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PDBsum entry 3n8y

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Oxidoreductase PDB id
3n8y
Jmol
Contents
Protein chains
553 a.a.
Ligands
HEM ×2
DIF ×2
NAG-NAG-BMA-BMA ×2
NAG-NDG-BMA-MAN-
MAN
BOG ×4
NAG-NDG
NAG-NDG-BMA-BMA
SAL
Waters ×142
HEADER    OXIDOREDUCTASE                          28-MAY-10   3N8Y
TITLE     STRUCTURE OF ASPIRIN ACETYLATED CYCLOOXYGENASE-1 IN COMPLEX WITH
TITLE    2 DICLOFENAC
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROSTAGLANDIN G/H SYNTHASE 1;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: CYCLOOXYGENASE-1, COX-1, PROSTAGLANDIN-ENDOPEROXIDE SYNTHASE
COMPND   5 1, PROSTAGLANDIN H2 SYNTHASE 1, PGH SYNTHASE 1, PGHS-1, PHS 1;
COMPND   6 EC: 1.14.99.1;
COMPND   7 ENGINEERED: YES;
COMPND   8 MOL_ID: 2;
COMPND   9 MOLECULE: PROSTAGLANDIN G/H SYNTHASE 1;
COMPND  10 CHAIN: B;
COMPND  11 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: OVIS ARIES;
SOURCE   3 ORGANISM_COMMON: SHEEP;
SOURCE   4 ORGANISM_TAXID: 9940;
SOURCE   5 STRAIN: SHEEP;
SOURCE   6 GENE: COX1, PTGS1;
SOURCE   7 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: SF21;
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PFASTBAC-HTOCOX-1;
SOURCE  12 MOL_ID: 2;
SOURCE  13 ORGANISM_SCIENTIFIC: OVIS ARIES;
SOURCE  14 ORGANISM_COMMON: SHEEP;
SOURCE  15 ORGANISM_TAXID: 9940;
SOURCE  16 GENE: COX1, PTGS1;
SOURCE  17 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE  19 EXPRESSION_SYSTEM_STRAIN: SF21;
SOURCE  20 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE  21 EXPRESSION_SYSTEM_PLASMID: PFASTBAC-HTOCOX-1
KEYWDS    COX-1, CYCLOOXYGENASE, PEROXIDASE, PROSTAGLANDIN, HEME, ASPIRIN
KEYWDS   2 ACETYLATION, DICLOFENAC, MEROHEDRAL TWINNED, OXIDOREDUCTASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    R.S.SIDHU
REVDAT   3   18-SEP-13 3N8Y    1       REMARK VERSN
REVDAT   2   01-SEP-10 3N8Y    1       JRNL
REVDAT   1   28-JUL-10 3N8Y    0
JRNL        AUTH   R.S.SIDHU,J.Y.LEE,C.YUAN,W.L.SMITH
JRNL        TITL   COMPARISON OF CYCLOOXYGENASE-1 CRYSTAL STRUCTURES:
JRNL        TITL 2 CROSS-TALK BETWEEN MONOMERS COMPRISING CYCLOOXYGENASE-1
JRNL        TITL 3 HOMODIMERS
JRNL        REF    BIOCHEMISTRY                  V.  49  7069 2010
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   20669977
JRNL        DOI    10.1021/BI1003298
REMARK   2
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0102
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) : 2.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.84
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.8
REMARK   3   NUMBER OF REFLECTIONS             : 57157
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) : 0.184
REMARK   3   R VALUE            (WORKING SET) : 0.184
REMARK   3   FREE R VALUE                     : 0.200
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.700
REMARK   3   FREE R VALUE TEST SET COUNT      : 1577
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) : 2.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.67
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3405
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 79.31
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2970
REMARK   3   BIN FREE R VALUE SET COUNT          : 91
REMARK   3   BIN FREE R VALUE                    : 0.3370
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 8807
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 453
REMARK   3   SOLVENT ATOMS            : 142
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 47.01
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.08000
REMARK   3    B22 (A**2) : -0.08000
REMARK   3    B33 (A**2) : 0.17000
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 OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.046
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.189
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 21.955
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.936
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.930
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9648 ; 0.006 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 13181 ; 1.020 ; 2.027
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1112 ; 3.974 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   423 ;36.365 ;23.191
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1400 ;15.210 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    53 ;12.611 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1436 ; 0.058 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7344 ; 0.003 ; 0.021
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):  5568 ; 0.062 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8981 ; 0.120 ; 2.000
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4080 ; 0.207 ; 3.000
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4198 ; 0.342 ; 4.500
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL
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 : 0
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   LOOSE POSITIONAL   1    A    (A):   4300 ;  0.25 ;  5.00
REMARK   3   LOOSE THERMAL      1    A (A**2):   4300 ;  0.29 ; 10.00
REMARK   3
REMARK   3  TWIN DETAILS
REMARK   3   NUMBER OF TWIN DOMAINS  : 2
REMARK   3      TWIN DOMAIN   : 1
REMARK   3      TWIN OPERATOR : H, K, L
REMARK   3      TWIN FRACTION : 0.501
REMARK   3      TWIN DOMAIN   : 2
REMARK   3      TWIN OPERATOR : -H-K, K, -L
REMARK   3      TWIN FRACTION : 0.499
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 9
REMARK   3
REMARK   3   TLS GROUP : 1
REMARK   3    NUMBER OF COMPONENTS GROUP : 3
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A    32        A   584
REMARK   3    RESIDUE RANGE :   A   601        A   601
REMARK   3    RESIDUE RANGE :   A   701        A   701
REMARK   3    ORIGIN FOR THE GROUP (A):  36.1300 -52.2220  -1.5170
REMARK   3    T TENSOR
REMARK   3      T11:   0.1815 T22:   0.0782
REMARK   3      T33:   0.2994 T12:   0.0762
REMARK   3      T13:   0.0056 T23:  -0.0262
REMARK   3    L TENSOR
REMARK   3      L11:   1.2515 L22:   0.7032
REMARK   3      L33:   1.3250 L12:   0.3671
REMARK   3      L13:  -0.3130 L23:  -0.1823
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1264 S12:   0.1773 S13:  -0.1272
REMARK   3      S21:  -0.2167 S22:  -0.0089 S23:  -0.0651
REMARK   3      S31:   0.0834 S32:   0.0297 S33:   0.1353
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   751        A   751
REMARK   3    ORIGIN FOR THE GROUP (A):  19.8760 -40.8170  -3.0920
REMARK   3    T TENSOR
REMARK   3      T11:   0.1820 T22:   0.1355
REMARK   3      T33:   0.3361 T12:   0.0954
REMARK   3      T13:  -0.0936 T23:  -0.0348
REMARK   3    L TENSOR
REMARK   3      L11: 111.1356 L22:  29.7952
REMARK   3      L33:  27.4438 L12:  60.0286
REMARK   3      L13:  22.8620 L23:  12.5125
REMARK   3    S TENSOR
REMARK   3      S11:  -1.5216 S12:   0.9891 S13:   1.6877
REMARK   3      S21:  -0.7167 S22:   0.4824 S23:   0.8127
REMARK   3      S31:  -1.1872 S32:  -0.4624 S33:   1.0392
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 :   B    32        B   601
REMARK   3    ORIGIN FOR THE GROUP (A):  25.5940 -58.0450  36.8820
REMARK   3    T TENSOR
REMARK   3      T11:   0.1569 T22:   0.1547
REMARK   3      T33:   0.3071 T12:   0.0947
REMARK   3      T13:  -0.0116 T23:   0.0671
REMARK   3    L TENSOR
REMARK   3      L11:   1.1632 L22:   0.7944
REMARK   3      L33:   1.0719 L12:   0.3970
REMARK   3      L13:  -0.0973 L23:  -0.1514
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0104 S12:  -0.3145 S13:  -0.1297
REMARK   3      S21:   0.1604 S22:  -0.0791 S23:  -0.0133
REMARK   3      S31:  -0.0349 S32:   0.0804 S33:   0.0895
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   661        A   662
REMARK   3    ORIGIN FOR THE GROUP (A):   0.7890 -57.7630  -4.4760
REMARK   3    T TENSOR
REMARK   3      T11:   0.0346 T22:   0.0346
REMARK   3      T33:   0.0346 T12:   0.0000
REMARK   3      T13:   0.0000 T23:   0.0000
REMARK   3    L TENSOR
REMARK   3      L11:   0.0000 L22:   0.0000
REMARK   3      L33:   0.0000 L12:   0.0000
REMARK   3      L13:   0.0000 L23:   0.0000
REMARK   3    S TENSOR
REMARK   3      S11:   0.0000 S12:   0.0000 S13:   0.0000
REMARK   3      S21:   0.0000 S22:   0.0000 S23:   0.0000
REMARK   3      S31:   0.0000 S32:   0.0000 S33:  -0.0000
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 :   A   681        A   684
REMARK   3    ORIGIN FOR THE GROUP (A):  64.7310 -58.4530 -19.8920
REMARK   3    T TENSOR
REMARK   3      T11:   0.4749 T22:   0.5775
REMARK   3      T33:   0.3327 T12:  -0.0789
REMARK   3      T13:   0.0464 T23:  -0.0515
REMARK   3    L TENSOR
REMARK   3      L11:  22.3220 L22:  22.7773
REMARK   3      L33:  -6.6021 L12:  -0.0060
REMARK   3      L13:  -1.7254 L23:   0.4505
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1340 S12:   1.3908 S13:   0.2576
REMARK   3      S21:  -1.5419 S22:   0.0177 S23:  -0.1969
REMARK   3      S31:   0.0150 S32:  -0.1360 S33:   0.1163
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 :   A   671        A   675
REMARK   3    ORIGIN FOR THE GROUP (A):  29.8270 -79.8440  13.7110
REMARK   3    T TENSOR
REMARK   3      T11:   0.4728 T22:   0.5986
REMARK   3      T33:   0.4414 T12:  -0.1903
REMARK   3      T13:   0.0130 T23:   0.0794
REMARK   3    L TENSOR
REMARK   3      L11:  -0.8711 L22:   4.8975
REMARK   3      L33:   0.0134 L12:  -1.0142
REMARK   3      L13:   0.2264 L23:   3.0802
REMARK   3    S TENSOR
REMARK   3      S11:   0.0619 S12:  -0.1533 S13:  -0.0501
REMARK   3      S21:  -0.0095 S22:   0.0273 S23:  -0.0699
REMARK   3      S31:   0.0973 S32:  -0.1612 S33:  -0.0892
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  1661        B  1662
REMARK   3    ORIGIN FOR THE GROUP (A):  50.9290 -30.1910  40.6320
REMARK   3    T TENSOR
REMARK   3      T11:   0.5403 T22:   0.2679
REMARK   3      T33:   0.4480 T12:  -0.0114
REMARK   3      T13:  -0.1563 T23:  -0.0856
REMARK   3    L TENSOR
REMARK   3      L11:  75.3891 L22:  -4.5348
REMARK   3      L33:  -1.9642 L12:   8.7314
REMARK   3      L13:  -9.3571 L23:  -1.7962
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1846 S12:  -0.8229 S13:  -0.6153
REMARK   3      S21:  -0.1430 S22:   0.0405 S23:  -0.2943
REMARK   3      S31:  -0.1710 S32:   0.0407 S33:   0.1440
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  1681        B  1684
REMARK   3    ORIGIN FOR THE GROUP (A):  15.4170 -85.8760  54.9390
REMARK   3    T TENSOR
REMARK   3      T11:   0.6986 T22:   0.7382
REMARK   3      T33:   0.9894 T12:  -0.3418
REMARK   3      T13:   0.2966 T23:   0.0190
REMARK   3    L TENSOR
REMARK   3      L11:  -0.3819 L22:   5.1095
REMARK   3      L33:  -2.9265 L12:  -2.0330
REMARK   3      L13:   2.1478 L23:  -3.6882
REMARK   3    S TENSOR
REMARK   3      S11:   0.0916 S12:   0.0787 S13:   0.5510
REMARK   3      S21:   0.3731 S22:  -0.2998 S23:  -0.2219
REMARK   3      S31:  -0.2131 S32:  -0.1849 S33:   0.2082
REMARK   3
REMARK   3   TLS GROUP : 9
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B  1671        B  1675
REMARK   3    ORIGIN FOR THE GROUP (A):  52.3970 -66.9910  21.5780
REMARK   3    T TENSOR
REMARK   3      T11:   0.5240 T22:   0.6934
REMARK   3      T33:   0.6261 T12:   0.0150
REMARK   3      T13:   0.0413 T23:   0.0987
REMARK   3    L TENSOR
REMARK   3      L11:  -2.0756 L22:  11.4354
REMARK   3      L33:   7.9660 L12:   2.9595
REMARK   3      L13:   3.0120 L23:   2.2560
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0742 S12:   0.0547 S13:  -0.6515
REMARK   3      S21:  -0.8765 S22:   1.4691 S23:  -1.1206
REMARK   3      S31:  -0.0589 S32:   0.8164 S33:  -1.3950
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
REMARK   4
REMARK   4 3N8Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUN-10.
REMARK 100 THE RCSB ID CODE IS RCSB059529.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 25-JUL-08
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 21-ID-F
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97872
REMARK 200  MONOCHROMATOR                  : C(111)
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 58765
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.840
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0
REMARK 200  DATA REDUNDANCY                : 7.100
REMARK 200  R MERGE                    (I) : 0.07700
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 23.7391
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.67
REMARK 200  COMPLETENESS FOR SHELL     (%) : 79.3
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         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1Q4G
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 68.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE, LITHIUM CHLORIDE,
REMARK 280  SODIUM AZIDE, N-OCTYL GLUCOSIDE, PH 6.5, VAPOR DIFFUSION, SITTING
REMARK 280  DROP, TEMPERATURE 273K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
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   -X,-Y,Z+1/2
REMARK 290       5555   Y,-X+Y,Z+1/6
REMARK 290       6555   X-Y,X,Z+5/6
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       68.73733
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       34.36867
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       51.55300
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       17.18433
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       85.92167
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 16300 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     ARG A  79    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG A  83    CG   CD   NE   CZ   NH1  NH2
REMARK 470     PHE A 107    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 169    CG   CD   CE   NZ
REMARK 470     GLN A 170    CG   CD   OE1  NE2
REMARK 470     GLU A 175    CG   CD   OE1  OE2
REMARK 470     ARG A 179    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS A 186    CG   CD   CE   NZ
REMARK 470     GLU A 239    CG   CD   OE1  OE2
REMARK 470     GLN A 243    CG   CD   OE1  NE2
REMARK 470     LYS A 248    CG   CD   CE   NZ
REMARK 470     GLU A 268    CG   CD   OE1  OE2
REMARK 470     ARG A 277    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLN A 282    CG   CD   OE1  NE2
REMARK 470     LYS A 453    CG   CD   CE   NZ
REMARK 470     LYS A 473    CG   CD   CE   NZ
REMARK 470     GLN A 479    CG   CD   OE1  NE2
REMARK 470     LYS A 485    CG   CD   CE   NZ
REMARK 470     MET A 487    CG   SD   CE
REMARK 470     GLU A 492    CG   CD   OE1  OE2
REMARK 470     LYS A 511    CG   CD   CE   NZ
REMARK 470     LYS A 573    CG   CD   CE   NZ
REMARK 470     ARG B  79    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS B 168    CD   CE   NZ
REMARK 470     LYS B 169    CD   CE   NZ
REMARK 470     GLN B 170    CG   CD   OE1  NE2
REMARK 470     GLU B 175    CG   CD   OE1  OE2
REMARK 470     ARG B 179    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS B 186    CG   CD   CE   NZ
REMARK 470     LYS B 248    CG   CD   CE   NZ
REMARK 470     GLU B 268    CG   CD   OE1  OE2
REMARK 470     ARG B 277    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS B 317    CG   CD   CE   NZ
REMARK 470     ARG B 396    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS B 453    CG   CD   CE   NZ
REMARK 470     ARG B 459    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS B 473    CG   CD   CE   NZ
REMARK 470     LYS B 485    CG   CD   CE   NZ
REMARK 470     GLU B 486    CG   CD   OE1  OE2
REMARK 470     MET B 487    CG   SD   CE
REMARK 470     GLU B 490    CG   CD   OE1  OE2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480   M RES C SSEQI ATOMS
REMARK 480     GLN B  479   CD   OE1  NE2
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   ND2  ASN B    68     O5   NAG B  1661              1.46
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    ARG A  61       19.24     57.12
REMARK 500    THR A 129      -73.75   -105.20
REMARK 500    ASP A 135       36.71    -98.28
REMARK 500    ASP A 158       31.30    -95.76
REMARK 500    ARG A 185      -84.02    -91.46
REMARK 500    GLU A 347      -52.76   -132.58
REMARK 500    TRP A 387       53.08    -91.56
REMARK 500    GLU A 484     -165.51   -122.91
REMARK 500    HIS A 513     -171.99    -54.27
REMARK 500    ASN A 515       74.36     38.49
REMARK 500    VAL B  33      118.41     69.09
REMARK 500    THR B 129      -81.67   -102.58
REMARK 500    ASP B 135       32.96    -95.33
REMARK 500    GLU B 347      -49.75   -131.18
REMARK 500    TRP B 387       59.66    -94.83
REMARK 500    PHE B 409       17.51     59.14
REMARK 500    ASN B 515      -17.90     96.32
REMARK 500    VAL B 568      -60.51    -95.31
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    PHE B 529         16.72
REMARK 500    OAS B 530        -16.08
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 B 592        DISTANCE =  5.12 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEM B 601  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 388   NE2
REMARK 620 2 HEM B 601   NA   93.7
REMARK 620 3 HEM B 601   NB   87.5  90.0
REMARK 620 4 HEM B 601   NC   86.5 179.2  89.3
REMARK 620 5 HEM B 601   ND   93.6  90.1 178.9  90.7
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEM A 601  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 388   NE2
REMARK 620 2 HEM A 601   NA   97.1
REMARK 620 3 HEM A 601   NB   87.8  89.6
REMARK 620 4 HEM A 601   NC   84.8 178.0  89.8
REMARK 620 5 HEM A 601   ND   92.5  89.7 179.2  91.0
REMARK 620 6 HOH A  22   O   171.6  78.5  85.1  99.5  94.6
REMARK 620 N                    1     2     3     4     5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIF A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 682
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 683
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 684
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG A 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 673
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 674
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 675
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 751
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 754
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1661
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG B 1662
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1681
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1682
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA B 1683
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA B 1684
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1671
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG B 1672
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA B 1673
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA B 1674
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAL B 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIF B 585
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG B 1750
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG B 1751
DBREF  3N8Y A   32   584  UNP    P05979   PGH1_SHEEP      32    584
DBREF  3N8Y B   32   584  UNP    P05979   PGH1_SHEEP      32    584
SEQADV 3N8Y LEU A   92  UNP  P05979    MET    92 CONFLICT
SEQADV 3N8Y LEU B   92  UNP  P05979    MET    92 CONFLICT
SEQADV 3N8Y OAS B  530  UNP  P05979    SER   530 MICROHETEROGENEITY
SEQRES   1 A  553  PRO VAL ASN PRO CYS CYS TYR TYR PRO CYS GLN HIS GLN
SEQRES   2 A  553  GLY ILE CYS VAL ARG PHE GLY LEU ASP ARG TYR GLN CYS
SEQRES   3 A  553  ASP CYS THR ARG THR GLY TYR SER GLY PRO ASN CYS THR
SEQRES   4 A  553  ILE PRO GLU ILE TRP THR TRP LEU ARG THR THR LEU ARG
SEQRES   5 A  553  PRO SER PRO SER PHE ILE HIS PHE LEU LEU THR HIS GLY
SEQRES   6 A  553  ARG TRP LEU TRP ASP PHE VAL ASN ALA THR PHE ILE ARG
SEQRES   7 A  553  ASP THR LEU MET ARG LEU VAL LEU THR VAL ARG SER ASN
SEQRES   8 A  553  LEU ILE PRO SER PRO PRO THR TYR ASN ILE ALA HIS ASP
SEQRES   9 A  553  TYR ILE SER TRP GLU SER PHE SER ASN VAL SER TYR TYR
SEQRES  10 A  553  THR ARG ILE LEU PRO SER VAL PRO ARG ASP CYS PRO THR
SEQRES  11 A  553  PRO MET GLY THR LYS GLY LYS LYS GLN LEU PRO ASP ALA
SEQRES  12 A  553  GLU PHE LEU SER ARG ARG PHE LEU LEU ARG ARG LYS PHE
SEQRES  13 A  553  ILE PRO ASP PRO GLN GLY THR ASN LEU MET PHE ALA PHE
SEQRES  14 A  553  PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR SER
SEQRES  15 A  553  GLY LYS MET GLY PRO GLY PHE THR LYS ALA LEU GLY HIS
SEQRES  16 A  553  GLY VAL ASP LEU GLY HIS ILE TYR GLY ASP ASN LEU GLU
SEQRES  17 A  553  ARG GLN TYR GLN LEU ARG LEU PHE LYS ASP GLY LYS LEU
SEQRES  18 A  553  LYS TYR GLN MET LEU ASN GLY GLU VAL TYR PRO PRO SER
SEQRES  19 A  553  VAL GLU GLU ALA PRO VAL LEU MET HIS TYR PRO ARG GLY
SEQRES  20 A  553  ILE PRO PRO GLN SER GLN MET ALA VAL GLY GLN GLU VAL
SEQRES  21 A  553  PHE GLY LEU LEU PRO GLY LEU MET LEU TYR ALA THR ILE
SEQRES  22 A  553  TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP LEU LEU LYS
SEQRES  23 A  553  ALA GLU HIS PRO THR TRP GLY ASP GLU GLN LEU PHE GLN
SEQRES  24 A  553  THR ALA ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE
SEQRES  25 A  553  VAL ILE GLU GLU TYR VAL GLN GLN LEU SER GLY TYR PHE
SEQRES  26 A  553  LEU GLN LEU LYS PHE ASP PRO GLU LEU LEU PHE GLY ALA
SEQRES  27 A  553  GLN PHE GLN TYR ARG ASN ARG ILE ALA MET GLU PHE ASN
SEQRES  28 A  553  GLN LEU TYR HIS TRP HIS PRO LEU MET PRO ASP SER PHE
SEQRES  29 A  553  ARG VAL GLY PRO GLN ASP TYR SER TYR GLU GLN PHE LEU
SEQRES  30 A  553  PHE ASN THR SER MET LEU VAL ASP TYR GLY VAL GLU ALA
SEQRES  31 A  553  LEU VAL ASP ALA PHE SER ARG GLN PRO ALA GLY ARG ILE
SEQRES  32 A  553  GLY GLY GLY ARG ASN ILE ASP HIS HIS ILE LEU HIS VAL
SEQRES  33 A  553  ALA VAL ASP VAL ILE LYS GLU SER ARG VAL LEU ARG LEU
SEQRES  34 A  553  GLN PRO PHE ASN GLU TYR ARG LYS ARG PHE GLY MET LYS
SEQRES  35 A  553  PRO TYR THR SER PHE GLN GLU LEU THR GLY GLU LYS GLU
SEQRES  36 A  553  MET ALA ALA GLU LEU GLU GLU LEU TYR GLY ASP ILE ASP
SEQRES  37 A  553  ALA LEU GLU PHE TYR PRO GLY LEU LEU LEU GLU LYS CYS
SEQRES  38 A  553  HIS PRO ASN SER ILE PHE GLY GLU SER MET ILE GLU MET
SEQRES  39 A  553  GLY ALA PRO PHE SER LEU LYS GLY LEU LEU GLY ASN PRO
SEQRES  40 A  553  ILE CYS SER PRO GLU TYR TRP LYS ALA SER THR PHE GLY
SEQRES  41 A  553  GLY GLU VAL GLY PHE ASN LEU VAL LYS THR ALA THR LEU
SEQRES  42 A  553  LYS LYS LEU VAL CYS LEU ASN THR LYS THR CYS PRO TYR
SEQRES  43 A  553  VAL SER PHE HIS VAL PRO ASP
SEQRES   1 B  553  PRO VAL ASN PRO CYS CYS TYR TYR PRO CYS GLN HIS GLN
SEQRES   2 B  553  GLY ILE CYS VAL ARG PHE GLY LEU ASP ARG TYR GLN CYS
SEQRES   3 B  553  ASP CYS THR ARG THR GLY TYR SER GLY PRO ASN CYS THR
SEQRES   4 B  553  ILE PRO GLU ILE TRP THR TRP LEU ARG THR THR LEU ARG
SEQRES   5 B  553  PRO SER PRO SER PHE ILE HIS PHE LEU LEU THR HIS GLY
SEQRES   6 B  553  ARG TRP LEU TRP ASP PHE VAL ASN ALA THR PHE ILE ARG
SEQRES   7 B  553  ASP THR LEU MET ARG LEU VAL LEU THR VAL ARG SER ASN
SEQRES   8 B  553  LEU ILE PRO SER PRO PRO THR TYR ASN ILE ALA HIS ASP
SEQRES   9 B  553  TYR ILE SER TRP GLU SER PHE SER ASN VAL SER TYR TYR
SEQRES  10 B  553  THR ARG ILE LEU PRO SER VAL PRO ARG ASP CYS PRO THR
SEQRES  11 B  553  PRO MET GLY THR LYS GLY LYS LYS GLN LEU PRO ASP ALA
SEQRES  12 B  553  GLU PHE LEU SER ARG ARG PHE LEU LEU ARG ARG LYS PHE
SEQRES  13 B  553  ILE PRO ASP PRO GLN GLY THR ASN LEU MET PHE ALA PHE
SEQRES  14 B  553  PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR SER
SEQRES  15 B  553  GLY LYS MET GLY PRO GLY PHE THR LYS ALA LEU GLY HIS
SEQRES  16 B  553  GLY VAL ASP LEU GLY HIS ILE TYR GLY ASP ASN LEU GLU
SEQRES  17 B  553  ARG GLN TYR GLN LEU ARG LEU PHE LYS ASP GLY LYS LEU
SEQRES  18 B  553  LYS TYR GLN MET LEU ASN GLY GLU VAL TYR PRO PRO SER
SEQRES  19 B  553  VAL GLU GLU ALA PRO VAL LEU MET HIS TYR PRO ARG GLY
SEQRES  20 B  553  ILE PRO PRO GLN SER GLN MET ALA VAL GLY GLN GLU VAL
SEQRES  21 B  553  PHE GLY LEU LEU PRO GLY LEU MET LEU TYR ALA THR ILE
SEQRES  22 B  553  TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP LEU LEU LYS
SEQRES  23 B  553  ALA GLU HIS PRO THR TRP GLY ASP GLU GLN LEU PHE GLN
SEQRES  24 B  553  THR ALA ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE
SEQRES  25 B  553  VAL ILE GLU GLU TYR VAL GLN GLN LEU SER GLY TYR PHE
SEQRES  26 B  553  LEU GLN LEU LYS PHE ASP PRO GLU LEU LEU PHE GLY ALA
SEQRES  27 B  553  GLN PHE GLN TYR ARG ASN ARG ILE ALA MET GLU PHE ASN
SEQRES  28 B  553  GLN LEU TYR HIS TRP HIS PRO LEU MET PRO ASP SER PHE
SEQRES  29 B  553  ARG VAL GLY PRO GLN ASP TYR SER TYR GLU GLN PHE LEU
SEQRES  30 B  553  PHE ASN THR SER MET LEU VAL ASP TYR GLY VAL GLU ALA
SEQRES  31 B  553  LEU VAL ASP ALA PHE SER ARG GLN PRO ALA GLY ARG ILE
SEQRES  32 B  553  GLY GLY GLY ARG ASN ILE ASP HIS HIS ILE LEU HIS VAL
SEQRES  33 B  553  ALA VAL ASP VAL ILE LYS GLU SER ARG VAL LEU ARG LEU
SEQRES  34 B  553  GLN PRO PHE ASN GLU TYR ARG LYS ARG PHE GLY MET LYS
SEQRES  35 B  553  PRO TYR THR SER PHE GLN GLU LEU THR GLY GLU LYS GLU
SEQRES  36 B  553  MET ALA ALA GLU LEU GLU GLU LEU TYR GLY ASP ILE ASP
SEQRES  37 B  553  ALA LEU GLU PHE TYR PRO GLY LEU LEU LEU GLU LYS CYS
SEQRES  38 B  553  HIS PRO ASN SER ILE PHE GLY GLU SER MET ILE GLU MET
SEQRES  39 B  553  GLY ALA PRO PHE OAS LEU LYS GLY LEU LEU GLY ASN PRO
SEQRES  40 B  553  ILE CYS SER PRO GLU TYR TRP LYS ALA SER THR PHE GLY
SEQRES  41 B  553  GLY GLU VAL GLY PHE ASN LEU VAL LYS THR ALA THR LEU
SEQRES  42 B  553  LYS LYS LEU VAL CYS LEU ASN THR LYS THR CYS PRO TYR
SEQRES  43 B  553  VAL SER PHE HIS VAL PRO ASP
MODRES 3N8Y ASN B   68  ASN  GLYCOSYLATION SITE
MODRES 3N8Y ASN A  144  ASN  GLYCOSYLATION SITE
MODRES 3N8Y ASN A  410  ASN  GLYCOSYLATION SITE
MODRES 3N8Y ASN B  144  ASN  GLYCOSYLATION SITE
MODRES 3N8Y ASN B  410  ASN  GLYCOSYLATION SITE
MODRES 3N8Y OAS B  530  SER  O-ACETYLSERINE
HET    OAS  B 530      15
HET    HEM  A 601      43
HET    DIF  A 701      19
HET    NAG  A 681      14
HET    NAG  A 682      14
HET    BMA  A 683      11
HET    BMA  A 684      11
HET    NAG  A 671      14
HET    NDG  A 672      14
HET    BMA  A 673      11
HET    MAN  A 674      11
HET    MAN  A 675      11
HET    BOG  A 751      20
HET    BOG  A 754      20
HET    HEM  B 601      43
HET    NAG  B1661      14
HET    NDG  B1662      14
HET    NAG  B1681      14
HET    NAG  B1682      14
HET    BMA  B1683      11
HET    BMA  B1684      11
HET    NAG  B1671      14
HET    NDG  B1672      14
HET    BMA  B1673      11
HET    BMA  B1674      11
HET    SAL  B 900      10
HET    DIF  B 585      19
HET    BOG  B1750      20
HET    BOG  B1751      20
HETNAM     OAS O-ACETYLSERINE
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM     DIF 2-[2,6-DICHLOROPHENYL)AMINO]BENZENEACETIC ACID
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     BMA BETA-D-MANNOSE
HETNAM     NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE
HETNAM     MAN ALPHA-D-MANNOSE
HETNAM     BOG B-OCTYLGLUCOSIDE
HETNAM     SAL 2-HYDROXYBENZOIC ACID
HETSYN     HEM HEME
HETSYN     DIF DICLOFENAC
HETSYN     SAL SALICYLIC ACID
FORMUL   2  OAS    C5 H9 N O4
FORMUL   3  HEM    2(C34 H32 FE N4 O4)
FORMUL   4  DIF    2(C14 H11 CL2 N O2)
FORMUL   5  NAG    7(C8 H15 N O6)
FORMUL   5  BMA    7(C6 H12 O6)
FORMUL   6  NDG    3(C8 H15 N O6)
FORMUL   6  MAN    2(C6 H12 O6)
FORMUL   7  BOG    4(C14 H28 O6)
FORMUL  13  SAL    C7 H6 O3
FORMUL  17  HOH   *142(H2 O)
HELIX    1   1 ASN A   34  TYR A   39  5                                   6
HELIX    2   2 GLU A   73  ARG A   83  1                                  11
HELIX    3   3 SER A   85  THR A   94  1                                  10
HELIX    4   4 GLY A   96  ALA A  105  1                                  10
HELIX    5   5 PHE A  107  ASN A  122  1                                  16
HELIX    6   6 SER A  138  ASN A  144  1                                   7
HELIX    7   7 ASP A  173  LEU A  182  1                                  10
HELIX    8   8 ASN A  195  HIS A  207  1                                  13
HELIX    9   9 ASN A  237  ARG A  245  1                                   9
HELIX   10  10 GLN A  289  LEU A  294  5                                   6
HELIX   11  11 LEU A  295  HIS A  320  1                                  26
HELIX   12  12 GLY A  324  GLU A  347  1                                  24
HELIX   13  13 GLU A  347  GLY A  354  1                                   8
HELIX   14  14 ASP A  362  PHE A  367  5                                   6
HELIX   15  15 ALA A  378  TYR A  385  1                                   8
HELIX   16  16 TRP A  387  MET A  391  5                                   5
HELIX   17  17 SER A  403  LEU A  408  1                                   6
HELIX   18  18 SER A  412  GLY A  418  1                                   7
HELIX   19  19 GLY A  418  GLN A  429  1                                  12
HELIX   20  20 ILE A  444  ARG A  459  1                                  16
HELIX   21  21 PRO A  462  PHE A  470  1                                   9
HELIX   22  22 SER A  477  GLY A  483  1                                   7
HELIX   23  23 LYS A  485  GLY A  496  1                                  12
HELIX   24  24 ASP A  497  LEU A  501  5                                   5
HELIX   25  25 GLU A  502  LEU A  509  1                                   8
HELIX   26  26 GLY A  519  LEU A  535  1                                  17
HELIX   27  27 ASN A  537  SER A  541  5                                   5
HELIX   28  28 ALA A  547  PHE A  550  5                                   4
HELIX   29  29 GLY A  551  THR A  561  1                                  11
HELIX   30  30 THR A  563  LEU A  570  1                                   8
HELIX   31  31 ASN B   34  TYR B   39  5                                   6
HELIX   32  32 GLU B   73  LEU B   82  1                                  10
HELIX   33  33 SER B   85  THR B   94  1                                  10
HELIX   34  34 GLY B   96  ALA B  105  1                                  10
HELIX   35  35 PHE B  107  ASN B  122  1                                  16
HELIX   36  36 SER B  138  ASN B  144  1                                   7
HELIX   37  37 ASP B  173  LEU B  182  1                                  10
HELIX   38  38 ASN B  195  HIS B  207  1                                  13
HELIX   39  39 ASN B  237  ARG B  245  1                                   9
HELIX   40  40 PRO B  280  GLN B  284  5                                   5
HELIX   41  41 VAL B  291  LEU B  294  5                                   4
HELIX   42  42 LEU B  295  HIS B  320  1                                  26
HELIX   43  43 GLY B  324  GLU B  347  1                                  24
HELIX   44  44 GLU B  347  GLY B  354  1                                   8
HELIX   45  45 ASP B  362  ALA B  369  5                                   8
HELIX   46  46 ALA B  378  TYR B  385  1                                   8
HELIX   47  47 TRP B  387  MET B  391  5                                   5
HELIX   48  48 SER B  403  LEU B  408  1                                   6
HELIX   49  49 SER B  412  GLN B  429  1                                  18
HELIX   50  50 ILE B  444  ARG B  459  1                                  16
HELIX   51  51 PRO B  462  PHE B  470  1                                   9
HELIX   52  52 SER B  477  GLY B  483  1                                   7
HELIX   53  53 LYS B  485  GLY B  496  1                                  12
HELIX   54  54 ASP B  497  LEU B  501  5                                   5
HELIX   55  55 GLU B  502  LEU B  508  1                                   7
HELIX   56  56 GLY B  519  GLY B  536  1                                  18
HELIX   57  57 ASN B  537  SER B  541  5                                   5
HELIX   58  58 ALA B  547  GLY B  551  5                                   5
HELIX   59  59 GLY B  552  THR B  561  1                                  10
HELIX   60  60 THR B  563  CYS B  569  1                                   7
HELIX   61  61 LEU B  570  THR B  572  5                                   3
SHEET    1   A 2 ILE A  46  PHE A  50  0
SHEET    2   A 2 ARG A  54  ASP A  58 -1  O  ARG A  54   N  PHE A  50
SHEET    1   B 2 TYR A  64  SER A  65  0
SHEET    2   B 2 ILE A  71  PRO A  72 -1  O  ILE A  71   N  SER A  65
SHEET    1   C 2 GLN A 255  LEU A 257  0
SHEET    2   C 2 GLU A 260  TYR A 262 -1  O  GLU A 260   N  LEU A 257
SHEET    1   D 2 PHE A 395  VAL A 397  0
SHEET    2   D 2 GLN A 400  TYR A 402 -1  O  TYR A 402   N  PHE A 395
SHEET    1   E 2 ILE B  46  PHE B  50  0
SHEET    2   E 2 ARG B  54  ASP B  58 -1  O  GLN B  56   N  VAL B  48
SHEET    1   F 2 TYR B  64  SER B  65  0
SHEET    2   F 2 ILE B  71  PRO B  72 -1  O  ILE B  71   N  SER B  65
SHEET    1   G 2 GLN B 255  LEU B 257  0
SHEET    2   G 2 GLU B 260  TYR B 262 -1  O  TYR B 262   N  GLN B 255
SHEET    1   H 2 PHE B 395  VAL B 397  0
SHEET    2   H 2 GLN B 400  TYR B 402 -1  O  TYR B 402   N  PHE B 395
SSBOND   1 CYS A   36    CYS A   47                          1555   1555  2.04
SSBOND   2 CYS A   37    CYS A  159                          1555   1555  2.04
SSBOND   3 CYS A   41    CYS A   57                          1555   1555  2.03
SSBOND   4 CYS A   59    CYS A   69                          1555   1555  2.03
SSBOND   5 CYS A  569    CYS A  575                          1555   1555  2.04
SSBOND   6 CYS B   36    CYS B   47                          1555   1555  2.04
SSBOND   7 CYS B   37    CYS B  159                          1555   1555  2.03
SSBOND   8 CYS B   41    CYS B   57                          1555   1555  2.03
SSBOND   9 CYS B   59    CYS B   69                          1555   1555  2.03
SSBOND  10 CYS B  569    CYS B  575                          1555   1555  2.03
LINK         ND2 ASN B  68                 C1  NAG B1661     1555   1555  1.38
LINK         ND2 ASN A 144                 C1  NAG A 671     1555   1555  1.44
LINK         ND2 ASN A 410                 C1  NAG A 681     1555   1555  1.44
LINK         ND2 ASN B 144                 C1  NAG B1671     1555   1555  1.44
LINK         O6  MAN A 674                 C1  MAN A 675     1555   1555  1.45
LINK         O4  NAG A 681                 C1  NAG A 682     1555   1555  1.45
LINK         O4  NAG A 671                 C1  NDG A 672     1555   1555  1.45
LINK         O4  NAG B1661                 C1  NDG B1662     1555   1555  1.46
LINK         O4  NAG B1671                 C1  NDG B1672     1555   1555  1.46
LINK         NE2 HIS B 388                FE   HEM B 601     1555   1555  1.87
LINK         NE2 HIS A 388                FE   HEM A 601     1555   1555  1.87
LINK        FE   HEM A 601                 O   HOH A  22     1555   1555  2.15
LINK         C  APHE B 529                 N  AOAS B 530     1555   1555  1.27
LINK         C  BPHE B 529                 N  BOAS B 530     1555   1555  1.45
LINK         ND2 ASN B 410                 C1  NAG B1681     1555   1555  1.44
LINK         O6  BMA B1683                 C1  BMA B1684     1555   1555  1.44
LINK         O6  BMA A 683                 C1  BMA A 684     1555   1555  1.45
LINK         O6  BMA B1673                 C1  BMA B1674     1555   1555  1.45
LINK         O4  NAG B1681                 C1  NAG B1682     1555   1555  1.45
LINK         O4  NAG B1682                 C1  BMA B1683     1555   1555  1.45
LINK         O6  BMA A 673                 C1  MAN A 674     1555   1555  1.45
LINK         O4  NAG A 682                 C1  BMA A 683     1555   1555  1.45
LINK         O4  NDG B1672                 C1  BMA B1673     1555   1555  1.45
LINK         O4  NDG A 672                 C1  BMA A 673     1555   1555  1.46
LINK         C  AOAS B 530                 N  ALEU B 531     1555   1555  1.26
LINK         C  BOAS B 530                 N  BLEU B 531     1555   1555  1.26
CISPEP   1 SER A  126    PRO A  127          0         0.40
CISPEP   2 SER B  126    PRO B  127          0        -0.32
SITE     1 AC1 15 HOH A  22  TYR A 148  ALA A 199  ALA A 202
SITE     2 AC1 15 GLN A 203  THR A 206  PHE A 210  THR A 212
SITE     3 AC1 15 LEU A 295  ASN A 382  TYR A 385  HIS A 386
SITE     4 AC1 15 TRP A 387  HIS A 388  MET A 391
SITE     1 AC2 13 VAL A 349  LEU A 352  SER A 353  TYR A 355
SITE     2 AC2 13 TYR A 385  TRP A 387  MET A 522  ILE A 523
SITE     3 AC2 13 GLY A 526  ALA A 527  SER A 530  LEU A 531
SITE     4 AC2 13 HOH A 608
SITE     1 AC3  8 TYR A 402  GLN A 406  ASN A 410  MET A 413
SITE     2 AC3  8 ASP A 416  NAG A 682  GLY B 278  ILE B 279
SITE     1 AC4  6 GLN A 400  GLN A 406  ASP A 416  NAG A 681
SITE     2 AC4  6 BMA A 683  GLN B 282
SITE     1 AC5  3 GLN A 400  NAG A 682  BMA A 684
SITE     1 AC6  2 HOH A 603  BMA A 683
SITE     1 AC7  5 GLU A 140  ASN A 144  TYR A 147  NDG A 672
SITE     2 AC7  5 LEU B 238
SITE     1 AC8  4 MET A 216  NAG A 671  BMA A 673  LEU B 238
SITE     1 AC9  3 HOH A 624  NDG A 672  MAN A 674
SITE     1 BC1  4 HOH A 624  BMA A 673  MAN A 675  GLN B 243
SITE     1 BC2  2 MAN A 674  GLN B 243
SITE     1 BC3  7 PRO A  84  PRO A  86  VAL A 119  ARG A 120
SITE     2 BC3  7 GLY A 471  GLU A 524  HOH A 621
SITE     1 BC4  3 LEU A  82  PRO A  84  SER A  85
SITE     1 BC5 13 ALA B 199  GLN B 203  HIS B 207  PHE B 210
SITE     2 BC5 13 THR B 212  LEU B 295  ASN B 382  TYR B 385
SITE     3 BC5 13 HIS B 386  TRP B 387  HIS B 388  MET B 391
SITE     4 BC5 13 VAL B 447
SITE     1 BC6  4 TYR B  55  ASN B  68  HOH B 621  NDG B1662
SITE     1 BC7  3 TYR B  38  ASP B 584  NAG B1661
SITE     1 BC8  8 TYR B 402  GLN B 406  ASN B 410  SER B 412
SITE     2 BC8  8 MET B 413  ASP B 416  TYR B 417  NAG B1682
SITE     1 BC9  3 ASP B 416  NAG B1681  BMA B1683
SITE     1 CC1  3 GLN B 400  NAG B1682  BMA B1684
SITE     1 CC2  2 GLN B 400  BMA B1683
SITE     1 CC3  4 LEU A 238  ASN B 144  TYR B 147  NDG B1672
SITE     1 CC4  5 LEU A 238  TYR A 242  MET B 216  NAG B1671
SITE     2 CC4  5 BMA B1673
SITE     1 CC5  2 NDG B1672  BMA B1674
SITE     1 CC6  2 HOH B 596  BMA B1673
SITE     1 CC7  5 VAL B 349  LEU B 352  TYR B 355  ALA B 527
SITE     2 CC7  5 OAS B 530
SITE     1 CC8 13 TYR B 348  VAL B 349  LEU B 352  SER B 353
SITE     2 CC8 13 TYR B 355  TYR B 385  TRP B 387  MET B 522
SITE     3 CC8 13 ILE B 523  GLY B 526  ALA B 527  OAS B 530
SITE     4 CC8 13 LEU B 531
SITE     1 CC9  5 ARG B  83  PRO B  84  SER B  85  SER B  87
SITE     2 CC9  5 PHE B  88
SITE     1 DC1  8 HOH B  12  ARG B  83  PRO B  86  ILE B  89
SITE     2 DC1  8 VAL B 119  ARG B 120  LEU B 123  GLU B 524
CRYST1  182.327  182.327  103.106  90.00  90.00 120.00 P 65          6
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      0.005485  0.003167  0.000000        0.00000
SCALE2      0.000000  0.006333  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009699        0.00000
      
PROCHECK
Go to PROCHECK summary
 References