| PDB FORMAT Version 2.3 |
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)). 1234567890123456789012345678901234567890123456789012345678901234567890 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 1.46Subtopic: 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.
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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.
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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.
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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.
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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.
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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.
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REMARK 860
REMARK 860 CORRECTION AFTER RELEASE
REMARK 860 FREE TEXT GOES HERE.
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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.
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REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 FREE TEXT GOES HERE.
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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:
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REMARK 999
REMARK 999 SEQUENCE
REMARK 999 FREE TEXT GOES HERE.
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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.
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