR. 

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REMARK 650                                                            
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.


REMARK 700, Sheet

Further details on the sheet contents of the structure. Several standard templates are shown.

Template

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REMARK 700
REMARK 700 SHEET
REMARK 700 FREE TEXT GOES HERE. 
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD:                                 
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED.  IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, 
REMARK 700 TWO SHEETS ARE DEFINED.  STRANDS N1, N2, N3 AND N4 OF SHEET
REMARK 700 XXX AND XXX ARE IDENTICAL. 

REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD:                                 
REMARK 700 THE SHEET PRESENTED AS XXX ON SHEET RECORDS BELOW IS
REMARK 700 ACTUALLY AN N-STRANDED BETA-BARREL.  THIS IS
REMARK 700 REPRESENTED BY A N+1-STRANDED SHEET IN WHICH THE FIRST AND
REMARK 700 LAST STRANDS ARE IDENTICAL. 

REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD:                                 
REMARK 700 THERE ARE SEVERAL BIFURCATED SHEETS IN THIS STRUCTURE. 
REMARK 700 EACH IS REPRESENTED BY TWO SHEETS WHICH HAVE ONE OR MORE
REMARK 700 IDENTICAL STRANDS. 
REMARK 700 SHEETS XXX AND XXX REPRESENT ONE BIFURCATED SHEET. 
REMARK 700 SHEETS XXX AND XXX REPRESENT ONE BIFURCATED SHEET. 

N1, N2, N3 and N4 represent strand numbers, and XXX represents sheet identifiers.

When the remark for several bifurcated sheets is used, its last line is repeated for the appropriate number of bifurcated sheets, as shown in the last template above.

Example

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REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED.  IN   
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS are defined.  STRANDS 3, 4, AND 5 
REMARK 700 OF SHEET *B2A* AND *B2B* ARE IDENTICAL.  STRANDS 3, 4, AND
REMARK 700 5 OF SHEET *B2C* AND *B2D* ARE IDENTICAL.                 
REMARK 700                                                           
REMARK 700 SHEET
REMARK 700 STRANDS 1 TO 4 OF THE BETA-SHEET HAVE GREEK-KEY TOPOLOGY. 
REMARK 700 THE SHEET FORMS A FIVE-STRANDED BETA-BARREL WITH BULGES IN 
REMARK 700 STRANDS 3 AND 5.  IN ORDER TO REPRESENT THIS FEATURE IN THE
REMARK 700 SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.               

REMARK 700                                                            
REMARK 700 SHEET                                                      
REMARK 700 THE SHEET PRESENTED AS S5 ON SHEET RECORDS BELOW IS        
REMARK 700 ACTUALLY A 6-STRANDED BETA-BARREL.  THIS IS                
REMARK 700 REPRESENTED BY A 7-STRANDED SHEET IN WHICH THE FIRST AND   
REMARK 700 LAST STRANDS ARE IDENTICAL.                                

REMARK 700                                                            
REMARK 700 SHEET                                                      
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.


REMARK 750, Turn

Further details on the turns.

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REMARK 750
REMARK 750 TURN
REMARK 750 FREE TEXT GOES HERE.

Example

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REMARK 750
REMARK 750 TURN
REMARK 750  TURN_ID: T4, TYPE I (ONE OR MORE OF THE PHI, PSI ANGLES    
REMARK 750  DEVIATE BY MORE THAN PLUS,MINUS 45 DEGREES FROM THE IDEAL  
REMARK 750  VALUES USED BY WILMOT & THORNTON(1989)). 
REMARK 750                                                             
REMARK 750  TURN_ID: T10, TYPE I (ONE OR MORE OF THE PHI, PSI ANGLES   
REMARK 750  DEVIATE BY MORE THAN PLUS,MINUS 45 DEGREES FROM THE IDEAL  
REMARK 750  VALUES USED BY WILMOT & THORNTON(1989)). 
REMARK 750                                                             
REMARK 750  TURN_ID: T16, TYPE VIII (ONE OR MORE OF THE PHI, PSI       
REMARK 750  ANGLES DEVIATE BY MORE THAN PLUS,MINUS 45 DEGREES FROM     
REMARK 750  THE IDEAL VALUES USED BY WILMOT & THORNTON(1989)). 


REMARK 800, Site

Further details on the site contents of the entry. Remark 800 is mandatory if site records exist.

Template

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REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: FREE TEXT GOES HERE.
REMARK 800 SITE_DESCRIPTION: FREE TEXT GOES HERE.

Example

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REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: RCA
REMARK 800 SITE_DESCRIPTION: DESIGNATED RECOGNITION REGION IN PRIMARY
REMARK 800 REFERENCE.  PROPOSED TO AFFECT SUBSTRATE SPECIFICITY.      
REMARK 800
REMARK 800 SITE_IDENTIFIER: RCB                                       
REMARK 800 SITE_DESCRIPTION: DESIGNATED RECOGNITION REGION IN PRIMARY 
REMARK 800  REFERENCE.  PROPOSED TO AFFECT SUBSTRATE SPECIFICITY.     


REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: BAT BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: CA BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: CA BINDING SITE FOR CHAIN A


REMARK 860, Correction, After Release

Further details on corrections that have been made to the PDB entry, as referred to in the REVDAT record.

Template

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REMARK 860
REMARK 860 CORRECTION AFTER RELEASE
REMARK 860 FREE TEXT GOES HERE.

Example

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REMARK 860
REMARK 860 CORRECTION
REMARK 860 CORRECT RESIDUE IDENTIFICATION ON SITE RECORDS.  ADD       
REMARK 860 RESIDUE TO SITE RECORDS.  15-JUL-81.                       
REMARK 860                                                            
REMARK 860 CORRECT DATES IN REMARKS 7 AND 16. 15-JAN-82.    
REMARK 860                                                            
REMARK 860 CORRECT ATOM NAME FOR ATOM 6 FROM CG2 TO CG1.  07-MAR-83.  
REMARK 860                                                            
REMARK 860 CHANGE RESIDUE 122 FROM ASN TO ASP.  ADD REFERENCE.        
REMARK 860  12-MAY-83.                                      
REMARK 860                                                            
REMARK 860 INSERT REVDAT RECORDS. 30-SEP-83.              
REMARK 860                                                            
REMARK 860 CORRECT CODEN FOR REFERENCE 1.  27-OCT-83.     


REMARK 900, Related Entries

This remark gives ID codes of PDB files related to the entry. These may include coordinate entries deposited as a related set, the structure factor or NMR restraint file related to the entry, or the file containing the biologically functional molecule ("biomolecule") generated by the PDB from symmetry records.

Template

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REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 FREE TEXT GOES HERE.

Example

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REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 THE BIOMOLECULE RELATED TO THIS ENTRY HAS BEEN GENERATED
REMARK 900 AND IS AVAILABLE AS PDB FILE BIO1ABC.PDB
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 THE STRUCTURE FACTORS FOR THIS EXPERIMENT ARE AVAILABLE AS
REMARK 900 PDB FILE R1ABCSF.ENT

REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 THE LIST OF EXPERIMENTAL RESTRAINTS IS AVAILABLE AS PDB
REMARK 900 FILE 1ABC.MR

REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 THE BIOMOLECULE IS AVAILABLE AS PDB FILE BIO1ABC.PDB
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2CKI   RELATED DB: PDB
REMARK 900  STRUCTURE OF ULILYSIN, A MEMBER OF THE
REMARK 900  PAPPALYSIN FAMILY OF METZINCIN
REMARK 900  METALLOENDOPEPTIDASES.


REMARK 999 Sequence

Further details on the sequence.

For cases where there are gaps in the structure as reflected in missing ATOM records missing N- terminus and C-terminus residues are delineated in REMARK 999 records, whereas internal structural gaps are represented in SEQADV records. Several cases must be considered when evaluating these REMARK 999 records:

  • The missing N-terminus atoms are not found in the ATOM record as they represent precursor sequence and are not found in the mature protein.
  • The missing N-terminus residues were not found in the density map. Although PDB will attempt to flag these as SEQADV records, we cannot guarantee that they will always be handled uniformly. The primary reason for this inconsistency is that in a number of cases, neither PDB nor the depositors, are certain where chains start and end.
  • Template

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    REMARK 999
    REMARK 999 SEQUENCE
    REMARK 999 FREE TEXT GOES HERE.
    

    Example

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    REMARK 999                                                            
    REMARK 999 SEQUENCE                                                   
    REMARK 999                                                            
    REMARK 999  REFERENCE                                                 
    REMARK 999   REFERENCE: PETRA, ET AL., (1971) BIOCHEMISTRY 10, PP     
    REMARK 999   4023-4025.                                               
    REMARK 999                                                            
    REMARK 999   SHOHAM, G., NECHUSHTAI, R., STEPPUN, J.,NELSON, H.,      
    REMARK 999   NELSON N., UNPUBLISHED RESULTS.                          
    REMARK 999                                                            
    REMARK 999   LE HUEROU,I., GUILLOTEAU P., TOULLEC, R., PUIGSERVER, A.,
    REMARK 999   WICKER,C., (1991) BIOCHEMICAL, BIOPHYSICAL RESEARCH      
    REMARK 999   COMM., 175, PP 110 - 116.                                
    REMARK 999                                                            
    REMARK 999 THE SEQUENCE USED IS THAT PROVIDED BY THE CDNA, WHICH      
    REMARK 999 CORRECTS SEVERAL ASP/ASN AND GLU/GLN MISASSIGNMENTS.       
    REMARK 999                                                            
    REMARK 999 SEQUENCE                                                   
    REMARK 999 MET A    1  - MET A    1  - MISSING FROM SWS    P10599     
    REMARK 999                                                            
    REMARK 999 THR AT POSITION 74 WAS FOUND BY WOLMAN ET AL., JOURNAL OF  
    REMARK 999 BIOCHEMISTRY 263, 15506 (1988).                            
    
    REMARK 900
    REMARK 900 RELATED ENTRIES
    REMARK 900 RELATED ID: 1CJD   RELATED DB: PDB
    REMARK 900  THE BACTERIOPHAGE PRD1 COAT PROTEIN, P3, IS
    REMARK 900  STRUCTURALLY SIMILAR TO HUMAN ADENOVIRUS HEXON
    REMARK 900 RELATED ID: 1HB5   RELATED DB: PDB
    REMARK 900  QUASI-ATOMIC RESOLUTION MODEL OF BACTERIOPHAGE
    REMARK 900  PRD1 P3-SHELL, OBTAINED BY COMBINED CRYO-
    REMARK 900  EM AND X-RAY CRYSTALLOGRAPHY.
    


    2007 wwPDB