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PDBsum entry 3s5p

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Top Page protein ligands Protein-protein interface(s) links
Isomerase PDB id
3s5p
Jmol
Contents
Protein chains
134 a.a.
125 a.a.
Ligands
SO4 ×5
Waters ×50
HEADER    ISOMERASE                               23-MAY-11   3S5P
TITLE     CRYSTAL STRUCTURE OF RIBOSE-5-PHOSPHATE ISOMERASE B RPIB FROM GIARDIA
TITLE    2 LAMBLIA
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: RIBOSE 5-PHOSPHATE ISOMERASE;
COMPND   3 CHAIN: A, B;
COMPND   4 EC: 5.3.1.6;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: GIARDIA LAMBLIA;
SOURCE   3 ORGANISM_TAXID: 184922;
SOURCE   4 STRAIN: ATCC 50803 WB C6;
SOURCE   5 GENE: GL50803_27614;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PAVA0421
KEYWDS    STRUCTURAL GENOMICS, SEATTLE STRUCTURAL GENOMICS CENTER FOR
KEYWDS   2 INFECTIOUS DISEASE, SSGCID, GIARDIA, ISOMERASE, RIBOSE-5-PHOSPHATE,
KEYWDS   3 RIBULOSE-5-PHOSPHATE, RPIB, RPIA, PENTOSE PHOSPHATE PATHWAY,
KEYWDS   4 PENTOSE-PHOSPHATE SHUNT, FLAGELLATED PROTOZOAN PARASITE,
KEYWDS   5 GASTROINTESTINAL TRACT PARASITE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)
REVDAT   1   01-JUN-11 3S5P    0
JRNL        AUTH   T.E.EDWARDS,J.ABENDROTH,
JRNL        AUTH 2 SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE
JRNL        AUTH 3 (SSGCID)
JRNL        TITL   CRYSTAL STRUCTURE OF RIBOSE-5-PHOSPHATE ISOMERASE B RPIB
JRNL        TITL 2 FROM GIARDIA LAMBLIA
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0109
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.62
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.3
REMARK   3   NUMBER OF REFLECTIONS             : 13881
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.200
REMARK   3   R VALUE            (WORKING SET) : 0.198
REMARK   3   FREE R VALUE                     : 0.234
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 701
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 937
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.14
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3000
REMARK   3   BIN FREE R VALUE SET COUNT          : 58
REMARK   3   BIN FREE R VALUE                    : 0.3320
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 1810
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 25
REMARK   3   SOLVENT ATOMS            : 50
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 55.73
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 50.48
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.46000
REMARK   3    B22 (A**2) : 0.46000
REMARK   3    B33 (A**2) : -0.69000
REMARK   3    B12 (A**2) : 0.23000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.210
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.150
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.011
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.929
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1861 ; 0.014 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2510 ; 1.416 ; 1.955
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   257 ; 5.719 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    68 ;30.831 ;22.647
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   274 ;14.996 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    15 ;20.057 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   286 ; 0.086 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1377 ; 0.005 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1270 ; 0.833 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1971 ; 1.552 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   591 ; 2.284 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   538 ; 3.563 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 1
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 1
REMARK   3     CHAIN NAMES                    : A B
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     A      1       A     128      4
REMARK   3           1     B      1       B     128      4
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   MEDIUM POSITIONAL  1    A    (A):    821 ; 0.220 ; 0.500
REMARK   3   MEDIUM THERMAL     1    A (A**2):    821 ; 0.940 ; 2.000
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 8
REMARK   3
REMARK   3   TLS GROUP : 1
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A     1        A    20
REMARK   3    ORIGIN FOR THE GROUP (A): -47.6426   8.6514   5.7593
REMARK   3    T TENSOR
REMARK   3      T11:   0.6644 T22:   0.2577
REMARK   3      T33:   0.3380 T12:  -0.2026
REMARK   3      T13:   0.1227 T23:  -0.1341
REMARK   3    L TENSOR
REMARK   3      L11:   2.5513 L22:   3.2599
REMARK   3      L33:  11.6521 L12:   1.3657
REMARK   3      L13:   1.7621 L23:  -1.1527
REMARK   3    S TENSOR
REMARK   3      S11:   0.3564 S12:  -0.4726 S13:   0.5082
REMARK   3      S21:   0.8151 S22:  -0.2839 S23:  -0.0379
REMARK   3      S31:  -2.0210 S32:   0.6948 S33:  -0.0725
REMARK   3
REMARK   3   TLS GROUP : 2
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A    21        A    60
REMARK   3    ORIGIN FOR THE GROUP (A): -51.2796   2.6279  10.7068
REMARK   3    T TENSOR
REMARK   3      T11:   0.4002 T22:   0.2087
REMARK   3      T33:   0.2960 T12:  -0.0854
REMARK   3      T13:   0.2313 T23:  -0.1429
REMARK   3    L TENSOR
REMARK   3      L11:   4.0468 L22:  11.1490
REMARK   3      L33:   9.4226 L12:  -4.1162
REMARK   3      L13:   0.7985 L23:  -4.9235
REMARK   3    S TENSOR
REMARK   3      S11:   0.2996 S12:  -0.0258 S13:   0.5458
REMARK   3      S21:   1.0793 S22:  -0.0742 S23:   0.3576
REMARK   3      S31:  -0.8822 S32:   0.3101 S33:  -0.2254
REMARK   3
REMARK   3   TLS GROUP : 3
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A    61        A    90
REMARK   3    ORIGIN FOR THE GROUP (A): -42.5940  -4.8510   4.3504
REMARK   3    T TENSOR
REMARK   3      T11:   0.2834 T22:   0.1270
REMARK   3      T33:   0.1677 T12:  -0.1075
REMARK   3      T13:   0.0502 T23:  -0.1090
REMARK   3    L TENSOR
REMARK   3      L11:   2.1007 L22:   2.8458
REMARK   3      L33:   2.7020 L12:   0.0233
REMARK   3      L13:   0.8313 L23:  -0.9445
REMARK   3    S TENSOR
REMARK   3      S11:   0.1338 S12:  -0.0922 S13:   0.0418
REMARK   3      S21:   0.2850 S22:  -0.1637 S23:  -0.0717
REMARK   3      S31:  -0.1813 S32:   0.2904 S33:   0.0299
REMARK   3
REMARK   3   TLS GROUP : 4
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A    91        A   128
REMARK   3    ORIGIN FOR THE GROUP (A): -49.6712  -2.4386  -2.1034
REMARK   3    T TENSOR
REMARK   3      T11:   0.1910 T22:   0.0666
REMARK   3      T33:   0.1763 T12:  -0.0364
REMARK   3      T13:   0.0632 T23:  -0.1014
REMARK   3    L TENSOR
REMARK   3      L11:   1.8466 L22:   4.2501
REMARK   3      L33:   3.7023 L12:   1.7417
REMARK   3      L13:  -0.6189 L23:  -1.9666
REMARK   3    S TENSOR
REMARK   3      S11:   0.0991 S12:   0.0018 S13:   0.0565
REMARK   3      S21:   0.0497 S22:  -0.0941 S23:   0.2451
REMARK   3      S31:  -0.1212 S32:  -0.0319 S33:  -0.0050
REMARK   3
REMARK   3   TLS GROUP : 5
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B     1        B    21
REMARK   3    ORIGIN FOR THE GROUP (A): -32.0348 -19.4149 -12.2121
REMARK   3    T TENSOR
REMARK   3      T11:   0.2190 T22:   0.1130
REMARK   3      T33:   0.1379 T12:   0.1018
REMARK   3      T13:  -0.0282 T23:  -0.0375
REMARK   3    L TENSOR
REMARK   3      L11:   4.2125 L22:   2.8756
REMARK   3      L33:   3.6981 L12:   0.0375
REMARK   3      L13:  -0.8996 L23:  -0.1695
REMARK   3    S TENSOR
REMARK   3      S11:   0.1876 S12:   0.2393 S13:  -0.0424
REMARK   3      S21:  -0.1420 S22:  -0.0624 S23:   0.0324
REMARK   3      S31:   0.2095 S32:  -0.0826 S33:  -0.1252
REMARK   3
REMARK   3   TLS GROUP : 6
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B    22        B    58
REMARK   3    ORIGIN FOR THE GROUP (A): -28.6675 -21.9418  -3.4576
REMARK   3    T TENSOR
REMARK   3      T11:   0.4471 T22:   0.2104
REMARK   3      T33:   0.1554 T12:   0.0556
REMARK   3      T13:  -0.0850 T23:   0.0147
REMARK   3    L TENSOR
REMARK   3      L11:   2.9286 L22:   6.1733
REMARK   3      L33:   8.3989 L12:  -1.8023
REMARK   3      L13:  -1.2047 L23:   4.5035
REMARK   3    S TENSOR
REMARK   3      S11:   0.3781 S12:  -0.1727 S13:  -0.1263
REMARK   3      S21:   0.9520 S22:  -0.1132 S23:   0.0316
REMARK   3      S31:   1.3645 S32:   0.4069 S33:  -0.2650
REMARK   3
REMARK   3   TLS GROUP : 7
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B    59        B    97
REMARK   3    ORIGIN FOR THE GROUP (A): -33.9873 -10.2041  -0.4685
REMARK   3    T TENSOR
REMARK   3      T11:   0.2866 T22:   0.1724
REMARK   3      T33:   0.1635 T12:  -0.0153
REMARK   3      T13:  -0.0168 T23:  -0.0682
REMARK   3    L TENSOR
REMARK   3      L11:   1.0298 L22:   1.0318
REMARK   3      L33:   2.9670 L12:  -0.7392
REMARK   3      L13:  -0.6913 L23:  -0.0553
REMARK   3    S TENSOR
REMARK   3      S11:   0.0676 S12:  -0.1087 S13:   0.0511
REMARK   3      S21:   0.2299 S22:  -0.0678 S23:  -0.0519
REMARK   3      S31:   0.1100 S32:   0.3650 S33:   0.0002
REMARK   3
REMARK   3   TLS GROUP : 8
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B    98        B   129
REMARK   3    ORIGIN FOR THE GROUP (A): -29.2934  -7.8979  -5.4638
REMARK   3    T TENSOR
REMARK   3      T11:   0.2070 T22:   0.1399
REMARK   3      T33:   0.1838 T12:   0.0140
REMARK   3      T13:  -0.0111 T23:  -0.0497
REMARK   3    L TENSOR
REMARK   3      L11:   2.6753 L22:   2.4366
REMARK   3      L33:   5.7571 L12:  -1.3270
REMARK   3      L13:   0.4176 L23:  -0.3426
REMARK   3    S TENSOR
REMARK   3      S11:   0.2509 S12:  -0.0390 S13:   0.1730
REMARK   3      S21:   0.0789 S22:  -0.1628 S23:  -0.2519
REMARK   3      S31:  -0.0667 S32:   0.4319 S33:  -0.0881
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.40
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK   3  POSITIONS U VALUES : RESIDUAL ONLY
REMARK   4
REMARK   4 3S5P COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-MAY-11.
REMARK 100 THE RCSB ID CODE IS RCSB065793.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 07-APR-10
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 4.2
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SSRL
REMARK 200  BEAMLINE                       : BL7-1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97946
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200  DATA SCALING SOFTWARE          : XSCALE
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13930
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.6
REMARK 200  DATA REDUNDANCY                : 3.700
REMARK 200  R MERGE                    (I) : 0.03700
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 22.3900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.36
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.3
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.53500
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.530
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2VVR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: GILAA.01163.A.A1 PS00138 AT 24 MG/ML
REMARK 280  WITH 5 MM RIBOSE-5-PHOSPHATE AGAINST JCSG+ SCREEN CONDITION A6
REMARK 280  0.2 M LI2SO4, 0.1 M PHOSPHATE/CITRATE PH 4.2, 20% PEG 1000,
REMARK 280  CRYSTAL TRACKING ID 215117A6, VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 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+1/3
REMARK 290       3555   -X+Y,-X,Z+2/3
REMARK 290       4555   Y,X,-Z
REMARK 290       5555   X-Y,-Y,-Z+2/3
REMARK 290       6555   -X,-X+Y,-Z+1/3
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       22.74667
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       45.49333
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       45.49333
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       22.74667
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2620 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11090 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -78.0 KCAL/MOL
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2310 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11410 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -74.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   2 -0.500000  0.866025  0.000000      -44.60000
REMARK 350   BIOMT2   2 -0.866025 -0.500000  0.000000      -77.24947
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000      -22.74667
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7630 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -169.0 KCAL/MOL
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 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -22.74667
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375      HOH B 176  LIES ON A SPECIAL POSITION.
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     MET A   -20
REMARK 465     ALA A   -19
REMARK 465     HIS A   -18
REMARK 465     HIS A   -17
REMARK 465     HIS A   -16
REMARK 465     HIS A   -15
REMARK 465     HIS A   -14
REMARK 465     HIS A   -13
REMARK 465     MET A   -12
REMARK 465     GLY A   -11
REMARK 465     THR A   -10
REMARK 465     LEU A    -9
REMARK 465     GLU A    -8
REMARK 465     ALA A    -7
REMARK 465     GLN A    -6
REMARK 465     THR A    -5
REMARK 465     GLN A    -4
REMARK 465     GLY A    -3
REMARK 465     GLU A    35
REMARK 465     SER A    36
REMARK 465     ASP A    37
REMARK 465     ALA A    38
REMARK 465     SER A    39
REMARK 465     VAL A    40
REMARK 465     ASP A    41
REMARK 465     TYR A    42
REMARK 465     ILE A   140
REMARK 465     SER A   141
REMARK 465     ALA A   142
REMARK 465     MET A   143
REMARK 465     GLU A   144
REMARK 465     GLU A   145
REMARK 465     MET B   -20
REMARK 465     ALA B   -19
REMARK 465     HIS B   -18
REMARK 465     HIS B   -17
REMARK 465     HIS B   -16
REMARK 465     HIS B   -15
REMARK 465     HIS B   -14
REMARK 465     HIS B   -13
REMARK 465     MET B   -12
REMARK 465     GLY B   -11
REMARK 465     THR B   -10
REMARK 465     LEU B    -9
REMARK 465     GLU B    -8
REMARK 465     ALA B    -7
REMARK 465     GLN B    -6
REMARK 465     THR B    -5
REMARK 465     GLN B    -4
REMARK 465     GLY B    -3
REMARK 465     SER B    36
REMARK 465     ASP B    37
REMARK 465     ALA B    38
REMARK 465     SER B    39
REMARK 465     VAL B    40
REMARK 465     ASP B    41
REMARK 465     TYR B    42
REMARK 465     GLY B   130
REMARK 465     GLY B   131
REMARK 465     ARG B   132
REMARK 465     HIS B   133
REMARK 465     ALA B   134
REMARK 465     ALA B   135
REMARK 465     ARG B   136
REMARK 465     ILE B   137
REMARK 465     ALA B   138
REMARK 465     LYS B   139
REMARK 465     ILE B   140
REMARK 465     SER B   141
REMARK 465     ALA B   142
REMARK 465     MET B   143
REMARK 465     GLU B   144
REMARK 465     GLU B   145
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     SER A   0    OG
REMARK 470     LYS A   2    CG   CD   CE   NZ
REMARK 470     HIS A   9    CG   ND1  CD2  CE1  NE2
REMARK 470     ARG A  12    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLN A  20    CG   CD   OE1  NE2
REMARK 470     GLU A  28    CG   CD   OE1  OE2
REMARK 470     ASP A  44    CG   OD1  OD2
REMARK 470     LYS A  47    CG   CD   CE   NZ
REMARK 470     GLU A  89    CG   CD   OE1  OE2
REMARK 470     ARG A 132    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG A 136    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS A 139    CG   CD   CE   NZ
REMARK 470     LYS B   2    CG   CD   CE   NZ
REMARK 470     GLU B  35    CG   CD   OE1  OE2
REMARK 470     ASP B  44    CG   OD1  OD2
REMARK 470     LYS B  47    CG   CD   CE   NZ
REMARK 470     ILE B  71    CG1  CG2  CD1
REMARK 470     LYS B  79    CG   CD   CE   NZ
REMARK 470     LYS B  97    CG   CD   CE   NZ
REMARK 470     ARG B 109    CG   CD   NE   CZ   NH1  NH2
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    CYS A  65     -169.23   -126.90
REMARK 500    ASP B  44      -74.64    -47.59
REMARK 500    PHE B  45       18.46    -68.71
REMARK 500    ALA B  46      -76.63    -94.84
REMARK 500    LYS B  47      -39.69    -38.97
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 RESIDUE SO4 A 146
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 147
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 146
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 147
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 148
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3QD5   RELATED DB: PDB
REMARK 900 RPIB FROM COCCIDIOIDES IMMITIS
REMARK 900 RELATED ID: GILAA.01163.A   RELATED DB: TARGETDB
DBREF  3S5P A    1   145  UNP    A8B2K2   A8B2K2_GIAIC     1    145
DBREF  3S5P B    1   145  UNP    A8B2K2   A8B2K2_GIAIC     1    145
SEQADV 3S5P MET A  -20  UNP  A8B2K2              EXPRESSION TAG
SEQADV 3S5P ALA A  -19  UNP  A8B2K2              EXPRESSION TAG
SEQADV 3S5P HIS A  -18  UNP  A8B2K2              EXPRESSION TAG
SEQADV 3S5P HIS A  -17  UNP  A8B2K2              EXPRESSION TAG
SEQADV 3S5P HIS A  -16  UNP  A8B2K2              EXPRESSION TAG
SEQADV 3S5P HIS A  -15  UNP  A8B2K2              EXPRESSION TAG
SEQADV 3S5P HIS A  -14  UNP  A8B2K2              EXPRESSION TAG
SEQADV 3S5P HIS A  -13  UNP  A8B2K2              EXPRESSION TAG
SEQADV 3S5P MET A  -12  UNP  A8B2K2              EXPRESSION TAG
SEQADV 3S5P GLY A  -11  UNP  A8B2K2              EXPRESSION TAG
SEQADV 3S5P THR A  -10  UNP  A8B2K2              EXPRESSION TAG
SEQADV 3S5P LEU A   -9  UNP  A8B2K2              EXPRESSION TAG
SEQADV 3S5P GLU A   -8  UNP  A8B2K2              EXPRESSION TAG
SEQADV 3S5P ALA A   -7  UNP  A8B2K2              EXPRESSION TAG
SEQADV 3S5P GLN A   -6  UNP  A8B2K2              EXPRESSION TAG
SEQADV 3S5P THR A   -5  UNP  A8B2K2              EXPRESSION TAG
SEQADV 3S5P GLN A   -4  UNP  A8B2K2              EXPRESSION TAG
SEQADV 3S5P GLY A   -3  UNP  A8B2K2              EXPRESSION TAG
SEQADV 3S5P PRO A   -2  UNP  A8B2K2              EXPRESSION TAG
SEQADV 3S5P GLY A   -1  UNP  A8B2K2              EXPRESSION TAG
SEQADV 3S5P SER A    0  UNP  A8B2K2              EXPRESSION TAG
SEQADV 3S5P MET B  -20  UNP  A8B2K2              EXPRESSION TAG
SEQADV 3S5P ALA B  -19  UNP  A8B2K2              EXPRESSION TAG
SEQADV 3S5P HIS B  -18  UNP  A8B2K2              EXPRESSION TAG
SEQADV 3S5P HIS B  -17  UNP  A8B2K2              EXPRESSION TAG
SEQADV 3S5P HIS B  -16  UNP  A8B2K2              EXPRESSION TAG
SEQADV 3S5P HIS B  -15  UNP  A8B2K2              EXPRESSION TAG
SEQADV 3S5P HIS B  -14  UNP  A8B2K2              EXPRESSION TAG
SEQADV 3S5P HIS B  -13  UNP  A8B2K2              EXPRESSION TAG
SEQADV 3S5P MET B  -12  UNP  A8B2K2              EXPRESSION TAG
SEQADV 3S5P GLY B  -11  UNP  A8B2K2              EXPRESSION TAG
SEQADV 3S5P THR B  -10  UNP  A8B2K2              EXPRESSION TAG
SEQADV 3S5P LEU B   -9  UNP  A8B2K2              EXPRESSION TAG
SEQADV 3S5P GLU B   -8  UNP  A8B2K2              EXPRESSION TAG
SEQADV 3S5P ALA B   -7  UNP  A8B2K2              EXPRESSION TAG
SEQADV 3S5P GLN B   -6  UNP  A8B2K2              EXPRESSION TAG
SEQADV 3S5P THR B   -5  UNP  A8B2K2              EXPRESSION TAG
SEQADV 3S5P GLN B   -4  UNP  A8B2K2              EXPRESSION TAG
SEQADV 3S5P GLY B   -3  UNP  A8B2K2              EXPRESSION TAG
SEQADV 3S5P PRO B   -2  UNP  A8B2K2              EXPRESSION TAG
SEQADV 3S5P GLY B   -1  UNP  A8B2K2              EXPRESSION TAG
SEQADV 3S5P SER B    0  UNP  A8B2K2              EXPRESSION TAG
SEQRES   1 A  166  MET ALA HIS HIS HIS HIS HIS HIS MET GLY THR LEU GLU
SEQRES   2 A  166  ALA GLN THR GLN GLY PRO GLY SER MET LYS VAL ALA PHE
SEQRES   3 A  166  ALA SER ASP HIS GLY GLY ARG ASP LEU ARG MET PHE LEU
SEQRES   4 A  166  GLN GLN ARG ALA SER ALA HIS GLY TYR GLU VAL MET ASP
SEQRES   5 A  166  LEU GLY THR GLU SER ASP ALA SER VAL ASP TYR PRO ASP
SEQRES   6 A  166  PHE ALA LYS ILE GLY CYS GLU ALA VAL THR SER GLY ARG
SEQRES   7 A  166  ALA ASP CYS CYS ILE LEU VAL CYS GLY THR GLY ILE GLY
SEQRES   8 A  166  ILE SER ILE ALA ALA ASN LYS MET LYS GLY ILE ARG CYS
SEQRES   9 A  166  ALA LEU CYS SER THR GLU TYR ASP ALA GLU MET ALA ARG
SEQRES  10 A  166  LYS HIS ASN ASN ALA ASN ALA LEU ALA LEU GLY GLY ARG
SEQRES  11 A  166  THR THR GLY PRO GLU VAL ALA ALA SER ILE LEU SER ARG
SEQRES  12 A  166  PHE LEU SER THR ASN PHE GLU GLY GLY ARG HIS ALA ALA
SEQRES  13 A  166  ARG ILE ALA LYS ILE SER ALA MET GLU GLU
SEQRES   1 B  166  MET ALA HIS HIS HIS HIS HIS HIS MET GLY THR LEU GLU
SEQRES   2 B  166  ALA GLN THR GLN GLY PRO GLY SER MET LYS VAL ALA PHE
SEQRES   3 B  166  ALA SER ASP HIS GLY GLY ARG ASP LEU ARG MET PHE LEU
SEQRES   4 B  166  GLN GLN ARG ALA SER ALA HIS GLY TYR GLU VAL MET ASP
SEQRES   5 B  166  LEU GLY THR GLU SER ASP ALA SER VAL ASP TYR PRO ASP
SEQRES   6 B  166  PHE ALA LYS ILE GLY CYS GLU ALA VAL THR SER GLY ARG
SEQRES   7 B  166  ALA ASP CYS CYS ILE LEU VAL CYS GLY THR GLY ILE GLY
SEQRES   8 B  166  ILE SER ILE ALA ALA ASN LYS MET LYS GLY ILE ARG CYS
SEQRES   9 B  166  ALA LEU CYS SER THR GLU TYR ASP ALA GLU MET ALA ARG
SEQRES  10 B  166  LYS HIS ASN ASN ALA ASN ALA LEU ALA LEU GLY GLY ARG
SEQRES  11 B  166  THR THR GLY PRO GLU VAL ALA ALA SER ILE LEU SER ARG
SEQRES  12 B  166  PHE LEU SER THR ASN PHE GLU GLY GLY ARG HIS ALA ALA
SEQRES  13 B  166  ARG ILE ALA LYS ILE SER ALA MET GLU GLU
HET    SO4  A 146       5
HET    SO4  A 147       5
HET    SO4  B 146       5
HET    SO4  B 147       5
HET    SO4  B 148       5
HETNAM     SO4 SULFATE ION
FORMUL   3  SO4    5(O4 S 2-)
FORMUL   8  HOH   *50(H2 O)
HELIX    1   1 GLY A   11  HIS A   25  1                                  15
HELIX    2   2 PRO A   43  SER A   55  1                                  13
HELIX    3   3 GLY A   68  LYS A   77  1                                  10
HELIX    4   4 THR A   88  HIS A   98  1                                  11
HELIX    5   5 GLY A  112  THR A  126  1                                  15
HELIX    6   6 GLU A  129  ALA A  135  1                                   7
HELIX    7   7 GLY B   11  HIS B   25  1                                  15
HELIX    8   8 PRO B   43  SER B   55  1                                  13
HELIX    9   9 GLY B   68  LYS B   77  1                                  10
HELIX   10  10 THR B   88  HIS B   98  1                                  11
HELIX   11  11 GLY B  112  THR B  126  1                                  15
SHEET    1   A 5 GLU A  28  GLY A  33  0
SHEET    2   A 5 LYS A   2  SER A   7  1  N  VAL A   3   O  GLU A  28
SHEET    3   A 5 CYS A  60  CYS A  65  1  O  ILE A  62   N  ALA A   4
SHEET    4   A 5 ALA A 103  GLY A 107  1  O  LEU A 104   N  LEU A  63
SHEET    5   A 5 CYS A  83  LEU A  85  1  N  ALA A  84   O  ALA A 105
SHEET    1   B 5 GLU B  28  THR B  34  0
SHEET    2   B 5 LYS B   2  SER B   7  1  N  VAL B   3   O  GLU B  28
SHEET    3   B 5 CYS B  60  CYS B  65  1  O  ILE B  62   N  ALA B   4
SHEET    4   B 5 ALA B 103  GLY B 107  1  O  LEU B 104   N  LEU B  63
SHEET    5   B 5 CYS B  83  LEU B  85  1  N  ALA B  84   O  ALA B 103
SITE     1 AC1 10 CYS A  65  GLY A  66  THR A  67  GLY A  68
SITE     2 AC1 10 ILE A  69  GLY A  70  ILE A  71  HOH A 153
SITE     3 AC1 10 HOH A 167  ASN B  99
SITE     1 AC2  4 LYS A  77  MET B  78  LYS B  79  GLY B  80
SITE     1 AC3  9 GLY A  80  ARG A  82  ARG B  12  ARG B  15
SITE     2 AC3  9 GLY B  33  THR B  34  LYS B  77  HOH B 153
SITE     3 AC3  9 HOH B 154
SITE     1 AC4  7 ASN A  99  GLY B  66  THR B  67  GLY B  68
SITE     2 AC4  7 ILE B  69  GLY B  70  HOH B 169
SITE     1 AC5  6 GLY A 130  GLY A 131  HOH A 164  PHE B  17
SITE     2 AC5  6 GLN B  20  ARG B  21
CRYST1   89.200   89.200   68.240  90.00  90.00 120.00 P 31 2 1     12
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      0.011211  0.006473  0.000000        0.00000
SCALE2      0.000000  0.012945  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014654        0.00000
      
PROCHECK
Go to PROCHECK summary
 References