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PDBsum entry 3t1u

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Isomerase PDB id
3t1u
Jmol
Contents
Protein chain
163 a.a.
Ligands
SIN-ALA-PHE-PRO-
PHE-NIT
Waters ×118
HEADER    ISOMERASE                               22-JUL-11   3T1U
TITLE     CRYSTAL STRUCTURE OF THE COMPLEX OF CYCLOPHILIN-A ENZYME FROM
TITLE    2 AZOTOBACTER VINELANDII WITH SUCAFPFPNA PEPTIDE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: CYCLOPHILIN-A;
COMPND   5 EC: 5.2.1.8;
COMPND   6 ENGINEERED: YES;
COMPND   7 MOL_ID: 2;
COMPND   8 MOLECULE: SUCCINYL-ALA-PHE-PRO-PHE-P-NITROANILIDE;
COMPND   9 CHAIN: B;
COMPND  10 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: AZOTOBACTER VINELANDII;
SOURCE   3 ORGANISM_TAXID: 322710;
SOURCE   4 STRAIN: DJ / ATCC BAA-1303;
SOURCE   5 GENE: AVIN_23510;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28;
SOURCE  11 MOL_ID: 2;
SOURCE  12 SYNTHETIC: YES
KEYWDS    PEPTIDYL-PROLYL ISOMERASE, PPIASE, ISOMERASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    M.KARPUSAS,E.CHRISTOFORIDES,K.BETHANIS,M.DIMOU,P.KATINAKIS
REVDAT   2   23-JAN-13 3T1U    1       JRNL
REVDAT   1   07-MAR-12 3T1U    0
JRNL        AUTH   E.CHRISTOFORIDES,M.DIMOU,P.KATINAKIS,K.BETHANIS,M.KARPUSAS
JRNL        TITL   STRUCTURE OF A BACTERIAL CYTOPLASMIC CYCLOPHILIN A IN
JRNL        TITL 2 COMPLEX WITH A TETRAPEPTIDE.
JRNL        REF    ACTA CRYSTALLOGR.,SECT.F      V.  68   259 2012
JRNL        REFN                   ESSN 1744-3091
JRNL        PMID   22442217
JRNL        DOI    10.1107/S1744309112000188
REMARK   2
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : NULL
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.21
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.7
REMARK   3   NUMBER OF REFLECTIONS             : 11174
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.201
REMARK   3   FREE R VALUE                     : 0.238
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.200
REMARK   3   FREE R VALUE TEST SET COUNT      : 1156
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 1296
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 118
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.47
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -1.66500
REMARK   3    B22 (A**2) : -1.66500
REMARK   3    B33 (A**2) : 3.33000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : NULL
REMARK   3   BOND ANGLES            (DEGREES) : NULL
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.313 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.921 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.976 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.794 ; 2.500
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : 39.91
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 3T1U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUL-11.
REMARK 100 THE RCSB ID CODE IS RCSB066930.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-10
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11291
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : 0.05400
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 24.7200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.9
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.30400
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 4.740
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1LOP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 42.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 19% PEG8000, 0.1 M SODIUM ACETATE, 0.1
REMARK 280  M SODIUM CACODYLATE, PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280  TEMPERATURE 291.16K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/2
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/2
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/2
REMARK 290       7555   Y,X,-Z
REMARK 290       8555   -Y,-X,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       33.20500
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       33.20500
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       35.76500
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       33.20500
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       33.20500
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       35.76500
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       33.20500
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       33.20500
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       35.76500
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       33.20500
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       33.20500
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       35.76500
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 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     VAL A 127    CG1  CG2
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   O    HOH A   267     O    HOH A   267     7555     2.00
REMARK 500
REMARK 500 REMARK: NULL
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 (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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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   RES CSSEQI ATM2   DEVIATION
REMARK 500    PHE B   4   C     PHE B   4   O       0.131
REMARK 500
REMARK 500 REMARK: NULL
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 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    PHE A  16       75.69   -107.36
REMARK 500    ALA A  20       58.90   -150.11
REMARK 500    PHE A  48      -80.12   -135.75
REMARK 500    TYR A  81        0.77     83.37
REMARK 500    ARG A  87     -167.42   -169.72
REMARK 500    HIS A  92       40.09    -98.76
REMARK 500    SER A  95      -88.40   -132.35
REMARK 500    ASN A 105       67.54   -118.93
REMARK 500    ALA A 145     -137.43     51.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3T17   RELATED DB: PDB
DBREF  3T1U A    2   163  UNP    C1DHE4   C1DHE4_AZOVD     2    163
DBREF  3T1U B    0     5  PDB    3T1U     3T1U             0      5
SEQADV 3T1U SER A    1  UNP  C1DHE4              EXPRESSION TAG
SEQRES   1 A  163  SER ILE LYS LEU GLN THR ASN HIS GLY THR ILE THR LEU
SEQRES   2 A  163  LYS LEU PHE ALA ASP LYS ALA PRO GLU THR ALA ALA ASN
SEQRES   3 A  163  PHE GLU GLN TYR VAL LYS ASP GLY HIS TYR ASP GLY THR
SEQRES   4 A  163  ILE PHE HIS ARG VAL ILE ASP GLY PHE MET ILE GLN GLY
SEQRES   5 A  163  GLY GLY PHE GLU PRO GLY MET LYS GLN LYS SER THR ARG
SEQRES   6 A  163  ALA PRO ILE LYS ASN GLU ALA ASN ASN GLY LEU SER ASN
SEQRES   7 A  163  LYS LYS TYR THR ILE ALA MET ALA ARG THR PRO ASP PRO
SEQRES   8 A  163  HIS SER ALA SER ALA GLN PHE PHE ILE ASN VAL LYS ASP
SEQRES   9 A  163  ASN ALA PHE LEU ASP HIS THR ALA PRO THR ALA HIS GLY
SEQRES  10 A  163  TRP GLY TYR ALA VAL PHE GLY GLU VAL VAL GLU GLY THR
SEQRES  11 A  163  ASP VAL VAL ASP ARG ILE LYS SER VAL ALA THR GLY SER
SEQRES  12 A  163  ARG ALA GLY HIS GLY ASP VAL PRO VAL ASP ASP VAL ILE
SEQRES  13 A  163  ILE GLU LYS ALA GLU ILE VAL
SEQRES   1 B    6  SIN ALA PHE PRO PHE NIT
HET    SIN  B   0       7
HET    NIT  B   5      10
HETNAM     SIN SUCCINIC ACID
HETNAM     NIT 4-NITROANILINE
HETSYN     NIT PARANITROANILINE
FORMUL   2  SIN    C4 H6 O4
FORMUL   2  NIT    C6 H6 N2 O2
FORMUL   3  HOH   *118(H2 O)
HELIX    1   1 ALA A   20  ASP A   33  1                                  14
HELIX    2   2 ASN A  105  ASP A  109  5                                   5
HELIX    3   3 GLY A  129  LYS A  137  1                                   9
SHEET    1   A 9 THR A  39  ILE A  40  0
SHEET    2   A 9 ILE A 156  ILE A 162 -1  O  ILE A 157   N  THR A  39
SHEET    3   A 9 ILE A   2  THR A   6 -1  N  GLN A   5   O  LYS A 159
SHEET    4   A 9 GLY A   9  LEU A  15 -1  O  LEU A  13   N  ILE A   2
SHEET    5   A 9 VAL A 122  GLU A 128 -1  O  VAL A 127   N  THR A  12
SHEET    6   A 9 THR A  82  MET A  85 -1  N  ILE A  83   O  PHE A 123
SHEET    7   A 9 PHE A  98  ASN A 101 -1  O  PHE A  99   N  ALA A  84
SHEET    8   A 9 MET A  49  GLY A  52 -1  N  ILE A  50   O  ILE A 100
SHEET    9   A 9 ARG A  43  ILE A  45 -1  N  ARG A  43   O  GLN A  51
SHEET    1   B 2 PHE A  55  GLU A  56  0
SHEET    2   B 2 LYS A  60  GLN A  61 -1  O  LYS A  60   N  GLU A  56
SHEET    1   C 2 THR A 141  ARG A 144  0
SHEET    2   C 2 HIS A 147  PRO A 151 -1  O  HIS A 147   N  ARG A 144
LINK         C4  SIN B   0                 N   ALA B   1     1555   1555  1.33
LINK         C   PHE B   4                 N1  NIT B   5     1555   1555  1.33
CISPEP   1 PHE B    2    PRO B    3          0         2.32
CRYST1   66.410   66.410   71.530  90.00  90.00  90.00 P 42 21 2     8
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      0.015058  0.000000  0.000000        0.00000
SCALE2      0.000000  0.015058  0.000000        0.00000
SCALE3      0.000000  0.000000  0.013980        0.00000
      
PROCHECK
Go to PROCHECK summary
 References