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PDBsum entry 3nxq

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Hydrolase/hydrolase inhibitor PDB id
3nxq
Jmol
Contents
Protein chain
607 a.a.
Ligands
RX4 ×2
NAG-FUC ×2
NAG-NAG ×2
NAG-NAG-BMA-FUC ×2
P6G ×2
PEG ×2
PG4 ×2
Metals
_ZN ×2
_CL ×2
Waters ×563
HEADER    HYDROLASE/HYDROLASE INHIBITOR           14-JUL-10   3NXQ
TITLE     ANGIOTENSIN CONVERTING ENZYME N DOMAIN GLYCSOYLATION MUTANT (NDOM389)
TITLE    2 IN COMPLEX WITH RXP407
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ANGIOTENSIN-CONVERTING ENZYME;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: N DOMAIN (UNP RESIDUES 30-657);
COMPND   5 SYNONYM: ACE, DIPEPTIDYL CARBOXYPEPTIDASE I, KININASE II,
COMPND   6 ANGIOTENSIN-CONVERTING ENZYME, SOLUBLE FORM;
COMPND   7 EC: 3.4.15.1, 3.2.1.-;
COMPND   8 ENGINEERED: YES;
COMPND   9 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: ACE, DCP, DCP1;
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: OVARY CELLS
KEYWDS    DICARBOXY ZINC METALLOPEPTIDASE, HYDROLASE, HYDROLASE-HYDROLASE
KEYWDS   2 INHIBITOR COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    C.S.ANTHONY,H.R.CORRADI,S.L.U.SCHWAGER,P.REDELINGHUYS,D.GEORGIADIS,
AUTHOR   2 V.DIVE,K.R.ACHARYA,E.D.STURROCK
REVDAT   3   19-JAN-11 3NXQ    1       JRNL
REVDAT   2   22-SEP-10 3NXQ    1       AUTHOR
REVDAT   1   08-SEP-10 3NXQ    0
JRNL        AUTH   C.S.ANTHONY,H.R.CORRADI,S.L.SCHWAGER,P.REDELINGHUYS,
JRNL        AUTH 2 D.GEORGIADIS,V.DIVE,K.R.ACHARYA,E.D.STURROCK
JRNL        TITL   THE N DOMAIN OF HUMAN ANGIOTENSIN-I-CONVERTING ENZYME: THE
JRNL        TITL 2 ROLE OF N-GLYCOSYLATION AND THE CRYSTAL STRUCTURE IN COMPLEX
JRNL        TITL 3 WITH AN N DOMAIN-SPECIFIC PHOSPHINIC INHIBITOR, RXP407.
JRNL        REF    J.BIOL.CHEM.                  V. 285 35685 2010
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   20826823
JRNL        DOI    10.1074/JBC.M110.167866
REMARK   2
REMARK   2 RESOLUTION.    1.99 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) : 1.99
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.81
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.6
REMARK   3   NUMBER OF REFLECTIONS             : 100680
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) : 0.194
REMARK   3   R VALUE            (WORKING SET) : 0.194
REMARK   3   FREE R VALUE                     : 0.237
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1025
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) : 1.99
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.04
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 7149
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.02
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2610
REMARK   3   BIN FREE R VALUE SET COUNT          : 78
REMARK   3   BIN FREE R VALUE                    : 0.2840
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 9844
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 343
REMARK   3   SOLVENT ATOMS            : 563
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.81
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -1.65000
REMARK   3    B22 (A**2) : -0.28000
REMARK   3    B33 (A**2) : 0.26000
REMARK   3    B12 (A**2) : 1.20000
REMARK   3    B13 (A**2) : 1.24000
REMARK   3    B23 (A**2) : 0.14000
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): 0.158
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.114
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.486
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.954
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): 10567 ; 0.007 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 14420 ; 1.064 ; 1.967
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1232 ; 4.880 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   520 ;36.232 ;23.673
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1571 ;13.910 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    65 ;17.309 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1525 ; 0.079 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  8221 ; 0.004 ; 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):  6128 ; 0.396 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9854 ; 0.784 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4439 ; 1.250 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4557 ; 2.166 ; 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 : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 10
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    98
REMARK   3    ORIGIN FOR THE GROUP (A): -23.8762 -22.7001 -18.2247
REMARK   3    T TENSOR
REMARK   3      T11:   0.0639 T22:   0.1159
REMARK   3      T33:   0.1778 T12:   0.0108
REMARK   3      T13:  -0.0849 T23:  -0.0143
REMARK   3    L TENSOR
REMARK   3      L11:   0.9422 L22:   1.0142
REMARK   3      L33:   1.8995 L12:   0.5369
REMARK   3      L13:  -1.2192 L23:  -1.0423
REMARK   3    S TENSOR
REMARK   3      S11:   0.0929 S12:   0.0587 S13:  -0.1418
REMARK   3      S21:  -0.0010 S22:  -0.0855 S23:   0.0996
REMARK   3      S31:  -0.0768 S32:  -0.0523 S33:  -0.0074
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    99        A   278
REMARK   3    ORIGIN FOR THE GROUP (A):   3.9193  -5.4908 -17.6816
REMARK   3    T TENSOR
REMARK   3      T11:   0.1357 T22:   0.1023
REMARK   3      T33:   0.0751 T12:   0.0124
REMARK   3      T13:   0.0036 T23:   0.0021
REMARK   3    L TENSOR
REMARK   3      L11:   1.0476 L22:   0.5714
REMARK   3      L33:   0.1445 L12:  -0.1129
REMARK   3      L13:   0.0972 L23:   0.0908
REMARK   3    S TENSOR
REMARK   3      S11:   0.0480 S12:  -0.0034 S13:   0.0441
REMARK   3      S21:  -0.0754 S22:  -0.0018 S23:  -0.0400
REMARK   3      S31:  -0.0471 S32:  -0.0098 S33:  -0.0462
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   279        A   416
REMARK   3    ORIGIN FOR THE GROUP (A):   3.7101 -25.4366 -28.4258
REMARK   3    T TENSOR
REMARK   3      T11:   0.1105 T22:   0.1321
REMARK   3      T33:   0.0857 T12:   0.0069
REMARK   3      T13:  -0.0108 T23:  -0.0098
REMARK   3    L TENSOR
REMARK   3      L11:   1.1513 L22:   0.6513
REMARK   3      L33:   0.5264 L12:  -0.2220
REMARK   3      L13:  -0.2426 L23:   0.0831
REMARK   3    S TENSOR
REMARK   3      S11:   0.0533 S12:   0.0342 S13:  -0.0370
REMARK   3      S21:  -0.0928 S22:  -0.0645 S23:  -0.0202
REMARK   3      S31:  -0.0580 S32:  -0.0525 S33:   0.0112
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   417        A   558
REMARK   3    ORIGIN FOR THE GROUP (A):   5.2331 -16.2348 -12.9080
REMARK   3    T TENSOR
REMARK   3      T11:   0.1199 T22:   0.1368
REMARK   3      T33:   0.1019 T12:   0.0025
REMARK   3      T13:  -0.0083 T23:  -0.0022
REMARK   3    L TENSOR
REMARK   3      L11:   0.2510 L22:   0.5802
REMARK   3      L33:   0.1507 L12:  -0.1094
REMARK   3      L13:  -0.0098 L23:   0.1124
REMARK   3    S TENSOR
REMARK   3      S11:   0.0096 S12:  -0.0714 S13:  -0.0257
REMARK   3      S21:   0.0160 S22:  -0.0042 S23:  -0.0267
REMARK   3      S31:  -0.0289 S32:  -0.0237 S33:  -0.0054
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   559        A   610
REMARK   3    ORIGIN FOR THE GROUP (A):  18.1312  -8.5210  -9.0726
REMARK   3    T TENSOR
REMARK   3      T11:   0.0881 T22:   0.1283
REMARK   3      T33:   0.0679 T12:  -0.0091
REMARK   3      T13:  -0.0151 T23:  -0.0287
REMARK   3    L TENSOR
REMARK   3      L11:   1.0061 L22:   1.0611
REMARK   3      L33:   0.5238 L12:   0.2374
REMARK   3      L13:  -0.2243 L23:   0.1573
REMARK   3    S TENSOR
REMARK   3      S11:   0.0357 S12:  -0.0856 S13:  -0.0033
REMARK   3      S21:   0.0485 S22:   0.0557 S23:  -0.2152
REMARK   3      S31:  -0.0373 S32:  -0.0036 S33:  -0.0914
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     1        B    96
REMARK   3    ORIGIN FOR THE GROUP (A):   0.6933  -3.9492  37.2204
REMARK   3    T TENSOR
REMARK   3      T11:   0.1762 T22:   0.1213
REMARK   3      T33:   0.0500 T12:   0.0190
REMARK   3      T13:  -0.0072 T23:   0.0179
REMARK   3    L TENSOR
REMARK   3      L11:   2.5858 L22:   3.3757
REMARK   3      L33:   0.7797 L12:   2.1880
REMARK   3      L13:  -1.3149 L23:  -1.3875
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1823 S12:   0.0333 S13:  -0.0383
REMARK   3      S21:   0.0870 S22:   0.1625 S23:  -0.0243
REMARK   3      S31:   0.1283 S32:  -0.0042 S33:   0.0198
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    97        B   275
REMARK   3    ORIGIN FOR THE GROUP (A):   4.5573  14.5241  10.5627
REMARK   3    T TENSOR
REMARK   3      T11:   0.1082 T22:   0.0835
REMARK   3      T33:   0.0945 T12:  -0.0126
REMARK   3      T13:  -0.0042 T23:  -0.0171
REMARK   3    L TENSOR
REMARK   3      L11:   0.2381 L22:   0.7519
REMARK   3      L33:   0.9676 L12:  -0.3110
REMARK   3      L13:  -0.0045 L23:   0.0281
REMARK   3    S TENSOR
REMARK   3      S11:   0.0368 S12:  -0.0017 S13:  -0.0191
REMARK   3      S21:  -0.0860 S22:  -0.0179 S23:  -0.0420
REMARK   3      S31:  -0.0445 S32:   0.0575 S33:  -0.0189
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   276        B   406
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.6538  22.6922  29.5599
REMARK   3    T TENSOR
REMARK   3      T11:   0.1167 T22:   0.1199
REMARK   3      T33:   0.0880 T12:  -0.0080
REMARK   3      T13:   0.0093 T23:  -0.0033
REMARK   3    L TENSOR
REMARK   3      L11:   0.7843 L22:   1.1720
REMARK   3      L33:   0.6885 L12:  -0.4748
REMARK   3      L13:  -0.1072 L23:   0.1574
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0125 S12:  -0.0770 S13:  -0.0262
REMARK   3      S21:   0.0262 S22:   0.0061 S23:  -0.0488
REMARK   3      S31:  -0.0690 S32:  -0.0622 S33:   0.0064
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   407        B   558
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.7111  15.4441  14.0803
REMARK   3    T TENSOR
REMARK   3      T11:   0.1127 T22:   0.1200
REMARK   3      T33:   0.1160 T12:  -0.0087
REMARK   3      T13:  -0.0158 T23:  -0.0142
REMARK   3    L TENSOR
REMARK   3      L11:   0.3791 L22:   0.3282
REMARK   3      L33:   0.8134 L12:  -0.2775
REMARK   3      L13:  -0.2285 L23:   0.3944
REMARK   3    S TENSOR
REMARK   3      S11:   0.0496 S12:   0.0076 S13:  -0.0818
REMARK   3      S21:  -0.0843 S22:  -0.0564 S23:   0.0495
REMARK   3      S31:  -0.0021 S32:  -0.1245 S33:   0.0068
REMARK   3
REMARK   3   TLS GROUP : 10
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B   559        B   610
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.0622  20.3679   0.1290
REMARK   3    T TENSOR
REMARK   3      T11:   0.1311 T22:   0.0702
REMARK   3      T33:   0.0364 T12:   0.0152
REMARK   3      T13:  -0.0427 T23:  -0.0229
REMARK   3    L TENSOR
REMARK   3      L11:   0.8157 L22:   1.0139
REMARK   3      L33:   1.7705 L12:   0.1257
REMARK   3      L13:  -0.4652 L23:  -0.1297
REMARK   3    S TENSOR
REMARK   3      S11:   0.0417 S12:   0.0745 S13:  -0.0872
REMARK   3      S21:  -0.2137 S22:  -0.1023 S23:   0.1019
REMARK   3      S31:  -0.2122 S32:  -0.2104 S33:   0.0605
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 3NXQ COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUL-10.
REMARK 100 THE RCSB ID CODE IS RCSB060410.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 08-FEB-10
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 8.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : DIAMOND
REMARK 200  BEAMLINE                       : I02
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 106279
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.990
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.05400
REMARK 200   FOR THE DATA SET  : 12.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
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         : 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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 55.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 150NL CONDITION MORPHEUS A9 (0.06M
REMARK 280  DIVALENTS, 0.1M TRIS/BICINE PH 8.5, 30% PEG550MME/PEG20K) AND
REMARK 280  150NL ADDITIVE G10 (0.2% W/V 1,4-CYCLOHEXANEDICARBOXYLIC ACID,
REMARK 280  0.2% W/V 2,5-PYRIDINEDICARBOXYLIC ACID, 0.2% W/V GLUTARIC ACID,
REMARK 280  0.2% W/V TRANS-1,2-CYCLOHEXANEDICARBOXYLIC ACID, 0.2% W/V TRANS-
REMARK 280  ACONITIC ACID, 0.02 M HEPES SODIUM PH 6.8) , VAPOR DIFFUSION,
REMARK 280  SITTING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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     PRO A   130
REMARK 465     GLN A   131
REMARK 465     LYS A   132
REMARK 465     ILE A   611
REMARK 465     ASP A   612
REMARK 465     LEU A   613
REMARK 465     VAL A   614
REMARK 465     THR A   615
REMARK 465     ASP A   616
REMARK 465     GLU A   617
REMARK 465     ALA A   618
REMARK 465     GLU A   619
REMARK 465     ALA A   620
REMARK 465     SER A   621
REMARK 465     LYS A   622
REMARK 465     PHE A   623
REMARK 465     VAL A   624
REMARK 465     GLU A   625
REMARK 465     GLU A   626
REMARK 465     TYR A   627
REMARK 465     ASP A   628
REMARK 465     LEU A   629
REMARK 465     ILE B   611
REMARK 465     ASP B   612
REMARK 465     LEU B   613
REMARK 465     VAL B   614
REMARK 465     THR B   615
REMARK 465     ASP B   616
REMARK 465     GLU B   617
REMARK 465     ALA B   618
REMARK 465     GLU B   619
REMARK 465     ALA B   620
REMARK 465     SER B   621
REMARK 465     LYS B   622
REMARK 465     PHE B   623
REMARK 465     VAL B   624
REMARK 465     GLU B   625
REMARK 465     GLU B   626
REMARK 465     TYR B   627
REMARK 465     ASP B   628
REMARK 465     LEU B   629
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     GLU A  56    CD   OE1  OE2
REMARK 470     GLN A  70    CD   OE1  NE2
REMARK 470     LEU A 129    CG   CD1  CD2
REMARK 470     THR A 133    OG1  CG2
REMARK 470     THR A 135    OG1  CG2
REMARK 470     ASP A 273    CG   OD1  OD2
REMARK 470     LYS A 341    CD   CE   NZ
REMARK 470     GLU A 403    CD   OE1  OE2
REMARK 470     ARG A 413    CG   CD   NE   CZ   NH1  NH2
REMARK 470     THR A 415    OG1  CG2
REMARK 470     LYS A 517    CE   NZ
REMARK 470     LYS A 542    CE   NZ
REMARK 470     GLU B  56    CD   OE1  OE2
REMARK 470     GLN B  70    OE1  NE2
REMARK 470     LYS B  71    CG   CD   CE   NZ
REMARK 470     GLN B 131    CG   CD   OE1  NE2
REMARK 470     LYS B 132    CG   CD   CE   NZ
REMARK 470     THR B 135    OG1  CG2
REMARK 470     LYS B 187    CE   NZ
REMARK 470     GLU B 212    CD   OE1  OE2
REMARK 470     LYS B 274    CE   NZ
REMARK 470     LYS B 341    CE   NZ
REMARK 470     GLU B 403    CG   CD   OE1  OE2
REMARK 470     ARG B 413    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS B 517    CE   NZ
REMARK 470     GLU B 522    CG   CD   OE1  OE2
REMARK 470     LYS B 542    CE   NZ
REMARK 470     GLU B 554    CD   OE1  OE2
REMARK 470     LYS B 572    CE   NZ
REMARK 470     ASP B 605    CG   OD1  OD2
REMARK 470     ASN B 606    CG   OD1
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    ASN A  45       77.57   -170.93
REMARK 500    ASN A 203       55.23     33.67
REMARK 500    ASP A 324     -167.65    -74.92
REMARK 500    ARG A 413      123.50    -34.95
REMARK 500    ASN B  45       77.69   -173.67
REMARK 500    THR B 133       49.83    -77.05
REMARK 500    THR B 135       76.74     49.29
REMARK 500    LYS B 341      -45.46   -130.75
REMARK 500    ASN B 606       56.90   -116.66
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610   M RES C SSEQI
REMARK 610     P6G A  708
REMARK 610     PG4 B  704
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                              ZN A 650  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 361   NE2
REMARK 620 2 HIS A 365   NE2 107.5
REMARK 620 3 GLU A 389   OE1  95.8 104.5
REMARK 620 4 RX4 A 700   O3  108.8 138.8  90.6
REMARK 620 5 RX4 A 700   O4   95.3  91.2 157.2  66.9
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN B 650  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 389   OE1
REMARK 620 2 HIS B 365   NE2 102.1
REMARK 620 3 HIS B 361   NE2  94.3 107.7
REMARK 620 4 RX4 B 700   O3   91.4 137.2 111.6
REMARK 620 5 RX4 B 700   O4  160.2  89.5  97.4  69.4
REMARK 620 N                    1     2     3     4
REMARK 630
REMARK 630 MOLECULE TYPE: NULL
REMARK 630 MOLECULE NAME: N~2~-ACETYL-N-{(1R)-1-[(S)-[(2S)-3-{[(2S)-1-AMINO-
REMARK 630 1-OXOPROPAN-2-YL]AMINO}-2-METHYL-3-OXOPROPYL](HYDROXY)PHOSPHORYL]-
REMARK 630 2-PHENYLETHYL}-L-ALPHA-ASPARAGINE
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 630  SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 630
REMARK 630   M RES C SSSEQI
REMARK 630     RX4 A   700
REMARK 630     RX4 B   700
REMARK 630 SOURCE: NULL
REMARK 630 SUBCOMP:    ACE ASP RT1 ALA NH2
REMARK 630 STRUCTURE DETAILS: NULL
REMARK 630 OTHER DETAILS: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 650
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RX4 A 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 630
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC A 631
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 632
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 633
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 634
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 635
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 636
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC A 637
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P6G A 708
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 706
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 650
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RX4 B 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 630
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC B 631
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 632
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 633
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 634
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 635
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA B 636
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC B 637
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P6G B 709
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 710
DBREF  3NXQ A    1   629  UNP    P12821   ACE_HUMAN       30    658
DBREF  3NXQ B    1   629  UNP    P12821   ACE_HUMAN       30    658
SEQADV 3NXQ GLN A    9  UNP  P12821    ASN    38 ENGINEERED MUTATION
SEQADV 3NXQ GLN A   25  UNP  P12821    ASN    54 ENGINEERED MUTATION
SEQADV 3NXQ GLN A   82  UNP  P12821    ASN   111 ENGINEERED MUTATION
SEQADV 3NXQ GLN A  117  UNP  P12821    ASN   146 ENGINEERED MUTATION
SEQADV 3NXQ GLN A  131  UNP  P12821    ASN   160 ENGINEERED MUTATION
SEQADV 3NXQ GLN A  289  UNP  P12821    ASN   318 ENGINEERED MUTATION
SEQADV 3NXQ ARG A  545  UNP  P12821    GLN   574 ENGINEERED MUTATION
SEQADV 3NXQ LEU A  576  UNP  P12821    PRO   605 ENGINEERED MUTATION
SEQADV 3NXQ LEU A  629  UNP  P12821    ARG   658 ENGINEERED MUTATION
SEQADV 3NXQ GLN B    9  UNP  P12821    ASN    38 ENGINEERED MUTATION
SEQADV 3NXQ GLN B   25  UNP  P12821    ASN    54 ENGINEERED MUTATION
SEQADV 3NXQ GLN B   82  UNP  P12821    ASN   111 ENGINEERED MUTATION
SEQADV 3NXQ GLN B  117  UNP  P12821    ASN   146 ENGINEERED MUTATION
SEQADV 3NXQ GLN B  131  UNP  P12821    ASN   160 ENGINEERED MUTATION
SEQADV 3NXQ GLN B  289  UNP  P12821    ASN   318 ENGINEERED MUTATION
SEQADV 3NXQ ARG B  545  UNP  P12821    GLN   574 ENGINEERED MUTATION
SEQADV 3NXQ LEU B  576  UNP  P12821    PRO   605 ENGINEERED MUTATION
SEQADV 3NXQ LEU B  629  UNP  P12821    ARG   658 ENGINEERED MUTATION
SEQRES   1 A  629  LEU ASP PRO GLY LEU GLN PRO GLY GLN PHE SER ALA ASP
SEQRES   2 A  629  GLU ALA GLY ALA GLN LEU PHE ALA GLN SER TYR GLN SER
SEQRES   3 A  629  SER ALA GLU GLN VAL LEU PHE GLN SER VAL ALA ALA SER
SEQRES   4 A  629  TRP ALA HIS ASP THR ASN ILE THR ALA GLU ASN ALA ARG
SEQRES   5 A  629  ARG GLN GLU GLU ALA ALA LEU LEU SER GLN GLU PHE ALA
SEQRES   6 A  629  GLU ALA TRP GLY GLN LYS ALA LYS GLU LEU TYR GLU PRO
SEQRES   7 A  629  ILE TRP GLN GLN PHE THR ASP PRO GLN LEU ARG ARG ILE
SEQRES   8 A  629  ILE GLY ALA VAL ARG THR LEU GLY SER ALA ASN LEU PRO
SEQRES   9 A  629  LEU ALA LYS ARG GLN GLN TYR ASN ALA LEU LEU SER GLN
SEQRES  10 A  629  MET SER ARG ILE TYR SER THR ALA LYS VAL CYS LEU PRO
SEQRES  11 A  629  GLN LYS THR ALA THR CYS TRP SER LEU ASP PRO ASP LEU
SEQRES  12 A  629  THR ASN ILE LEU ALA SER SER ARG SER TYR ALA MET LEU
SEQRES  13 A  629  LEU PHE ALA TRP GLU GLY TRP HIS ASN ALA ALA GLY ILE
SEQRES  14 A  629  PRO LEU LYS PRO LEU TYR GLU ASP PHE THR ALA LEU SER
SEQRES  15 A  629  ASN GLU ALA TYR LYS GLN ASP GLY PHE THR ASP THR GLY
SEQRES  16 A  629  ALA TYR TRP ARG SER TRP TYR ASN SER PRO THR PHE GLU
SEQRES  17 A  629  ASP ASP LEU GLU HIS LEU TYR GLN GLN LEU GLU PRO LEU
SEQRES  18 A  629  TYR LEU ASN LEU HIS ALA PHE VAL ARG ARG ALA LEU HIS
SEQRES  19 A  629  ARG ARG TYR GLY ASP ARG TYR ILE ASN LEU ARG GLY PRO
SEQRES  20 A  629  ILE PRO ALA HIS LEU LEU GLY ASP MET TRP ALA GLN SER
SEQRES  21 A  629  TRP GLU ASN ILE TYR ASP MET VAL VAL PRO PHE PRO ASP
SEQRES  22 A  629  LYS PRO ASN LEU ASP VAL THR SER THR MET LEU GLN GLN
SEQRES  23 A  629  GLY TRP GLN ALA THR HIS MET PHE ARG VAL ALA GLU GLU
SEQRES  24 A  629  PHE PHE THR SER LEU GLU LEU SER PRO MET PRO PRO GLU
SEQRES  25 A  629  PHE TRP GLU GLY SER MET LEU GLU LYS PRO ALA ASP GLY
SEQRES  26 A  629  ARG GLU VAL VAL CYS HIS ALA SER ALA TRP ASP PHE TYR
SEQRES  27 A  629  ASN ARG LYS ASP PHE ARG ILE LYS GLN CYS THR ARG VAL
SEQRES  28 A  629  THR MET ASP GLN LEU SER THR VAL HIS HIS GLU MET GLY
SEQRES  29 A  629  HIS ILE GLN TYR TYR LEU GLN TYR LYS ASP LEU PRO VAL
SEQRES  30 A  629  SER LEU ARG ARG GLY ALA ASN PRO GLY PHE HIS GLU ALA
SEQRES  31 A  629  ILE GLY ASP VAL LEU ALA LEU SER VAL SER THR PRO GLU
SEQRES  32 A  629  HIS LEU HIS LYS ILE GLY LEU LEU ASP ARG VAL THR ASN
SEQRES  33 A  629  ASP THR GLU SER ASP ILE ASN TYR LEU LEU LYS MET ALA
SEQRES  34 A  629  LEU GLU LYS ILE ALA PHE LEU PRO PHE GLY TYR LEU VAL
SEQRES  35 A  629  ASP GLN TRP ARG TRP GLY VAL PHE SER GLY ARG THR PRO
SEQRES  36 A  629  PRO SER ARG TYR ASN PHE ASP TRP TRP TYR LEU ARG THR
SEQRES  37 A  629  LYS TYR GLN GLY ILE CYS PRO PRO VAL THR ARG ASN GLU
SEQRES  38 A  629  THR HIS PHE ASP ALA GLY ALA LYS PHE HIS VAL PRO ASN
SEQRES  39 A  629  VAL THR PRO TYR ILE ARG TYR PHE VAL SER PHE VAL LEU
SEQRES  40 A  629  GLN PHE GLN PHE HIS GLU ALA LEU CYS LYS GLU ALA GLY
SEQRES  41 A  629  TYR GLU GLY PRO LEU HIS GLN CYS ASP ILE TYR ARG SER
SEQRES  42 A  629  THR LYS ALA GLY ALA LYS LEU ARG LYS VAL LEU ARG ALA
SEQRES  43 A  629  GLY SER SER ARG PRO TRP GLN GLU VAL LEU LYS ASP MET
SEQRES  44 A  629  VAL GLY LEU ASP ALA LEU ASP ALA GLN PRO LEU LEU LYS
SEQRES  45 A  629  TYR PHE GLN LEU VAL THR GLN TRP LEU GLN GLU GLN ASN
SEQRES  46 A  629  GLN GLN ASN GLY GLU VAL LEU GLY TRP PRO GLU TYR GLN
SEQRES  47 A  629  TRP HIS PRO PRO LEU PRO ASP ASN TYR PRO GLU GLY ILE
SEQRES  48 A  629  ASP LEU VAL THR ASP GLU ALA GLU ALA SER LYS PHE VAL
SEQRES  49 A  629  GLU GLU TYR ASP LEU
SEQRES   1 B  629  LEU ASP PRO GLY LEU GLN PRO GLY GLN PHE SER ALA ASP
SEQRES   2 B  629  GLU ALA GLY ALA GLN LEU PHE ALA GLN SER TYR GLN SER
SEQRES   3 B  629  SER ALA GLU GLN VAL LEU PHE GLN SER VAL ALA ALA SER
SEQRES   4 B  629  TRP ALA HIS ASP THR ASN ILE THR ALA GLU ASN ALA ARG
SEQRES   5 B  629  ARG GLN GLU GLU ALA ALA LEU LEU SER GLN GLU PHE ALA
SEQRES   6 B  629  GLU ALA TRP GLY GLN LYS ALA LYS GLU LEU TYR GLU PRO
SEQRES   7 B  629  ILE TRP GLN GLN PHE THR ASP PRO GLN LEU ARG ARG ILE
SEQRES   8 B  629  ILE GLY ALA VAL ARG THR LEU GLY SER ALA ASN LEU PRO
SEQRES   9 B  629  LEU ALA LYS ARG GLN GLN TYR ASN ALA LEU LEU SER GLN
SEQRES  10 B  629  MET SER ARG ILE TYR SER THR ALA LYS VAL CYS LEU PRO
SEQRES  11 B  629  GLN LYS THR ALA THR CYS TRP SER LEU ASP PRO ASP LEU
SEQRES  12 B  629  THR ASN ILE LEU ALA SER SER ARG SER TYR ALA MET LEU
SEQRES  13 B  629  LEU PHE ALA TRP GLU GLY TRP HIS ASN ALA ALA GLY ILE
SEQRES  14 B  629  PRO LEU LYS PRO LEU TYR GLU ASP PHE THR ALA LEU SER
SEQRES  15 B  629  ASN GLU ALA TYR LYS GLN ASP GLY PHE THR ASP THR GLY
SEQRES  16 B  629  ALA TYR TRP ARG SER TRP TYR ASN SER PRO THR PHE GLU
SEQRES  17 B  629  ASP ASP LEU GLU HIS LEU TYR GLN GLN LEU GLU PRO LEU
SEQRES  18 B  629  TYR LEU ASN LEU HIS ALA PHE VAL ARG ARG ALA LEU HIS
SEQRES  19 B  629  ARG ARG TYR GLY ASP ARG TYR ILE ASN LEU ARG GLY PRO
SEQRES  20 B  629  ILE PRO ALA HIS LEU LEU GLY ASP MET TRP ALA GLN SER
SEQRES  21 B  629  TRP GLU ASN ILE TYR ASP MET VAL VAL PRO PHE PRO ASP
SEQRES  22 B  629  LYS PRO ASN LEU ASP VAL THR SER THR MET LEU GLN GLN
SEQRES  23 B  629  GLY TRP GLN ALA THR HIS MET PHE ARG VAL ALA GLU GLU
SEQRES  24 B  629  PHE PHE THR SER LEU GLU LEU SER PRO MET PRO PRO GLU
SEQRES  25 B  629  PHE TRP GLU GLY SER MET LEU GLU LYS PRO ALA ASP GLY
SEQRES  26 B  629  ARG GLU VAL VAL CYS HIS ALA SER ALA TRP ASP PHE TYR
SEQRES  27 B  629  ASN ARG LYS ASP PHE ARG ILE LYS GLN CYS THR ARG VAL
SEQRES  28 B  629  THR MET ASP GLN LEU SER THR VAL HIS HIS GLU MET GLY
SEQRES  29 B  629  HIS ILE GLN TYR TYR LEU GLN TYR LYS ASP LEU PRO VAL
SEQRES  30 B  629  SER LEU ARG ARG GLY ALA ASN PRO GLY PHE HIS GLU ALA
SEQRES  31 B  629  ILE GLY ASP VAL LEU ALA LEU SER VAL SER THR PRO GLU
SEQRES  32 B  629  HIS LEU HIS LYS ILE GLY LEU LEU ASP ARG VAL THR ASN
SEQRES  33 B  629  ASP THR GLU SER ASP ILE ASN TYR LEU LEU LYS MET ALA
SEQRES  34 B  629  LEU GLU LYS ILE ALA PHE LEU PRO PHE GLY TYR LEU VAL
SEQRES  35 B  629  ASP GLN TRP ARG TRP GLY VAL PHE SER GLY ARG THR PRO
SEQRES  36 B  629  PRO SER ARG TYR ASN PHE ASP TRP TRP TYR LEU ARG THR
SEQRES  37 B  629  LYS TYR GLN GLY ILE CYS PRO PRO VAL THR ARG ASN GLU
SEQRES  38 B  629  THR HIS PHE ASP ALA GLY ALA LYS PHE HIS VAL PRO ASN
SEQRES  39 B  629  VAL THR PRO TYR ILE ARG TYR PHE VAL SER PHE VAL LEU
SEQRES  40 B  629  GLN PHE GLN PHE HIS GLU ALA LEU CYS LYS GLU ALA GLY
SEQRES  41 B  629  TYR GLU GLY PRO LEU HIS GLN CYS ASP ILE TYR ARG SER
SEQRES  42 B  629  THR LYS ALA GLY ALA LYS LEU ARG LYS VAL LEU ARG ALA
SEQRES  43 B  629  GLY SER SER ARG PRO TRP GLN GLU VAL LEU LYS ASP MET
SEQRES  44 B  629  VAL GLY LEU ASP ALA LEU ASP ALA GLN PRO LEU LEU LYS
SEQRES  45 B  629  TYR PHE GLN LEU VAL THR GLN TRP LEU GLN GLU GLN ASN
SEQRES  46 B  629  GLN GLN ASN GLY GLU VAL LEU GLY TRP PRO GLU TYR GLN
SEQRES  47 B  629  TRP HIS PRO PRO LEU PRO ASP ASN TYR PRO GLU GLY ILE
SEQRES  48 B  629  ASP LEU VAL THR ASP GLU ALA GLU ALA SER LYS PHE VAL
SEQRES  49 B  629  GLU GLU TYR ASP LEU
MODRES 3NXQ ASN A  416  ASN  GLYCOSYLATION SITE
MODRES 3NXQ ASN B   45  ASN  GLYCOSYLATION SITE
MODRES 3NXQ ASN B  416  ASN  GLYCOSYLATION SITE
MODRES 3NXQ ASN A   45  ASN  GLYCOSYLATION SITE
MODRES 3NXQ ASN A  480  ASN  GLYCOSYLATION SITE
MODRES 3NXQ ASN B  480  ASN  GLYCOSYLATION SITE
HET     ZN  A 650       1
HET    RX4  A 700      34
HET    NAG  A 630      14
HET    FUC  A 631      10
HET    NAG  A 632      14
HET    NAG  A 633      14
HET    NAG  A 634      14
HET    NAG  A 635      14
HET    BMA  A 636      11
HET    FUC  A 637      10
HET    P6G  A 708      13
HET     CL  A 900       1
HET    PEG  A 706       7
HET     CL  B 900       1
HET     ZN  B 650       1
HET    RX4  B 700      34
HET    NAG  B 630      14
HET    FUC  B 631      10
HET    NAG  B 632      14
HET    NAG  B 633      14
HET    NAG  B 634      14
HET    NAG  B 635      14
HET    BMA  B 636      11
HET    FUC  B 637      10
HET    PG4  B 704      10
HET    PG4  B 705      13
HET    P6G  B 709      19
HET    PEG  B 710       7
HETNAM      ZN ZINC ION
HETNAM     RX4 N~2~-ACETYL-N-{(1R)-1-[(S)-[(2S)-3-{[(2S)-1-AMINO-1-
HETNAM   2 RX4  OXOPROPAN-2-YL]AMINO}-2-METHYL-3-OXOPROPYL](HYDROXY)
HETNAM   3 RX4  PHOSPHORYL]-2-PHENYLETHYL}-L-ALPHA-ASPARAGINE
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     FUC ALPHA-L-FUCOSE
HETNAM     BMA BETA-D-MANNOSE
HETNAM     P6G HEXAETHYLENE GLYCOL
HETNAM      CL CHLORIDE ION
HETNAM     PEG DI(HYDROXYETHYL)ETHER
HETNAM     PG4 TETRAETHYLENE GLYCOL
HETSYN     RX4 AC-ASP-(L)PHE(PO2CH2)(L)ALA-ALA-NH2, RXP407
HETSYN     P6G POLYETHYLENE GLYCOL PEG400
FORMUL   3   ZN    2(ZN 2+)
FORMUL   4  RX4    2(C21 H31 N4 O8 P)
FORMUL   5  NAG    10(C8 H15 N O6)
FORMUL   5  FUC    4(C6 H12 O5)
FORMUL   7  BMA    2(C6 H12 O6)
FORMUL   8  P6G    2(C12 H26 O7)
FORMUL   9   CL    2(CL 1-)
FORMUL  10  PEG    2(C4 H10 O3)
FORMUL  17  PG4    2(C8 H18 O5)
FORMUL  21  HOH   *563(H2 O)
HELIX    1   1 ASP A    2  GLN A    6  5                                   5
HELIX    2   2 ASP A   13  THR A   44  1                                  32
HELIX    3   3 THR A   47  GLU A   77  1                                  31
HELIX    4   4 ILE A   79  PHE A   83  5                                   5
HELIX    5   5 ASP A   85  ARG A   96  1                                  12
HELIX    6   6 LEU A   98  LEU A  103  5                                   6
HELIX    7   7 PRO A  104  ALA A  125  1                                  22
HELIX    8   8 PRO A  141  SER A  150  1                                  10
HELIX    9   9 SER A  152  GLN A  188  1                                  37
HELIX   10  10 ASP A  193  TRP A  201  1                                   9
HELIX   11  11 THR A  206  GLY A  238  1                                  33
HELIX   12  12 TRP A  261  ASN A  263  5                                   3
HELIX   13  13 ILE A  264  VAL A  269  1                                   6
HELIX   14  14 VAL A  279  GLY A  287  1                                   9
HELIX   15  15 GLN A  289  LEU A  304  1                                  16
HELIX   16  16 PRO A  310  SER A  317  1                                   8
HELIX   17  17 THR A  352  TYR A  372  1                                  21
HELIX   18  18 PRO A  376  ARG A  380  5                                   5
HELIX   19  19 ASN A  384  SER A  400  1                                  17
HELIX   20  20 THR A  401  ILE A  408  1                                   8
HELIX   21  21 ASP A  417  ILE A  433  1                                  17
HELIX   22  22 PHE A  435  SER A  451  1                                  17
HELIX   23  23 PRO A  455  SER A  457  5                                   3
HELIX   24  24 ARG A  458  GLY A  472  1                                  15
HELIX   25  25 PHE A  484  LYS A  489  5                                   6
HELIX   26  26 TYR A  498  ALA A  519  1                                  22
HELIX   27  27 PRO A  524  CYS A  528  5                                   5
HELIX   28  28 SER A  533  GLY A  547  1                                  15
HELIX   29  29 PRO A  551  GLY A  561  1                                  11
HELIX   30  30 ALA A  567  GLY A  589  1                                  23
HELIX   31  31 ASP B    2  GLN B    6  5                                   5
HELIX   32  32 ASP B   13  THR B   44  1                                  32
HELIX   33  33 THR B   47  GLU B   77  1                                  31
HELIX   34  34 ILE B   79  PHE B   83  5                                   5
HELIX   35  35 ASP B   85  ARG B   96  1                                  12
HELIX   36  36 LEU B   98  LEU B  103  5                                   6
HELIX   37  37 PRO B  104  ALA B  125  1                                  22
HELIX   38  38 PRO B  141  SER B  150  1                                  10
HELIX   39  39 SER B  152  GLN B  188  1                                  37
HELIX   40  40 ASP B  193  TRP B  201  1                                   9
HELIX   41  41 THR B  206  GLY B  238  1                                  33
HELIX   42  42 TRP B  261  ASN B  263  5                                   3
HELIX   43  43 ILE B  264  VAL B  269  1                                   6
HELIX   44  44 VAL B  279  GLY B  287  1                                   9
HELIX   45  45 GLN B  289  LEU B  304  1                                  16
HELIX   46  46 PRO B  310  SER B  317  1                                   8
HELIX   47  47 THR B  352  TYR B  372  1                                  21
HELIX   48  48 PRO B  376  ARG B  380  5                                   5
HELIX   49  49 ASN B  384  SER B  400  1                                  17
HELIX   50  50 THR B  401  ILE B  408  1                                   8
HELIX   51  51 ASP B  417  ILE B  433  1                                  17
HELIX   52  52 ALA B  434  SER B  451  1                                  18
HELIX   53  53 PRO B  455  SER B  457  5                                   3
HELIX   54  54 ARG B  458  GLY B  472  1                                  15
HELIX   55  55 PHE B  484  LYS B  489  5                                   6
HELIX   56  56 TYR B  498  ALA B  519  1                                  22
HELIX   57  57 PRO B  524  CYS B  528  5                                   5
HELIX   58  58 SER B  533  ALA B  546  1                                  14
HELIX   59  59 PRO B  551  GLY B  561  1                                  11
HELIX   60  60 ALA B  567  ASN B  588  1                                  22
SHEET    1   A 2 LYS A 126  CYS A 128  0
SHEET    2   A 2 CYS A 136  SER A 138 -1  O  TRP A 137   N  VAL A 127
SHEET    1   B 2 ILE A 248  PRO A 249  0
SHEET    2   B 2 ILE A 473  CYS A 474  1  O  CYS A 474   N  ILE A 248
SHEET    1   C 2 SER A 333  ASP A 336  0
SHEET    2   C 2 PHE A 343  LYS A 346 -1  O  ARG A 344   N  TRP A 335
SHEET    1   D 2 ILE B 248  PRO B 249  0
SHEET    2   D 2 ILE B 473  CYS B 474  1  O  CYS B 474   N  ILE B 248
SHEET    1   E 2 SER B 333  ASP B 336  0
SHEET    2   E 2 PHE B 343  LYS B 346 -1  O  ARG B 344   N  TRP B 335
SSBOND   1 CYS A  128    CYS A  136                          1555   1555  2.05
SSBOND   2 CYS A  330    CYS A  348                          1555   1555  2.07
SSBOND   3 CYS A  516    CYS A  528                          1555   1555  2.03
SSBOND   4 CYS B  128    CYS B  136                          1555   1555  2.04
SSBOND   5 CYS B  330    CYS B  348                          1555   1555  2.06
SSBOND   6 CYS B  516    CYS B  528                          1555   1555  2.02
LINK         ND2 ASN A 416                 C1  NAG A 634     1555   1555  1.43
LINK         ND2 ASN B  45                 C1  NAG B 632     1555   1555  1.44
LINK         ND2 ASN B 416                 C1  NAG B 634     1555   1555  1.44
LINK         O6  NAG A 634                 C1  FUC A 637     1555   1555  1.44
LINK         ND2 ASN A  45                 C1  NAG A 632     1555   1555  1.44
LINK         O4  NAG B 632                 C1  NAG B 633     1555   1555  1.44
LINK         O4  NAG B 634                 C1  NAG B 635     1555   1555  1.44
LINK         O4  NAG A 634                 C1  NAG A 635     1555   1555  1.44
LINK         O4  NAG A 632                 C1  NAG A 633     1555   1555  1.44
LINK         ND2 ASN A 480                 C1  NAG A 630     1555   1555  1.45
LINK         O4  NAG B 635                 C1  BMA B 636     1555   1555  1.45
LINK         O4  NAG A 635                 C1  BMA A 636     1555   1555  1.45
LINK         O6  NAG B 630                 C1  FUC B 631     1555   1555  1.45
LINK         ND2 ASN B 480                 C1  NAG B 630     1555   1555  1.51
LINK         O6  NAG A 630                 C1  FUC A 631     1555   1555  1.45
LINK         NE2 HIS A 361                ZN    ZN A 650     1555   1555  1.97
LINK         OE1 GLU B 389                ZN    ZN B 650     1555   1555  1.97
LINK         NE2 HIS B 365                ZN    ZN B 650     1555   1555  2.00
LINK         NE2 HIS B 361                ZN    ZN B 650     1555   1555  2.02
LINK         NE2 HIS A 365                ZN    ZN A 650     1555   1555  2.05
LINK         OE1 GLU A 389                ZN    ZN A 650     1555   1555  2.07
LINK        ZN    ZN B 650                 O3  RX4 B 700     1555   1555  2.16
LINK        ZN    ZN A 650                 O3  RX4 A 700     1555   1555  2.22
LINK        ZN    ZN B 650                 O4  RX4 B 700     1555   1555  2.35
LINK        ZN    ZN A 650                 O4  RX4 A 700     1555   1555  2.42
LINK         O6  NAG B 634                 C1  FUC B 637     1555   1555  1.48
CISPEP   1 ASP A  140    PRO A  141          0         5.16
CISPEP   2 TYR A  607    PRO A  608          0        -1.00
CISPEP   3 ASP B  140    PRO B  141          0         8.09
CISPEP   4 TYR B  607    PRO B  608          0         2.60
SITE     1 AC1  4 HIS A 361  HIS A 365  GLU A 389  RX4 A 700
SITE     1 AC2 22 GLN A 259  HIS A 331  ALA A 332  SER A 333
SITE     2 AC2 22 ALA A 334  HIS A 361  GLU A 362  HIS A 365
SITE     3 AC2 22 TYR A 369  ARG A 381  GLU A 389  LYS A 489
SITE     4 AC2 22 PHE A 490  HIS A 491  TYR A 498  TYR A 501
SITE     5 AC2 22  ZN A 650  HOH A 656  HOH A 666  HOH A 697
SITE     6 AC2 22 HOH A 707  HOH A 813
SITE     1 AC3  5 ASN A 480  THR A 482  FUC A 631  ARG B 245
SITE     2 AC3  5 GLU B 596
SITE     1 AC4  2 NAG A 630  HOH A 705
SITE     1 AC5  6 ASN A  45  THR A  47  GLU A  49  ASN A  50
SITE     2 AC5  6 ARG A 326  NAG A 633
SITE     1 AC6  2 NAG A 632  HOH A 927
SITE     1 AC7  5 ASN A 416  PRO A 524  GLN A 527  NAG A 635
SITE     2 AC7  5 FUC A 637
SITE     1 AC8  2 NAG A 634  BMA A 636
SITE     1 AC9  2 GLU A 522  NAG A 635
SITE     1 BC1  3 PHE A  10  SER A  11  NAG A 634
SITE     1 BC2  7 PHE A 228  ARG A 231  ARG A 235  VAL A 268
SITE     2 BC2  7 VAL A 269  ASN A 588  HOH A 736
SITE     1 BC3  4 TYR A 202  PRO A 497  ARG A 500  HOH A 751
SITE     1 BC4  2 ARG A  96  PHE A 191
SITE     1 BC5  4 TYR B 202  PRO B 497  ARG B 500  HOH B 754
SITE     1 BC6  4 HIS B 361  HIS B 365  GLU B 389  RX4 B 700
SITE     1 BC7 25 GLN B 259  HIS B 331  ALA B 332  SER B 333
SITE     2 BC7 25 ALA B 334  HIS B 361  GLU B 362  HIS B 365
SITE     3 BC7 25 TYR B 369  ARG B 381  HIS B 388  GLU B 389
SITE     4 BC7 25 LYS B 489  PHE B 490  HIS B 491  THR B 496
SITE     5 BC7 25 TYR B 498  TYR B 501   ZN B 650  HOH B 683
SITE     6 BC7 25 HOH B 713  HOH B 769  HOH B 812  HOH B 815
SITE     7 BC7 25 HOH B 865
SITE     1 BC8  5 ARG A 245  GLU A 596  ASN B 480  THR B 482
SITE     2 BC8  5 FUC B 631
SITE     1 BC9  4 THR B 478  ASN B 480  NAG B 630  HOH B 706
SITE     1 CC1  6 ASN B  45  THR B  47  GLU B  49  ASN B  50
SITE     2 CC1  6 ARG B 326  NAG B 633
SITE     1 CC2  1 NAG B 632
SITE     1 CC3  4 ASN B 416  GLN B 527  NAG B 635  FUC B 637
SITE     1 CC4  2 NAG B 634  BMA B 636
SITE     1 CC5  1 NAG B 635
SITE     1 CC6  6 ASN B 416  ASP B 417  THR B 418  ASP B 421
SITE     2 CC6  6 NAG B 634  HOH B 729
SITE     1 CC7  5 TYR A 465  ARG B 453  TYR B 465  LEU B 466
SITE     2 CC7  5 HOH B 793
SITE     1 CC8  7 GLN A 286  GLY A 287  HIS A 292  GLN B 286
SITE     2 CC8  7 GLY B 287  HIS B 292  P6G B 709
SITE     1 CC9  5 ARG A 295  ILE A 408  ILE B 408  PG4 B 705
SITE     2 CC9  5 HOH B 756
SITE     1 DC1  2 ASP B 189  GLY B 190
CRYST1   72.882   76.685   82.646  88.63  64.17  75.70 P 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      0.013721 -0.003497 -0.007010        0.00000
SCALE2      0.000000  0.013457  0.001298        0.00000
SCALE3      0.000000  0.000000  0.013505        0.00000
      
PROCHECK
Go to PROCHECK summary
 References