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PDBsum entry 3nir

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Plant protein PDB id
3nir
Jmol
Contents
Protein chain
48 a.a.
Ligands
EOH ×4
Waters ×116
HEADER    PLANT PROTEIN                           16-JUN-10   3NIR
TITLE     CRYSTAL STRUCTURE OF SMALL PROTEIN CRAMBIN AT 0.48 A RESOLUTION
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CRAMBIN;
COMPND   3 CHAIN: A
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: CRAMBE HISPANICA;
SOURCE   3 ORGANISM_COMMON: ABYSSINIAN CRAMBE, ABYSSINIAN KALE;
SOURCE   4 ORGANISM_TAXID: 3721;
SOURCE   5 STRAIN: SUBSP. ABYSSINICA
KEYWDS    PLANT PROTEIN
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.SCHMIDT,M.TEETER,E.WECKERT,V.S.LAMZIN
REVDAT   1   18-MAY-11 3NIR    0
JRNL        AUTH   A.SCHMIDT,M.TEETER,E.WECKERT,V.S.LAMZIN
JRNL        TITL   CRYSTAL STRUCTURE OF SMALL PROTEIN CRAMBIN AT 0.48 A
JRNL        TITL 2 RESOLUTION
JRNL        REF    ACTA CRYSTALLOGR.,SECT.F      V.  67   424 2011
JRNL        REFN                   ESSN 1744-3091
JRNL        PMID   21505232
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   C.JELSCH,M.M.TEETER,V.S.LAMZIN,V.PICHON-PESME,R.H.BLESSING,
REMARK   1  AUTH 2 C.LECOMTE
REMARK   1  TITL   ACCURATE PROTEIN CRYSTALLOGRAPHY AT ULTRA-HIGH RESOLUTION:
REMARK   1  TITL 2 VALENCE ELECTRON DISTRIBUTION IN CRAMBIN.
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  97  3171 2000
REMARK   1  REFN                   ISSN 0027-8424
REMARK   1  DOI    10737790
REMARK   2
REMARK   2 RESOLUTION.    0.48 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : MOPRO
REMARK   3   AUTHORS     : GUILLOT,VIRY,GUILLOT,LECOMTE,JELSCH
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 0.48
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
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)   (%) : 97.0
REMARK   3   NUMBER OF REFLECTIONS             : 156860
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : RFREE INITIALLY, FINAL STAGES
REMARK   3                                      NONE
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.127
REMARK   3   FREE R VALUE                     : NULL
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL
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            : 341
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 12
REMARK   3   SOLVENT ATOMS            : 98
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 2.14
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 4.12
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
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 : OVERALL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
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:
REMARK   3  INITIAL REFINEMENT WITH REFMAC THEN SHELX, THEN MOPRO FOR MULTIPOLE
REMARK   3  REFINEMENT. ONLY DURING REFMAC CROSS VALIDATION WITH RFREE. IN THE
REMARK   3  LAST STAGES OF REFINEMENT THE SUM OF OCCUPANCIES FOR THE MULTIPLE
REMARK   3  CONFORMERS WAS NOT CONSTRAINED TO 1.00 AND ONLY WEAK STEREOCHEMICAL
REMARK   3  RESTRAINTS WERE APPLIED. ALTHOUGH OVERALL SUCH REFINEMENT OF THE
REMARK   3  MULTIPLE CONFORMERS WENT FINE, THERE WAS SOME INSTABILITY - FOR
REMARK   3  EXAMPLE THE REFINEMENT OF THE TEMPERATURE FACTORS FOR CA AND C
REMARK   3  ATOMS OF THE THIRD CONFORMER OF TYR A 29 DID NOT CONVERGE AND WERE
REMARK   3  TRUNCATED TO THE VALUE OF 50.
REMARK   3  BULK SOLVENT MODELING METHOD USED:BULK SOLVENT ENVELOPE METHOD
REMARK   3  FC(MOL)+FC(BULK)
REMARK   4
REMARK   4 3NIR COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-APR-11.
REMARK 100 THE RCSB ID CODE IS RCSB059880.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 05-JUL-01; 25-FEB-02
REMARK 200  TEMPERATURE           (KELVIN) : 100; 100
REMARK 200  PH                             : 7
REMARK 200  NUMBER OF CRYSTALS USED        : 3
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y
REMARK 200  RADIATION SOURCE               : PETRA II STORAGE RING; PETRA II
REMARK 200                                   STORAGE RING
REMARK 200  BEAMLINE                       : PETRA1; PETRA1
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.5498; 0.5636
REMARK 200  MONOCHROMATOR                  : DIAMOND (111) - GERMANIUM (220);
REMARK 200                                   DIAMOND (111) - GERMANIUM (220)
REMARK 200  OPTICS                         : NULL; NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD; CCD
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM; MAR CCD 165 MM
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK AND SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 156860
REMARK 200  RESOLUTION RANGE HIGH      (A) : 0.480
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     (%) : 97.0
REMARK 200  DATA REDUNDANCY                : 3.700
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.07500
REMARK 200   FOR THE DATA SET  : 9.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 0.48
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 0.49
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 1.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: ISOMORPHOUS TO PDB ENTRY
REMARK 200  1EJG
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1EJG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 60% ETHANOL IN WATER, PH 7, VAPOR
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,Y+1/2,-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        9.23550
REMARK 290   SMTRY3   2  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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 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   HG1  THR A    30     H    CYS A    32              1.15
REMARK 500   C    THR A    28     H    TYR A    29              1.18
REMARK 500   HZ   PHE A    13     HG2  GLU A    23              1.20
REMARK 500   HH   TYR A    29     HA   THR A    30              1.31
REMARK 500   H2   THR A     1     H    ILE A    35              1.32
REMARK 500   HB2  CYS A    16     HD2  TYR A    29              1.32
REMARK 500   HG   SER A    11     C2   EOH A  2002              1.40
REMARK 500   H1   THR A     1     O    HOH A  3055              1.43
REMARK 500   HB2  SER A    11     C2   EOH A  2002              1.47
REMARK 500   HG1  THR A    28     HD1  TYR A    29              1.54
REMARK 500   HG   SER A     6     H    ALA A     9              1.56
REMARK 500   HG   SER A    11     O    EOH A  2002              1.60
REMARK 500   O    HOH A  3022     O    HOH A  3114              1.70
REMARK 500   OG   SER A    11     C2   EOH A  2002              1.74
REMARK 500   O    HOH A  3053     O    HOH A  3117              1.74
REMARK 500   O    HOH A  3031     O    HOH A  3121              1.80
REMARK 500   CB   SER A    11     C2   EOH A  2002              1.87
REMARK 500   O    HOH A  3101     O    HOH A  3120              1.91
REMARK 500   O    HOH A  3090     O    HOH A  3121              2.05
REMARK 500   OG1  THR A     1     O    HOH A  3040              2.11
REMARK 500   O    HOH A  3086     O    HOH A  3119              2.14
REMARK 500   O    THR A    21     N    SER A  1022              2.19
REMARK 500
REMARK 500 REMARK: NULL
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  3101     O    HOH A  3118     1565     1.84
REMARK 500   O    HOH A  3057     O    HOH A  3098     2656     1.92
REMARK 500   O    HOH A  3028     O    HOH A  3123     1455     2.13
REMARK 500   C1   EOH A  2004     O    HOH A  3085     1455     2.14
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    PHE A  13   CB  -  CG  -  CD1 ANGL. DEV. =  -4.6 DEGREES
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    THR A   1        24.9      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A3111        DISTANCE =  5.44 ANGSTROMS
REMARK 525    HOH A3119        DISTANCE =  5.63 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EOH A 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EOH A 2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EOH A 2003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EOH A 2004
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EJG   RELATED DB: PDB
REMARK 900 CRAMBIN TO 0.54 A RESOLUTION
REMARK 900 RELATED ID: 1CRN   RELATED DB: PDB
REMARK 900 CRAMBIN AT ROOM TEMPERATURE
REMARK 900 RELATED ID: 1CNR   RELATED DB: PDB
REMARK 900 CRAMBIN, PURE P22/ L25 FORM
REMARK 900 RELATED ID: 1CBN   RELATED DB: PDB
REMARK 900 CRAMBIN TO 0.83 A RESOLUTION
REMARK 900 RELATED ID: 1AB1   RELATED DB: PDB
REMARK 900 CRAMBIN, PURE S22 / I25 FORM
DBREF  3NIR A    1    46  UNP    P01542   CRAM_CRAAB       1     46
SEQADV 3NIR SER A 1022  UNP  P01542              EXPRESSION TAG
SEQADV 3NIR ILE A 1025  UNP  P01542              EXPRESSION TAG
SEQRES   1 A   48  THR THR CYS CYS PRO SER ILE VAL ALA ARG SER ASN PHE
SEQRES   2 A   48  ASN VAL CYS ARG LEU PRO GLY THR PRO SER GLU ALA LEU
SEQRES   3 A   48  ILE CYS ALA THR TYR THR GLY CYS ILE ILE ILE PRO GLY
SEQRES   4 A   48  ALA THR CYS PRO GLY ASP TYR ALA ASN
HET    EOH  A2001       3
HET    EOH  A2002       6
HET    EOH  A2003       6
HET    EOH  A2004       3
HETNAM     EOH ETHANOL
FORMUL   2  EOH    4(C2 H6 O)
FORMUL   6  HOH   *98(H2 O)
HELIX    1   1 SER A    6  LEU A   18  1                                  13
HELIX    2   2 ILE A 1025  GLY A   31  1                                   7
SHEET    1   A 2 THR A   2  CYS A   3  0
SHEET    2   A 2 ILE A  33  ILE A  34 -1  O  ILE A  33   N  CYS A   3
SSBOND   1 CYS A    3    CYS A   40                          1555   1555  2.03
SSBOND   2 CYS A    4    CYS A   32                          1555   1555  2.05
SSBOND   3 CYS A   16    CYS A   26                          1555   1555  2.04
SITE     1 AC1  8 ALA A  45  ASN A  46  EOH A2004  HOH A3006
SITE     2 AC1  8 HOH A3027  HOH A3038  HOH A3087  HOH A3091
SITE     1 AC2 10 ILE A   7  VAL A   8  SER A  11  ALA A  27
SITE     2 AC2 10 GLY A  31  CYS A  32  ILE A  33  HOH A3002
SITE     3 AC2 10 HOH A3068  HOH A3102
SITE     1 AC3  3 ILE A   7  ASN A  46  HOH A3063
SITE     1 AC4  7 ASN A  14  LEU A  18  EOH A2001  HOH A3011
SITE     2 AC4  7 HOH A3020  HOH A3023  HOH A3085
CRYST1   22.329   18.471   40.769  90.00  90.55  90.00 P 1 21 1      2
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      0.044785  0.000000  0.000430        0.00000
SCALE2      0.000000  0.054139  0.000000        0.00000
SCALE3      0.000000  0.000000  0.024530        0.00000
      
PROCHECK
Go to PROCHECK summary
 References