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PDBsum entry 1unj

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DNA/antibiotic PDB id
1unj
Jmol
Contents
Protein chains
(+ 2 more) 11 a.a.
DNA/RNA
Waters ×14
HEADER    DNA/ANTIBIOTIC                          10-SEP-03   1UNJ
TITLE     CRYSTAL STRUCTURE OF A 7-AMINOACTINOMYCIN D COMPLEX WITH
TITLE    2 NON-COMPLEMENTARY DNA
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: 5'-D(*TP*TP*AP*GP*BRU*TP)-3';
COMPND   3 CHAIN: A, B, C, D, G, H, I, J, M, N, O, P, S, T, U, V;
COMPND   4 MOL_ID: 2;
COMPND   5 MOLECULE: 7-AMINO-ACTINOMYCIN D;
COMPND   6 CHAIN: E, F, K, L, Q, R, W, X;
COMPND   7 SYNONYM: DACTINOMYCIN
SOURCE    MOL_ID: 1;
SOURCE   2 SYNTHETIC: YES;
SOURCE   3 MOL_ID: 2;
SOURCE   4 SYNTHETIC: YES;
SOURCE   5 ORGANISM_SCIENTIFIC: STREPTOMYCES ANTIBIOTICUS;
SOURCE   6 ORGANISM_TAXID: 1890
KEYWDS    ACTINOMYCIN D, ACTINOMYCIN, ANTIBIOTIC, ANTI CANCER, ANTITUMOR,
KEYWDS   2 CHROMOPHORE, DEPSIPEPTIDE, DNA-ANTIBIOTIC COMPLEX, FLUORESCENT
KEYWDS   3 AGENT, HOOGSTEN BASE-PAIR
EXPDTA    X-RAY DIFFRACTION
AUTHOR    E.C.ALEXOPOULOS,R.KLEMENT,E.A.JARES-ERIJMAN,I.USON,T.M.JOVIN,
AUTHOR   2 G.M.SHELDRICK
REVDAT   5   20-JUL-11 1UNJ    1       TITLE  REVDAT REMARK SEQADV
REVDAT   4   13-JUL-11 1UNJ    1       VERSN
REVDAT   3   24-FEB-09 1UNJ    1       VERSN
REVDAT   2   06-APR-05 1UNJ    1       JRNL
REVDAT   1   16-DEC-04 1UNJ    0
JRNL        AUTH   E.C.ALEXOPOULOS,E.A.JARES-ERIJMAN,T.M.JOVIN,R.KLEMENT,
JRNL        AUTH 2 R.MACHINEK,G.M.SHELDRICK,I.USON
JRNL        TITL   CRYSTAL AND SOLUTION STRUCTURES OF 7-AMINO-ACTINOMYCIN D
JRNL        TITL 2 COMPLEXES WITH D(TTAGBRUT), D(TTAGTT) AND D(TTTAGTTT)
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  61   407 2005
JRNL        REFN                   ISSN 0907-4449
JRNL        PMID   15805595
JRNL        DOI    10.1107/S090744490500082X
REMARK   2
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : SHELXL-97
REMARK   3   AUTHORS     : G.M.SHELDRICK
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.5
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99
REMARK   3   CROSS-VALIDATION METHOD           : R FREE
REMARK   3   FREE R VALUE TEST SET SELECTION   : IN THIN SHELLS
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.2760
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.3163
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 577
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 11527
REMARK   3
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : NULL
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.2576
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.2962
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 13.2
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 501
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 9358
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS      : 0
REMARK   3   NUCLEIC ACID ATOMS : 1183
REMARK   3   HETEROGEN ATOMS    : 1048
REMARK   3   SOLVENT ATOMS      : 14
REMARK   3
REMARK   3  MODEL REFINEMENT.
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 2236.88
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 0.0
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 0
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 8996
REMARK   3   NUMBER OF RESTRAINTS                     : 17002
REMARK   3
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK   3   BOND LENGTHS                         (A) : 0.005
REMARK   3   ANGLE DISTANCES                      (A) : 0.015
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.029
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.159
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : NULL
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.003
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.004
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : NULL
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.002
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED: NULL
REMARK   3
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER
REMARK   3   SPECIAL CASE: NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1UNJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-OCT-03.
REMARK 100 THE PDBE ID CODE IS EBI-13477.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 15-JUL-02
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 5.60
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG
REMARK 200  BEAMLINE                       : BW7A
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9050,0.9196,0.9204
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : NULL
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11527
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0
REMARK 200  DATA REDUNDANCY                : 10.150
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 6.5700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.60
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.3
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.37
REMARK 200  R MERGE FOR SHELL          (I) : 0.48000
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 5.270
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHELXD
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS  (%): 40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NA.CITRATE PH 5.6,
REMARK 280  NA.ACETATE,(NH4)2SO4,HANGING DROP,T 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+2/3
REMARK 290       3555   -X+Y,-X,Z+1/3
REMARK 290       4555   Y,X,-Z
REMARK 290       5555   X-Y,-Y,-Z+1/3
REMARK 290       6555   -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       72.26667
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       36.13333
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       36.13333
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       72.26667
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DODECAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350                    AND CHAINS: 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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DODECAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, N, O, P, Q, R, S, T, U,V,
REMARK 350                    AND CHAINS: W, X
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 400
REMARK 400 COMPOUND
REMARK 400 ACTINOMYCIN D IS A BICYCLIC PEPTIDE, A MEMBER OF THE
REMARK 400 ACTINOMYCIN FAMILY.
REMARK 400 HERE, ACTINOMYCIN D IS REPRESENTED BY THE SEQUENCE (SEQRES)
REMARK 400
REMARK 400  GROUP: 1
REMARK 400   NAME: ACTINOMYCIN D
REMARK 400   CHAIN: E, F, K, L, Q, R, W, X
REMARK 400   COMPONENT_1: PEPTIDE LIKE SEQUENCE RESIDUES 1 TO 11
REMARK 400   DESCRIPTION: ACTINOMYCIN D CONSISTS OF TWO PENTAMER
REMARK 400                RINGS LINKED BY THE CHROMOPHORE (PX1)
REMARK 400                THE CHROMOPHORE PX1 IS A MODIFIED PXZ WITH
REMARK 400                C-NH2 REPLACING C-H IN POSITION 7 OF THE
REMARK 400                PHENOXAZONE RING.
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 465      DT A     1
REMARK 465      DT B     1
REMARK 465      DT B     2
REMARK 465      DT C     1
REMARK 465      DT D     1
REMARK 465      DT G     1
REMARK 465      DT H     1
REMARK 465      DT H     2
REMARK 465      DT I     1
REMARK 465      DT J     1
REMARK 465      DT M     1
REMARK 465      DT N     1
REMARK 465      DT O     1
REMARK 465      DT P     1
REMARK 465      DT S     1
REMARK 465      DT T     1
REMARK 465      DT U     1
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      DT C   6    C5'  C4'  O4'  C3'  C2'  C1'  N1   C2
REMARK 470      DT C   6    O2   N3   C4   O4   C5   C7   C6
REMARK 470      DT G   2    O5'
REMARK 470      DT I   6    O5'  C5'  C4'  O4'  C3'  C2'  C1'  N1
REMARK 470      DT I   6    C2   O2   N3   C4   O4   C5   C7   C6
REMARK 470      DT J   2    O5'
REMARK 470      DT N   2    O5'  C5'  C4'  O4'  C3'  C2'  C1'  N1
REMARK 470      DT N   2    C2   O2   N3   C4   O4   C5   C7   C6
REMARK 470      DT O   6    O5'  C5'  C4'  O4'  C3'  C2'  C1'  N1
REMARK 470      DT O   6    C2   O2   N3   C4   O4   C5   C7   C6
REMARK 470      DT T   2    O5'  C5'  C4'  O4'  C3'  C2'  C1'  N1
REMARK 470      DT T   2    C2   O2   N3   C4   O4   C5   C7   C6
REMARK 470      DT U   2    O5'
REMARK 470      DT U   6    O5'  C5'  C4'  O4'  C3'  C2'  C1'  N1
REMARK 470      DT U   6    C2   O2   N3   C4   O4   C5   C7   C6
REMARK 470      DT V   1    O5'  C5'
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.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   O4    DT I     2     N6    DA J     3     4466     2.19
REMARK 500
REMARK 500 REMARK: NULL
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(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500     DA B   3   O4' -  C1' -  N9  ANGL. DEV. =  -4.4 DEGREES
REMARK 500     DT C   2   O4' -  C1' -  N1  ANGL. DEV. =   1.8 DEGREES
REMARK 500     DA N   3   O4' -  C1' -  N9  ANGL. DEV. =  -4.5 DEGREES
REMARK 500     DT O   2   O4' -  C1' -  N1  ANGL. DEV. =   3.3 DEGREES
REMARK 500     DT P   6   O4' -  C4' -  C3' ANGL. DEV. =  -2.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        ANGLE
REMARK 500    THR R   1        -10.57
REMARK 500
REMARK 500 REMARK: NULL
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) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    DVA E   8       -24.6      D          D   OUTSIDE RANGE
REMARK 500    MVA E  11        22.9      L          L   OUTSIDE RANGE
REMARK 500    DVA K   8       -21.5      D          D   OUTSIDE RANGE
REMARK 500    MVA K  11        24.3      L          L   OUTSIDE RANGE
REMARK 500    MVA Q  11        25.0      L          L   OUTSIDE RANGE
REMARK 500    DVA W   8       -24.3      D          D   OUTSIDE RANGE
REMARK 500    MVA W  11        24.6      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN E OF 7-AMINO-ACTINOMYCIN D
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN F OF 7-AMINO-ACTINOMYCIN D
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN K OF 7-AMINO-ACTINOMYCIN D
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN L OF 7-AMINO-ACTINOMYCIN D
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN Q OF 7-AMINO-ACTINOMYCIN D
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN R OF 7-AMINO-ACTINOMYCIN D
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN W OF 7-AMINO-ACTINOMYCIN D
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN X OF 7-AMINO-ACTINOMYCIN D
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1A7Z   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF ACTINOMYCIN Z3
REMARK 900 RELATED ID: 209D   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF N8-ACTINOMYCIN D COMPLEXED WITH
REMARK 900  D(GAAGCTTC)2
REMARK 900 RELATED ID: 1UNM   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF 7-AMINOACTINOMYCIN D COMPLEXED
REMARK 900  WITH NON-COMPLEMENTARY DNA
REMARK 900 RELATED ID: 1I3W   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF ACTINOMYCIN D COMPLEXED WITH
REMARK 900  DNA (CGATCGATCG)2
REMARK 900 RELATED ID: 1A7Y   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF ACTINOMYCIN D
REMARK 900 RELATED ID: 1FJA   RELATED DB: PDB
REMARK 900  SOLUTION STRUCTURE OF ACTINOMYCIN D COMPLEXED WITH
REMARK 900  DNA (AAGCGCTT)2
REMARK 900 RELATED ID: 173D   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF ACTINOMYCIN D COMPLEXED WITH
REMARK 900  DNA (GAAGCTTC)2
REMARK 900 RELATED ID: 2D55   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF ACTINOMYCIN D COMPLEXED WITH
REMARK 900  DNA (GAAGCTTC)2
REMARK 900 RELATED ID: 1DSC   RELATED DB: PDB
REMARK 900  SOLUTION STRUCTURE OF ACTINOMYCIN D COMPLEXED WITH
REMARK 900  DNA (GAAGCTTC)2
REMARK 900 RELATED ID: 1L1V   RELATED DB: PDB
REMARK 900  SOLUTION STRUCTURE OF ACTNIOMYCIN D COMPLEXED WITH
REMARK 900  MISMATCHED DNA (GTCACCGAC)
REMARK 900 RELATED ID: 316D   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF F8-ACTINOMYCIN D COMPLEXED WITH
REMARK 900  DNA (GAAGCTTC)2
REMARK 900 RELATED ID: 1DSD   RELATED DB: PDB
REMARK 900  SOLUTION STRUCTURE OF ACTINOMYCIN D COMPLEXED WITH
REMARK 900  DNA (GATGCTTC)2
REMARK 900 RELATED ID: 1MNV   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF ACTINOMYCIN D COMPLEXED WITH
REMARK 900  DNA (ATGCTGCAT)2
REMARK 900 RELATED ID: 1OVF   RELATED DB: PDB
REMARK 900  SOLUTIOM STRUCTURE OF ACTINOMYCIN D COMPLEXED WITH
REMARK 900  DNA (CCGTTTTGTGG)2
REMARK 900 RELATED ID: 1QFI   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF ACTINOMYCIN X2
DBREF  1UNJ A    1     6  PDB    1UNJ     1UNJ             1      6
DBREF  1UNJ B    1     6  PDB    1UNJ     1UNJ             1      6
DBREF  1UNJ C    1     6  PDB    1UNJ     1UNJ             1      6
DBREF  1UNJ D    1     6  PDB    1UNJ     1UNJ             1      6
DBREF  1UNJ G    1     6  PDB    1UNJ     1UNJ             1      6
DBREF  1UNJ H    1     6  PDB    1UNJ     1UNJ             1      6
DBREF  1UNJ I    1     6  PDB    1UNJ     1UNJ             1      6
DBREF  1UNJ J    1     6  PDB    1UNJ     1UNJ             1      6
DBREF  1UNJ M    1     6  PDB    1UNJ     1UNJ             1      6
DBREF  1UNJ N    1     6  PDB    1UNJ     1UNJ             1      6
DBREF  1UNJ O    1     6  PDB    1UNJ     1UNJ             1      6
DBREF  1UNJ P    1     6  PDB    1UNJ     1UNJ             1      6
DBREF  1UNJ S    1     6  PDB    1UNJ     1UNJ             1      6
DBREF  1UNJ T    1     6  PDB    1UNJ     1UNJ             1      6
DBREF  1UNJ U    1     6  PDB    1UNJ     1UNJ             1      6
DBREF  1UNJ V    1     6  PDB    1UNJ     1UNJ             1      6
DBREF  1UNJ E    1    11  NOR    NOR00228 NOR00228         1     11
DBREF  1UNJ F    1    11  NOR    NOR00228 NOR00228         1     11
DBREF  1UNJ K    1    11  NOR    NOR00228 NOR00228         1     11
DBREF  1UNJ L    1    11  NOR    NOR00228 NOR00228         1     11
DBREF  1UNJ Q    1    11  NOR    NOR00228 NOR00228         1     11
DBREF  1UNJ R    1    11  NOR    NOR00228 NOR00228         1     11
DBREF  1UNJ W    1    11  NOR    NOR00228 NOR00228         1     11
DBREF  1UNJ X    1    11  NOR    NOR00228 NOR00228         1     11
SEQADV 1UNJ PX1 E    6  NOR  NOR00228  PXZ     6 MODIFIED CHROMOPHORE
SEQADV 1UNJ PX1 F    6  NOR  NOR00228  PXZ     6 MODIFIED CHROMOPHORE
SEQADV 1UNJ PX1 K    6  NOR  NOR00228  PXZ     6 MODIFIED CHROMOPHORE
SEQADV 1UNJ PX1 L    6  NOR  NOR00228  PXZ     6 MODIFIED CHROMOPHORE
SEQADV 1UNJ PX1 Q    6  NOR  NOR00228  PXZ     6 MODIFIED CHROMOPHORE
SEQADV 1UNJ PX1 R    6  NOR  NOR00228  PXZ     6 MODIFIED CHROMOPHORE
SEQADV 1UNJ PX1 W    6  NOR  NOR00228  PXZ     6 MODIFIED CHROMOPHORE
SEQADV 1UNJ PX1 X    6  NOR  NOR00228  PXZ     6 MODIFIED CHROMOPHORE
SEQRES   1 A    6   DT  DT  DA  DG BRU  DT
SEQRES   1 B    6   DT  DT  DA  DG BRU  DT
SEQRES   1 C    6   DT  DT  DA  DG BRU  DT
SEQRES   1 D    6   DT  DT  DA  DG BRU  DT
SEQRES   1 G    6   DT  DT  DA  DG BRU  DT
SEQRES   1 H    6   DT  DT  DA  DG BRU  DT
SEQRES   1 I    6   DT  DT  DA  DG BRU  DT
SEQRES   1 J    6   DT  DT  DA  DG BRU  DT
SEQRES   1 M    6   DT  DT  DA  DG BRU  DT
SEQRES   1 N    6   DT  DT  DA  DG BRU  DT
SEQRES   1 O    6   DT  DT  DA  DG BRU  DT
SEQRES   1 P    6   DT  DT  DA  DG BRU  DT
SEQRES   1 S    6   DT  DT  DA  DG BRU  DT
SEQRES   1 T    6   DT  DT  DA  DG BRU  DT
SEQRES   1 U    6   DT  DT  DA  DG BRU  DT
SEQRES   1 V    6   DT  DT  DA  DG BRU  DT
SEQRES   1 E   11  THR DVA PRO SAR MVA PX1 THR DVA PRO SAR MVA
SEQRES   1 F   11  THR DVA PRO SAR MVA PX1 THR DVA PRO SAR MVA
SEQRES   1 K   11  THR DVA PRO SAR MVA PX1 THR DVA PRO SAR MVA
SEQRES   1 L   11  THR DVA PRO SAR MVA PX1 THR DVA PRO SAR MVA
SEQRES   1 Q   11  THR DVA PRO SAR MVA PX1 THR DVA PRO SAR MVA
SEQRES   1 R   11  THR DVA PRO SAR MVA PX1 THR DVA PRO SAR MVA
SEQRES   1 W   11  THR DVA PRO SAR MVA PX1 THR DVA PRO SAR MVA
SEQRES   1 X   11  THR DVA PRO SAR MVA PX1 THR DVA PRO SAR MVA
MODRES 1UNJ BRU A    5    U  URACIL MODIFIED WITH BR
MODRES 1UNJ BRU B    5    U  URACIL MODIFIED WITH BR
MODRES 1UNJ BRU C    5    U  URACIL MODIFIED WITH BR
MODRES 1UNJ BRU D    5    U  URACIL MODIFIED WITH BR
MODRES 1UNJ BRU G    5    U  URACIL MODIFIED WITH BR
MODRES 1UNJ BRU H    5    U  URACIL MODIFIED WITH BR
MODRES 1UNJ BRU I    5    U  URACIL MODIFIED WITH BR
MODRES 1UNJ BRU J    5    U  URACIL MODIFIED WITH BR
MODRES 1UNJ BRU M    5    U  URACIL MODIFIED WITH BR
MODRES 1UNJ BRU N    5    U  URACIL MODIFIED WITH BR
MODRES 1UNJ BRU O    5    U  URACIL MODIFIED WITH BR
MODRES 1UNJ BRU P    5    U  URACIL MODIFIED WITH BR
MODRES 1UNJ BRU S    5    U  URACIL MODIFIED WITH BR
MODRES 1UNJ BRU T    5    U  URACIL MODIFIED WITH BR
MODRES 1UNJ BRU U    5    U  URACIL MODIFIED WITH BR
MODRES 1UNJ BRU V    5    U  URACIL MODIFIED WITH BR
HET    BRU  A   5      20
HET    BRU  B   5      20
HET    BRU  C   5      20
HET    BRU  D   5      20
HET    DVA  E   2       7
HET    SAR  E   4       5
HET    MVA  E   5       8
HET    PX1  E   6      23
HET    DVA  E   8       7
HET    SAR  E  10       5
HET    MVA  E  11       8
HET    DVA  F   2       7
HET    SAR  F   4       5
HET    MVA  F   5       8
HET    PX1  F   6      23
HET    DVA  F   8       7
HET    SAR  F  10       5
HET    MVA  F  11       8
HET    BRU  G   5      20
HET    BRU  H   5      20
HET    BRU  I   5      20
HET    BRU  J   5      20
HET    DVA  K   2       7
HET    SAR  K   4       5
HET    MVA  K   5       8
HET    PX1  K   6      23
HET    DVA  K   8       7
HET    SAR  K  10       5
HET    MVA  K  11       8
HET    DVA  L   2       7
HET    SAR  L   4       5
HET    MVA  L   5       8
HET    PX1  L   6      23
HET    DVA  L   8       7
HET    SAR  L  10       5
HET    MVA  L  11       8
HET    BRU  M   5      20
HET    BRU  N   5      20
HET    BRU  O   5      20
HET    BRU  P   5      20
HET    DVA  Q   2       7
HET    SAR  Q   4       5
HET    MVA  Q   5       8
HET    PX1  Q   6      23
HET    DVA  Q   8       7
HET    SAR  Q  10       5
HET    MVA  Q  11       8
HET    DVA  R   2       7
HET    SAR  R   4       5
HET    MVA  R   5       8
HET    PX1  R   6      23
HET    DVA  R   8       7
HET    SAR  R  10       5
HET    MVA  R  11       8
HET    BRU  S   5      20
HET    BRU  T   5      20
HET    BRU  U   5      20
HET    BRU  V   5      20
HET    DVA  W   2       7
HET    SAR  W   4       5
HET    MVA  W   5       8
HET    PX1  W   6      23
HET    DVA  W   8       7
HET    SAR  W  10       5
HET    MVA  W  11       8
HET    DVA  X   2       7
HET    SAR  X   4       5
HET    MVA  X   5       8
HET    PX1  X   6      23
HET    DVA  X   8       7
HET    SAR  X  10       5
HET    MVA  X  11       8
HETNAM     BRU 5-BROMO-2'-DEOXYURIDINE-5'-MONOPHOSPHATE
HETNAM     DVA D-VALINE
HETNAM     SAR SARCOSINE
HETNAM     MVA N-METHYLVALINE
HETNAM     PX1 (1Z)-7-AMINO-1-(HYDROXYMETHYLENE)-2-IMINO-4,
HETNAM   2 PX1  6-DIMETHYL-3-OXO-2,3-DIHYDRO-1H-PHENOXAZINE-9-
HETNAM   3 PX1  CARBALDEHYDE
FORMUL   1  BRU    16(C9 H12 BR N2 O8 P)
FORMUL  17  DVA    16(C5 H11 N O2)
FORMUL  17  SAR    16(C3 H7 N O2)
FORMUL  17  MVA    16(C6 H13 N O2)
FORMUL  17  PX1    8(C16 H13 N3 O4)
FORMUL  25  HOH   *14(H2 O)
LINK         O3'  DG A   4                 P   BRU A   5     1555   1555  1.61
LINK         O3' BRU A   5                 P    DT A   6     1555   1555  1.61
LINK         O3'  DG B   4                 P   BRU B   5     1555   1555  1.61
LINK         O3' BRU B   5                 P    DT B   6     1555   1555  1.61
LINK         O3'  DG C   4                 P   BRU C   5     1555   1555  1.62
LINK         O3' BRU C   5                 P    DT C   6     1555   1555  1.60
LINK         O3'  DG D   4                 P   BRU D   5     1555   1555  1.61
LINK         O3' BRU D   5                 P    DT D   6     1555   1555  1.61
LINK         C   THR E   1                 N   DVA E   2     1555   1555  1.34
LINK         OG1 THR E   1                 C   MVA E   5     1555   1555  1.35
LINK         N   THR E   1                 C   PX1 E   6     1555   1555  1.33
LINK         C   DVA E   2                 N   PRO E   3     1555   1555  1.33
LINK         C   PRO E   3                 N   SAR E   4     1555   1555  1.32
LINK         C   SAR E   4                 N   MVA E   5     1555   1555  1.33
LINK         C'  PX1 E   6                 N   THR E   7     1555   1555  1.33
LINK         C   THR E   7                 N   DVA E   8     1555   1555  1.33
LINK         OG1 THR E   7                 C   MVA E  11     1555   1555  1.35
LINK         C   DVA E   8                 N   PRO E   9     1555   1555  1.33
LINK         C   PRO E   9                 N   SAR E  10     1555   1555  1.32
LINK         C   SAR E  10                 N   MVA E  11     1555   1555  1.34
LINK         C   THR F   1                 N   DVA F   2     1555   1555  1.34
LINK         N   THR F   1                 C   PX1 F   6     1555   1555  1.34
LINK         OG1 THR F   1                 C   MVA F   5     1555   1555  1.35
LINK         C   DVA F   2                 N   PRO F   3     1555   1555  1.33
LINK         C   PRO F   3                 N   SAR F   4     1555   1555  1.33
LINK         C   SAR F   4                 N   MVA F   5     1555   1555  1.33
LINK         C'  PX1 F   6                 N   THR F   7     1555   1555  1.33
LINK         C   THR F   7                 N   DVA F   8     1555   1555  1.33
LINK         OG1 THR F   7                 C   MVA F  11     1555   1555  1.36
LINK         C   DVA F   8                 N   PRO F   9     1555   1555  1.33
LINK         C   PRO F   9                 N   SAR F  10     1555   1555  1.33
LINK         C   SAR F  10                 N   MVA F  11     1555   1555  1.33
LINK         O3'  DG G   4                 P   BRU G   5     1555   1555  1.60
LINK         O3' BRU G   5                 P    DT G   6     1555   1555  1.62
LINK         O3'  DG H   4                 P   BRU H   5     1555   1555  1.60
LINK         O3' BRU H   5                 P    DT H   6     1555   1555  1.62
LINK         O3'  DG I   4                 P   BRU I   5     1555   1555  1.61
LINK         O3' BRU I   5                 P    DT I   6     1555   1555  1.61
LINK         O3'  DG J   4                 P   BRU J   5     1555   1555  1.61
LINK         O3' BRU J   5                 P    DT J   6     1555   1555  1.62
LINK         OG1 THR K   1                 C   MVA K   5     1555   1555  1.35
LINK         C   THR K   1                 N   DVA K   2     1555   1555  1.34
LINK         N   THR K   1                 C   PX1 K   6     1555   1555  1.34
LINK         C   DVA K   2                 N   PRO K   3     1555   1555  1.33
LINK         C   PRO K   3                 N   SAR K   4     1555   1555  1.32
LINK         C   SAR K   4                 N   MVA K   5     1555   1555  1.33
LINK         C'  PX1 K   6                 N   THR K   7     1555   1555  1.33
LINK         C   THR K   7                 N   DVA K   8     1555   1555  1.34
LINK         OG1 THR K   7                 C   MVA K  11     1555   1555  1.34
LINK         C   DVA K   8                 N   PRO K   9     1555   1555  1.33
LINK         C   PRO K   9                 N   SAR K  10     1555   1555  1.32
LINK         C   SAR K  10                 N   MVA K  11     1555   1555  1.33
LINK         OG1 THR L   1                 C   MVA L   5     1555   1555  1.35
LINK         N   THR L   1                 C   PX1 L   6     1555   1555  1.33
LINK         C   THR L   1                 N   DVA L   2     1555   1555  1.33
LINK         C   DVA L   2                 N   PRO L   3     1555   1555  1.33
LINK         C   PRO L   3                 N   SAR L   4     1555   1555  1.33
LINK         C   SAR L   4                 N   MVA L   5     1555   1555  1.33
LINK         C'  PX1 L   6                 N   THR L   7     1555   1555  1.32
LINK         OG1 THR L   7                 C   MVA L  11     1555   1555  1.35
LINK         C   THR L   7                 N   DVA L   8     1555   1555  1.34
LINK         C   DVA L   8                 N   PRO L   9     1555   1555  1.33
LINK         C   PRO L   9                 N   SAR L  10     1555   1555  1.33
LINK         C   SAR L  10                 N   MVA L  11     1555   1555  1.33
LINK         O3'  DG M   4                 P   BRU M   5     1555   1555  1.61
LINK         O3' BRU M   5                 P    DT M   6     1555   1555  1.61
LINK         O3'  DG N   4                 P   BRU N   5     1555   1555  1.60
LINK         O3' BRU N   5                 P    DT N   6     1555   1555  1.61
LINK         O3'  DG O   4                 P   BRU O   5     1555   1555  1.61
LINK         O3' BRU O   5                 P    DT O   6     1555   1555  1.60
LINK         O3'  DG P   4                 P   BRU P   5     1555   1555  1.61
LINK         O3' BRU P   5                 P    DT P   6     1555   1555  1.61
LINK         C   THR Q   1                 N   DVA Q   2     1555   1555  1.34
LINK         N   THR Q   1                 C   PX1 Q   6     1555   1555  1.33
LINK         OG1 THR Q   1                 C   MVA Q   5     1555   1555  1.35
LINK         C   DVA Q   2                 N   PRO Q   3     1555   1555  1.33
LINK         C   PRO Q   3                 N   SAR Q   4     1555   1555  1.32
LINK         C   SAR Q   4                 N   MVA Q   5     1555   1555  1.33
LINK         C'  PX1 Q   6                 N   THR Q   7     1555   1555  1.32
LINK         OG1 THR Q   7                 C   MVA Q  11     1555   1555  1.34
LINK         C   THR Q   7                 N   DVA Q   8     1555   1555  1.33
LINK         C   DVA Q   8                 N   PRO Q   9     1555   1555  1.33
LINK         C   PRO Q   9                 N   SAR Q  10     1555   1555  1.33
LINK         C   SAR Q  10                 N   MVA Q  11     1555   1555  1.34
LINK         N   THR R   1                 C   PX1 R   6     1555   1555  1.33
LINK         OG1 THR R   1                 C   MVA R   5     1555   1555  1.35
LINK         C   THR R   1                 N   DVA R   2     1555   1555  1.34
LINK         C   DVA R   2                 N   PRO R   3     1555   1555  1.33
LINK         C   PRO R   3                 N   SAR R   4     1555   1555  1.33
LINK         C   SAR R   4                 N   MVA R   5     1555   1555  1.33
LINK         C'  PX1 R   6                 N   THR R   7     1555   1555  1.33
LINK         OG1 THR R   7                 C   MVA R  11     1555   1555  1.35
LINK         C   THR R   7                 N   DVA R   8     1555   1555  1.33
LINK         C   DVA R   8                 N   PRO R   9     1555   1555  1.32
LINK         C   PRO R   9                 N   SAR R  10     1555   1555  1.33
LINK         C   SAR R  10                 N   MVA R  11     1555   1555  1.34
LINK         O3'  DG S   4                 P   BRU S   5     1555   1555  1.60
LINK         O3' BRU S   5                 P    DT S   6     1555   1555  1.61
LINK         O3'  DG T   4                 P   BRU T   5     1555   1555  1.61
LINK         O3' BRU T   5                 P    DT T   6     1555   1555  1.61
LINK         O3'  DG U   4                 P   BRU U   5     1555   1555  1.61
LINK         O3' BRU U   5                 P    DT U   6     1555   1555  1.61
LINK         O3'  DG V   4                 P   BRU V   5     1555   1555  1.61
LINK         O3' BRU V   5                 P    DT V   6     1555   1555  1.61
LINK         OG1 THR W   1                 C   MVA W   5     1555   1555  1.35
LINK         N   THR W   1                 C   PX1 W   6     1555   1555  1.33
LINK         C   THR W   1                 N   DVA W   2     1555   1555  1.34
LINK         C   DVA W   2                 N   PRO W   3     1555   1555  1.33
LINK         C   PRO W   3                 N   SAR W   4     1555   1555  1.32
LINK         C   SAR W   4                 N   MVA W   5     1555   1555  1.33
LINK         C'  PX1 W   6                 N   THR W   7     1555   1555  1.33
LINK         OG1 THR W   7                 C   MVA W  11     1555   1555  1.35
LINK         C   THR W   7                 N   DVA W   8     1555   1555  1.33
LINK         C   DVA W   8                 N   PRO W   9     1555   1555  1.32
LINK         C   PRO W   9                 N   SAR W  10     1555   1555  1.32
LINK         C   SAR W  10                 N   MVA W  11     1555   1555  1.34
LINK         OG1 THR X   1                 C   MVA X   5     1555   1555  1.35
LINK         N   THR X   1                 C   PX1 X   6     1555   1555  1.34
LINK         C   THR X   1                 N   DVA X   2     1555   1555  1.34
LINK         C   DVA X   2                 N   PRO X   3     1555   1555  1.33
LINK         C   PRO X   3                 N   SAR X   4     1555   1555  1.33
LINK         C   SAR X   4                 N   MVA X   5     1555   1555  1.33
LINK         C'  PX1 X   6                 N   THR X   7     1555   1555  1.33
LINK         OG1 THR X   7                 C   MVA X  11     1555   1555  1.34
LINK         C   THR X   7                 N   DVA X   8     1555   1555  1.33
LINK         C   DVA X   8                 N   PRO X   9     1555   1555  1.33
LINK         C   PRO X   9                 N   SAR X  10     1555   1555  1.32
LINK         C   SAR X  10                 N   MVA X  11     1555   1555  1.33
CISPEP   1 DVA E    2    PRO E    3          0        13.05
CISPEP   2 DVA E    8    PRO E    9          0         3.98
CISPEP   3 DVA F    2    PRO F    3          0         8.76
CISPEP   4 DVA F    8    PRO F    9          0         7.29
CISPEP   5 DVA K    2    PRO K    3          0         9.46
CISPEP   6 DVA K    8    PRO K    9          0         4.94
CISPEP   7 DVA L    2    PRO L    3          0         7.85
CISPEP   8 DVA L    8    PRO L    9          0         5.59
CISPEP   9 DVA Q    2    PRO Q    3          0         5.71
CISPEP  10 DVA Q    8    PRO Q    9          0         4.41
CISPEP  11 DVA R    2    PRO R    3          0        10.29
CISPEP  12 DVA R    8    PRO R    9          0         4.04
CISPEP  13 DVA W    2    PRO W    3          0         5.92
CISPEP  14 DVA W    8    PRO W    9          0         7.99
CISPEP  15 DVA X    2    PRO X    3          0        12.14
CISPEP  16 DVA X    8    PRO X    9          0         5.42
SITE     1 AC1 11  DA A   3   DG A   4  BRU A   5   DT A   6
SITE     2 AC1 11  DA C   3   DG C   4  BRU C   5   DT H   6
SITE     3 AC1 11  DT J   2  BRU T   5   DT V   1
SITE     1 AC2  8  DG B   4  BRU B   5   DA D   3   DG D   4
SITE     2 AC2  8 BRU D   5   DT D   6   DT G   2   DA G   3
SITE     1 AC3 10  DT B   6   DT D   2   DA G   3   DG G   4
SITE     2 AC3 10 BRU G   5   DT G   6   DA I   3   DG I   4
SITE     3 AC3 10 BRU I   5  DVA L   2
SITE     1 AC4  9  DT A   2   DA A   3   DG H   4  BRU H   5
SITE     2 AC4  9  DA J   3   DG J   4  BRU J   5   DT J   6
SITE     3 AC4  9 DVA K   8
SITE     1 AC5 12  DA M   3   DG M   4  BRU M   5   DT M   6
SITE     2 AC5 12  DG O   4  BRU O   5  HOH Q2001  DVA R   2
SITE     3 AC5 12 SAR R   4  DVA R   8   DT T   6   DT V   2
SITE     1 AC6 11  DA N   3   DG N   4  BRU N   5   DA P   3
SITE     2 AC6 11  DG P   4  BRU P   5   DT P   6  DVA Q   2
SITE     3 AC6 11 DVA Q   8   DT S   2   DA S   3
SITE     1 AC7 10  DT N   6   DT P   2   DA S   3   DG S   4
SITE     2 AC7 10 BRU S   5   DT S   6   DG U   4  BRU U   5
SITE     3 AC7 10 HOH W2001  DVA X   2
SITE     1 AC8 12  DT M   2   DA M   3   DT S   6   DA T   3
SITE     2 AC8 12  DG T   4  BRU T   5   DA V   3   DG V   4
SITE     3 AC8 12 BRU V   5   DT V   6  DVA W   2  DVA W   8
CRYST1   71.222   71.222  108.400  90.00  90.00 120.00 P 32 2 1     96
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.014041  0.008106  0.000000        0.00000
SCALE2      0.000000  0.016213  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009225        0.00000
      
PROCHECK
Go to PROCHECK summary
 References