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PDBsum entry 4ggq

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Isomerase, protein binding PDB id
4ggq
Jmol
Contents
Protein chains
191 a.a.
177 a.a.
Ligands
861 ×4
PEG
Metals
_CA ×2
Waters ×424
HEADER    ISOMERASE, PROTEIN BINDING              07-AUG-12   4GGQ
TITLE     CRYSTAL STRUCTURE OF A SMT FUSION PEPTIDYL-PROLYL CIS-TRANS ISOMERASE
TITLE    2 FROM BURKHOLDERIA PSEUDOMALLEI COMPLEXED WITH CJ40
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: UBIQUITIN-LIKE PROTEIN SMT3, PEPTIDYL-PROLYL CIS-TRANS
COMPND   3 ISOMERASE;
COMPND   4 CHAIN: C, A, B, D;
COMPND   5 FRAGMENT: Q12306 RESIDUES 13-98, Q3JK38 RESIDUES 2-113;
COMPND   6 EC: 5.2.1.8;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: BURKHOLDERIA PSEUDOMALLEI, SACCHAROMYCES
SOURCE   3 CEREVISIAE;
SOURCE   4 ORGANISM_TAXID: 320372, 559292;
SOURCE   5 STRAIN: 1710B, S288C;
SOURCE   6 GENE: BURPS1710B_A0907, SMT3, YDR510W, D9719.15;
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PET28-HISSMT
KEYWDS    SSGCID, ISOMERASE, STRUCTURAL GENOMICS, SEATTLE STRUCTURAL GENOMICS
KEYWDS   2 CENTER FOR INFECTIOUS DISEASE, PROTEIN BINDING
EXPDTA    X-RAY DIFFRACTION
AUTHOR    SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)
REVDAT   3   19-MAR-14 4GGQ    1       REMARK
REVDAT   2   12-MAR-14 4GGQ    1       JRNL
REVDAT   1   15-AUG-12 4GGQ    0
JRNL        AUTH   D.W.BEGLEY,D.FOX,D.JENNER,C.JULI,P.G.PIERCE,J.ABENDROTH,
JRNL        AUTH 2 M.MURUTHI,K.SAFFORD,V.ANDERSON,K.ATKINS,S.R.BARNES,S.O.MOEN,
JRNL        AUTH 3 A.C.RAYMOND,R.STACY,P.J.MYLER,B.L.STAKER,N.J.HARMER,
JRNL        AUTH 4 I.H.NORVILLE,U.HOLZGRABE,M.SARKAR-TYSON,T.E.EDWARDS,
JRNL        AUTH 5 D.D.LORIMER
JRNL        TITL   A STRUCTURAL BIOLOGY APPROACH ENABLES THE DEVELOPMENT OF
JRNL        TITL 2 ANTIMICROBIALS TARGETING BACTERIAL IMMUNOPHILINS.
JRNL        REF    ANTIMICROB.AGENTS CHEMOTHER.  V.  58  1458 2014
JRNL        REFN                   ISSN 0066-4804
JRNL        PMID   24366729
JRNL        DOI    10.1128/AAC.01875-13
REMARK   2
REMARK   2 RESOLUTION.    1.95 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.6.0117
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) : 1.95
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.02
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.0
REMARK   3   NUMBER OF REFLECTIONS             : 54575
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) : 0.189
REMARK   3   R VALUE            (WORKING SET) : 0.187
REMARK   3   FREE R VALUE                     : 0.220
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 2786
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) : 1.95
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.00
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3795
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.66
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2780
REMARK   3   BIN FREE R VALUE SET COUNT          : 177
REMARK   3   BIN FREE R VALUE                    : 0.2990
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 5398
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 145
REMARK   3   SOLVENT ATOMS            : 424
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 34.15
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.61
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.82000
REMARK   3    B22 (A**2) : -0.12000
REMARK   3    B33 (A**2) : -0.70000
REMARK   3    B12 (A**2) : 0.16000
REMARK   3    B13 (A**2) : 0.03000
REMARK   3    B23 (A**2) : -0.12000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.174
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.150
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.099
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.649
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.937
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5672 ; 0.015 ; 0.019
REMARK   3   BOND LENGTHS OTHERS               (A):  3687 ; 0.007 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7698 ; 1.475 ; 1.989
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9003 ; 1.241 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   744 ; 6.398 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   222 ;27.941 ;24.505
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   830 ;12.434 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    27 ;10.868 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   857 ; 0.090 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6455 ; 0.008 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  1144 ; 0.004 ; 0.020
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):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL
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 : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 8
REMARK   3
REMARK   3   TLS GROUP : 1
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   -77        A    -6
REMARK   3    ORIGIN FOR THE GROUP (A): -44.4006 -27.6052 -69.7345
REMARK   3    T TENSOR
REMARK   3      T11:   0.0270 T22:   0.0634
REMARK   3      T33:   0.0090 T12:  -0.0116
REMARK   3      T13:   0.0081 T23:   0.0044
REMARK   3    L TENSOR
REMARK   3      L11:   3.5191 L22:   2.6116
REMARK   3      L33:   4.0956 L12:  -0.5304
REMARK   3      L13:  -0.0958 L23:  -0.3705
REMARK   3    S TENSOR
REMARK   3      S11:   0.0046 S12:   0.1086 S13:   0.1247
REMARK   3      S21:  -0.1459 S22:  -0.0366 S23:  -0.0222
REMARK   3      S31:  -0.0267 S32:   0.0652 S33:   0.0320
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    -5        A   113
REMARK   3    ORIGIN FOR THE GROUP (A): -23.0383 -16.9595 -52.2166
REMARK   3    T TENSOR
REMARK   3      T11:   0.0361 T22:   0.0609
REMARK   3      T33:   0.0465 T12:   0.0031
REMARK   3      T13:  -0.0002 T23:   0.0211
REMARK   3    L TENSOR
REMARK   3      L11:   1.4257 L22:   1.5042
REMARK   3      L33:   1.8441 L12:  -0.6013
REMARK   3      L13:  -0.4487 L23:   0.2590
REMARK   3    S TENSOR
REMARK   3      S11:   0.0640 S12:   0.0171 S13:   0.0799
REMARK   3      S21:  -0.0987 S22:  -0.0336 S23:  -0.0236
REMARK   3      S31:  -0.1566 S32:  -0.0286 S33:  -0.0304
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   -76        B    -5
REMARK   3    ORIGIN FOR THE GROUP (A): -25.6177 -68.6780 -68.0470
REMARK   3    T TENSOR
REMARK   3      T11:   0.2445 T22:   0.1589
REMARK   3      T33:   0.2786 T12:  -0.0084
REMARK   3      T13:  -0.1142 T23:  -0.1751
REMARK   3    L TENSOR
REMARK   3      L11:   6.2172 L22:   4.5835
REMARK   3      L33:   3.5688 L12:   1.4181
REMARK   3      L13:   0.1020 L23:  -0.3533
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0689 S12:   0.5399 S13:  -0.6767
REMARK   3      S21:  -0.3380 S22:  -0.0702 S23:   0.4730
REMARK   3      S31:   0.1737 S32:  -0.1916 S33:   0.1391
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 :   B     1        B   113
REMARK   3    ORIGIN FOR THE GROUP (A): -47.1702 -54.5569 -52.6371
REMARK   3    T TENSOR
REMARK   3      T11:   0.0677 T22:   0.0078
REMARK   3      T33:   0.0684 T12:  -0.0049
REMARK   3      T13:   0.0212 T23:  -0.0024
REMARK   3    L TENSOR
REMARK   3      L11:   1.3520 L22:   1.9681
REMARK   3      L33:   1.9405 L12:   0.2341
REMARK   3      L13:   0.1721 L23:  -0.1311
REMARK   3    S TENSOR
REMARK   3      S11:   0.0074 S12:   0.0965 S13:   0.0312
REMARK   3      S21:   0.0279 S22:   0.0154 S23:   0.0568
REMARK   3      S31:   0.0834 S32:   0.0327 S33:  -0.0228
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 :   C   -77        C    -6
REMARK   3    ORIGIN FOR THE GROUP (A): -27.0636 -28.1061 -14.0734
REMARK   3    T TENSOR
REMARK   3      T11:   0.0456 T22:   0.0732
REMARK   3      T33:   0.0160 T12:   0.0163
REMARK   3      T13:  -0.0196 T23:   0.0100
REMARK   3    L TENSOR
REMARK   3      L11:   3.0843 L22:   2.6183
REMARK   3      L33:   3.3395 L12:   0.4466
REMARK   3      L13:  -0.1718 L23:  -0.2405
REMARK   3    S TENSOR
REMARK   3      S11:   0.0063 S12:  -0.1434 S13:  -0.1309
REMARK   3      S21:   0.0882 S22:  -0.0378 S23:  -0.0385
REMARK   3      S31:  -0.0282 S32:   0.0981 S33:   0.0315
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 :   C    -5        C   113
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.7289 -38.5274 -31.4224
REMARK   3    T TENSOR
REMARK   3      T11:   0.0545 T22:   0.0580
REMARK   3      T33:   0.0422 T12:   0.0059
REMARK   3      T13:   0.0038 T23:   0.0133
REMARK   3    L TENSOR
REMARK   3      L11:   1.2722 L22:   1.3642
REMARK   3      L33:   1.5482 L12:   0.3571
REMARK   3      L13:   0.1223 L23:  -0.0208
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0090 S12:   0.0066 S13:  -0.0626
REMARK   3      S21:   0.0475 S22:  -0.0328 S23:  -0.0004
REMARK   3      S31:   0.1788 S32:   0.0200 S33:   0.0418
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 :   D   -76        D    -7
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.3506 -63.1510 -13.8125
REMARK   3    T TENSOR
REMARK   3      T11:   0.2564 T22:   0.0296
REMARK   3      T33:   0.0734 T12:  -0.0019
REMARK   3      T13:   0.0679 T23:  -0.0249
REMARK   3    L TENSOR
REMARK   3      L11:   5.7863 L22:   7.4689
REMARK   3      L33:   3.8107 L12:  -0.9386
REMARK   3      L13:  -2.1702 L23:   1.8504
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0987 S12:  -0.0124 S13:   0.1336
REMARK   3      S21:   0.6427 S22:  -0.1693 S23:   0.1895
REMARK   3      S31:  -0.0684 S32:  -0.1424 S33:   0.2680
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 :   D    -6        D   113
REMARK   3    ORIGIN FOR THE GROUP (A): -26.1675 -77.1176 -30.8799
REMARK   3    T TENSOR
REMARK   3      T11:   0.0580 T22:   0.0042
REMARK   3      T33:   0.0723 T12:  -0.0042
REMARK   3      T13:   0.0039 T23:   0.0056
REMARK   3    L TENSOR
REMARK   3      L11:   1.0309 L22:   2.3515
REMARK   3      L33:   2.2711 L12:  -0.2718
REMARK   3      L13:  -0.3831 L23:   0.1493
REMARK   3    S TENSOR
REMARK   3      S11:   0.0812 S12:  -0.0467 S13:   0.0265
REMARK   3      S21:   0.0653 S22:  -0.0364 S23:  -0.0012
REMARK   3      S31:  -0.1288 S32:  -0.0138 S33:  -0.0448
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: U VALUES: WITH TLS ADDED HYDROGENS HAVE
REMARK   3  BEEN ADDED IN THE RIDING POSITIONS
REMARK   4
REMARK   4 4GGQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-AUG-12.
REMARK 100 THE RCSB ID CODE IS RCSB074161.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 29-JUN-12
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               : ALS
REMARK 200  BEAMLINE                       : 5.0.3
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.976484
REMARK 200  MONOCHROMATOR                  : SI(220) ASYMMETRIC CUT SINGLE
REMARK 200                                   CRYSTAL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200  DATA SCALING SOFTWARE          : XSCALE
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 54575
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.020
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.0
REMARK 200  DATA REDUNDANCY                : 2.400
REMARK 200  R MERGE                    (I) : 0.05300
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 12.6100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.8
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.50700
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MR
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   (%): 43.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: INTERNAL TRACKING NUMBER 235051A1.
REMARK 280  PUCK IBH5-4, MORPHEUS WELL A1. 10% PEG 20,000, 20% PEG MME550,
REMARK 280  0.03M DIVALENT CATIOS (MGCL2, CACL2), 0.1M MES/IMIDAZOLE PH 6.5,
REMARK 280  DIRECT CRYO. BUPSA.00130.A.D21, 20.00 MG/ML, CJ40 (EBSI2855),
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K
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, 3, 4
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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     MET C   -95
REMARK 465     GLY C   -94
REMARK 465     HIS C   -93
REMARK 465     HIS C   -92
REMARK 465     HIS C   -91
REMARK 465     HIS C   -90
REMARK 465     HIS C   -89
REMARK 465     HIS C   -88
REMARK 465     SER C   -87
REMARK 465     GLY C   -86
REMARK 465     GLU C   -85
REMARK 465     VAL C   -84
REMARK 465     LYS C   -83
REMARK 465     PRO C   -82
REMARK 465     GLU C   -81
REMARK 465     VAL C   -80
REMARK 465     LYS C   -79
REMARK 465     PRO C   -78
REMARK 465     MET A   -95
REMARK 465     GLY A   -94
REMARK 465     HIS A   -93
REMARK 465     HIS A   -92
REMARK 465     HIS A   -91
REMARK 465     HIS A   -90
REMARK 465     HIS A   -89
REMARK 465     HIS A   -88
REMARK 465     SER A   -87
REMARK 465     GLY A   -86
REMARK 465     GLU A   -85
REMARK 465     VAL A   -84
REMARK 465     LYS A   -83
REMARK 465     PRO A   -82
REMARK 465     GLU A   -81
REMARK 465     VAL A   -80
REMARK 465     LYS A   -79
REMARK 465     PRO A   -78
REMARK 465     MET B   -95
REMARK 465     GLY B   -94
REMARK 465     HIS B   -93
REMARK 465     HIS B   -92
REMARK 465     HIS B   -91
REMARK 465     HIS B   -90
REMARK 465     HIS B   -89
REMARK 465     HIS B   -88
REMARK 465     SER B   -87
REMARK 465     GLY B   -86
REMARK 465     GLU B   -85
REMARK 465     VAL B   -84
REMARK 465     LYS B   -83
REMARK 465     PRO B   -82
REMARK 465     GLU B   -81
REMARK 465     VAL B   -80
REMARK 465     LYS B   -79
REMARK 465     PRO B   -78
REMARK 465     GLU B   -77
REMARK 465     GLU B    -4
REMARK 465     GLN B    -3
REMARK 465     ILE B    -2
REMARK 465     GLY B    -1
REMARK 465     GLY B     0
REMARK 465     MET D   -95
REMARK 465     GLY D   -94
REMARK 465     HIS D   -93
REMARK 465     HIS D   -92
REMARK 465     HIS D   -91
REMARK 465     HIS D   -90
REMARK 465     HIS D   -89
REMARK 465     HIS D   -88
REMARK 465     SER D   -87
REMARK 465     GLY D   -86
REMARK 465     GLU D   -85
REMARK 465     VAL D   -84
REMARK 465     LYS D   -83
REMARK 465     PRO D   -82
REMARK 465     GLU D   -81
REMARK 465     VAL D   -80
REMARK 465     LYS D   -79
REMARK 465     PRO D   -78
REMARK 465     GLU D   -77
REMARK 465     SER D   -66
REMARK 465     SER D   -65
REMARK 465     GLY D   -41
REMARK 465     LYS D   -40
REMARK 465     GLU D   -39
REMARK 465     MET D   -38
REMARK 465     ASP D   -37
REMARK 465     ARG D    -5
REMARK 465     GLU D    -4
REMARK 465     GLN D    -3
REMARK 465     ILE D    -2
REMARK 465     GLY D    -1
REMARK 465     GLY D     0
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 C -77    CG   CD   OE1  OE2
REMARK 470     ARG C -51    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU C -39    CG   CD   OE1  OE2
REMARK 470     ASP C -37    CG   OD1  OD2
REMARK 470     ARG C -34    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG C  -5    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU C  -4    CG   CD   OE1  OE2
REMARK 470     ILE C  -2    CG1  CG2  CD1
REMARK 470     ARG C  24    CG   CD   NE   CZ   NH1  NH2
REMARK 470     MET C  61    CG   SD   CE
REMARK 470     GLU A -77    CG   CD   OE1  OE2
REMARK 470     ARG A -51    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS A -40    CG   CD   CE   NZ
REMARK 470     GLU A -39    CG   CD   OE1  OE2
REMARK 470     ASP A -37    CG   OD1  OD2
REMARK 470     ARG A -34    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG A  -5    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU A  -4    CG   CD   OE1  OE2
REMARK 470     ILE A  -2    CG1  CG2  CD1
REMARK 470     SER A   1    OG
REMARK 470     ARG A  24    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS A  74    CG   CD   CE   NZ
REMARK 470     THR B -76    OG1  CG2
REMARK 470     ILE B -74    CG1  CG2  CD1
REMARK 470     LYS B -71    CG   CD   CE   NZ
REMARK 470     ASP B -68    CG   OD1  OD2
REMARK 470     SER B -66    OG
REMARK 470     SER B -65    OG
REMARK 470     GLU B -64    CG   CD   OE1  OE2
REMARK 470     ILE B -63    CG1  CG2  CD1
REMARK 470     ILE B -59    CG1  CG2  CD1
REMARK 470     LYS B -58    CG   CD   CE   NZ
REMARK 470     LYS B -57    CG   CD   CE   NZ
REMARK 470     THR B -56    OG1  CG2
REMARK 470     THR B -55    OG1  CG2
REMARK 470     LEU B -53    CG   CD1  CD2
REMARK 470     ARG B -52    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG B -51    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS B -44    CG   CD   CE   NZ
REMARK 470     GLN B -42    CG   CD   OE1  NE2
REMARK 470     LYS B -40    CG   CD   CE   NZ
REMARK 470     GLU B -39    CG   CD   OE1  OE2
REMARK 470     ASP B -37    CG   OD1  OD2
REMARK 470     SER B -36    OG
REMARK 470     ARG B -34    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ASP B -30    CG   OD1  OD2
REMARK 470     ILE B -28    CG1  CG2  CD1
REMARK 470     ARG B -27    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ILE B -26    CG1  CG2  CD1
REMARK 470     GLN B -25    CG   CD   OE1  NE2
REMARK 470     ASP B -23    CG   OD1  OD2
REMARK 470     GLN B -22    CG   CD   OE1  NE2
REMARK 470     GLU B -19    CG   CD   OE1  OE2
REMARK 470     ASP B -18    CG   OD1  OD2
REMARK 470     LEU B -17    CG   CD1  CD2
REMARK 470     ASP B -16    CG   OD1  OD2
REMARK 470     GLU B -14    CG   CD   OE1  OE2
REMARK 470     ASN B -12    CG   OD1  ND2
REMARK 470     ILE B -10    CG1  CG2  CD1
REMARK 470     GLU B  -8    CG   CD   OE1  OE2
REMARK 470     ARG B  -5    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU B   7    CG   CD   OE1  OE2
REMARK 470     ARG B  24    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLN B  41    CG   CD   OE1  NE2
REMARK 470     THR D -76    OG1  CG2
REMARK 470     ILE D -74    CG1  CG2  CD1
REMARK 470     LYS D -71    CG   CD   CE   NZ
REMARK 470     SER D -69    OG
REMARK 470     ILE D -63    CG1  CG2  CD1
REMARK 470     ILE D -59    CG1  CG2  CD1
REMARK 470     LYS D -58    CG   CD   CE   NZ
REMARK 470     LYS D -57    CG   CD   CE   NZ
REMARK 470     ARG D -51    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS D -44    CG   CD   CE   NZ
REMARK 470     GLN D -42    CG   CD   OE1  NE2
REMARK 470     SER D -36    OG
REMARK 470     LEU D -35    CG   CD1  CD2
REMARK 470     ARG D -34    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LEU D -32    CG   CD1  CD2
REMARK 470     ASP D -30    CG   OD1  OD2
REMARK 470     ILE D -28    CG1  CG2  CD1
REMARK 470     ARG D -27    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLN D -25    CG   CD   OE1  NE2
REMARK 470     ASP D -16    CG   OD1  OD2
REMARK 470     GLU D -14    CG   CD   OE1  OE2
REMARK 470     GLU D  -8    CG   CD   OE1  OE2
REMARK 470     SER D   1    OG
REMARK 470     GLU D  17    CG   CD   OE1  OE2
REMARK 470     ARG D  24    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLN D  41    CG   CD   OE1  NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    ARG C  80   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES
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    SER C -66      -64.05   -130.03
REMARK 500    SER A -66      -62.52   -128.66
REMARK 500    VAL A  97      -34.74   -131.97
REMARK 500    SER B -66      -68.97   -126.11
REMARK 500
REMARK 500 REMARK: NULL
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                              CA C 201  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C  51   OD1
REMARK 620 2 PRO C  52   O    90.5
REMARK 620 3 HOH C 337   O    80.4  93.3
REMARK 620 4 HOH C 307   O   105.9  87.8 173.6
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A 201  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A  51   OD1
REMARK 620 2 PRO A  52   O    89.4
REMARK 620 3 HOH A 323   O    74.1  92.3
REMARK 620 4 HOH A 303   O    94.9  87.9 169.0
REMARK 620 N                    1     2     3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 861 C 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 861 A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 861 B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 861 D 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2KEO   RELATED DB: PDB
REMARK 900 RELATED ID: 2KO7   RELATED DB: PDB
REMARK 900 RELATED ID: 2L2S   RELATED DB: PDB
REMARK 900 RELATED ID: 3VAW   RELATED DB: PDB
REMARK 900 RELATED ID: 3UQB   RELATED DB: PDB
REMARK 900 RELATED ID: 3UQA   RELATED DB: PDB
REMARK 900 RELATED ID: 4DZ3   RELATED DB: PDB
REMARK 900 RELATED ID: 4DZ2   RELATED DB: PDB
REMARK 900 RELATED ID: 3UF8   RELATED DB: PDB
REMARK 900 RELATED ID: 4FN2   RELATED DB: PDB
REMARK 900 RELATED ID: 4G50   RELATED DB: PDB
REMARK 900 RELATED ID: SSGCID-BUPSA.00130.A   RELATED DB: TARGETTRACK
DBREF  4GGQ C  -85     0  UNP    Q12306   SMT3_YEAST      13     98
DBREF  4GGQ C    2   113  UNP    Q3JK38   Q3JK38_BURP1     2    113
DBREF  4GGQ A  -85     0  UNP    Q12306   SMT3_YEAST      13     98
DBREF  4GGQ A    2   113  UNP    Q3JK38   Q3JK38_BURP1     2    113
DBREF  4GGQ B  -85     0  UNP    Q12306   SMT3_YEAST      13     98
DBREF  4GGQ B    2   113  UNP    Q3JK38   Q3JK38_BURP1     2    113
DBREF  4GGQ D  -85     0  UNP    Q12306   SMT3_YEAST      13     98
DBREF  4GGQ D    2   113  UNP    Q3JK38   Q3JK38_BURP1     2    113
SEQADV 4GGQ MET C  -95  UNP  Q12306              EXPRESSION TAG
SEQADV 4GGQ GLY C  -94  UNP  Q12306              EXPRESSION TAG
SEQADV 4GGQ HIS C  -93  UNP  Q12306              EXPRESSION TAG
SEQADV 4GGQ HIS C  -92  UNP  Q12306              EXPRESSION TAG
SEQADV 4GGQ HIS C  -91  UNP  Q12306              EXPRESSION TAG
SEQADV 4GGQ HIS C  -90  UNP  Q12306              EXPRESSION TAG
SEQADV 4GGQ HIS C  -89  UNP  Q12306              EXPRESSION TAG
SEQADV 4GGQ HIS C  -88  UNP  Q12306              EXPRESSION TAG
SEQADV 4GGQ SER C  -87  UNP  Q12306              EXPRESSION TAG
SEQADV 4GGQ GLY C  -86  UNP  Q12306              EXPRESSION TAG
SEQADV 4GGQ SER C    1  UNP  Q12306              LINKER
SEQADV 4GGQ MET A  -95  UNP  Q12306              EXPRESSION TAG
SEQADV 4GGQ GLY A  -94  UNP  Q12306              EXPRESSION TAG
SEQADV 4GGQ HIS A  -93  UNP  Q12306              EXPRESSION TAG
SEQADV 4GGQ HIS A  -92  UNP  Q12306              EXPRESSION TAG
SEQADV 4GGQ HIS A  -91  UNP  Q12306              EXPRESSION TAG
SEQADV 4GGQ HIS A  -90  UNP  Q12306              EXPRESSION TAG
SEQADV 4GGQ HIS A  -89  UNP  Q12306              EXPRESSION TAG
SEQADV 4GGQ HIS A  -88  UNP  Q12306              EXPRESSION TAG
SEQADV 4GGQ SER A  -87  UNP  Q12306              EXPRESSION TAG
SEQADV 4GGQ GLY A  -86  UNP  Q12306              EXPRESSION TAG
SEQADV 4GGQ SER A    1  UNP  Q12306              LINKER
SEQADV 4GGQ MET B  -95  UNP  Q12306              EXPRESSION TAG
SEQADV 4GGQ GLY B  -94  UNP  Q12306              EXPRESSION TAG
SEQADV 4GGQ HIS B  -93  UNP  Q12306              EXPRESSION TAG
SEQADV 4GGQ HIS B  -92  UNP  Q12306              EXPRESSION TAG
SEQADV 4GGQ HIS B  -91  UNP  Q12306              EXPRESSION TAG
SEQADV 4GGQ HIS B  -90  UNP  Q12306              EXPRESSION TAG
SEQADV 4GGQ HIS B  -89  UNP  Q12306              EXPRESSION TAG
SEQADV 4GGQ HIS B  -88  UNP  Q12306              EXPRESSION TAG
SEQADV 4GGQ SER B  -87  UNP  Q12306              EXPRESSION TAG
SEQADV 4GGQ GLY B  -86  UNP  Q12306              EXPRESSION TAG
SEQADV 4GGQ SER B    1  UNP  Q12306              LINKER
SEQADV 4GGQ MET D  -95  UNP  Q12306              EXPRESSION TAG
SEQADV 4GGQ GLY D  -94  UNP  Q12306              EXPRESSION TAG
SEQADV 4GGQ HIS D  -93  UNP  Q12306              EXPRESSION TAG
SEQADV 4GGQ HIS D  -92  UNP  Q12306              EXPRESSION TAG
SEQADV 4GGQ HIS D  -91  UNP  Q12306              EXPRESSION TAG
SEQADV 4GGQ HIS D  -90  UNP  Q12306              EXPRESSION TAG
SEQADV 4GGQ HIS D  -89  UNP  Q12306              EXPRESSION TAG
SEQADV 4GGQ HIS D  -88  UNP  Q12306              EXPRESSION TAG
SEQADV 4GGQ SER D  -87  UNP  Q12306              EXPRESSION TAG
SEQADV 4GGQ GLY D  -86  UNP  Q12306              EXPRESSION TAG
SEQADV 4GGQ SER D    1  UNP  Q12306              LINKER
SEQRES   1 C  209  MET GLY HIS HIS HIS HIS HIS HIS SER GLY GLU VAL LYS
SEQRES   2 C  209  PRO GLU VAL LYS PRO GLU THR HIS ILE ASN LEU LYS VAL
SEQRES   3 C  209  SER ASP GLY SER SER GLU ILE PHE PHE LYS ILE LYS LYS
SEQRES   4 C  209  THR THR PRO LEU ARG ARG LEU MET GLU ALA PHE ALA LYS
SEQRES   5 C  209  ARG GLN GLY LYS GLU MET ASP SER LEU ARG PHE LEU TYR
SEQRES   6 C  209  ASP GLY ILE ARG ILE GLN ALA ASP GLN THR PRO GLU ASP
SEQRES   7 C  209  LEU ASP MET GLU ASP ASN ASP ILE ILE GLU ALA HIS ARG
SEQRES   8 C  209  GLU GLN ILE GLY GLY SER THR VAL VAL THR THR GLU SER
SEQRES   9 C  209  GLY LEU LYS TYR GLU ASP LEU THR GLU GLY SER GLY ALA
SEQRES  10 C  209  GLU ALA ARG ALA GLY GLN THR VAL SER VAL HIS TYR THR
SEQRES  11 C  209  GLY TRP LEU THR ASP GLY GLN LYS PHE ASP SER SER LYS
SEQRES  12 C  209  ASP ARG ASN ASP PRO PHE ALA PHE VAL LEU GLY GLY GLY
SEQRES  13 C  209  MET VAL ILE LYS GLY TRP ASP GLU GLY VAL GLN GLY MET
SEQRES  14 C  209  LYS VAL GLY GLY VAL ARG ARG LEU THR ILE PRO PRO GLN
SEQRES  15 C  209  LEU GLY TYR GLY ALA ARG GLY ALA GLY GLY VAL ILE PRO
SEQRES  16 C  209  PRO ASN ALA THR LEU VAL PHE GLU VAL GLU LEU LEU ASP
SEQRES  17 C  209  VAL
SEQRES   1 A  209  MET GLY HIS HIS HIS HIS HIS HIS SER GLY GLU VAL LYS
SEQRES   2 A  209  PRO GLU VAL LYS PRO GLU THR HIS ILE ASN LEU LYS VAL
SEQRES   3 A  209  SER ASP GLY SER SER GLU ILE PHE PHE LYS ILE LYS LYS
SEQRES   4 A  209  THR THR PRO LEU ARG ARG LEU MET GLU ALA PHE ALA LYS
SEQRES   5 A  209  ARG GLN GLY LYS GLU MET ASP SER LEU ARG PHE LEU TYR
SEQRES   6 A  209  ASP GLY ILE ARG ILE GLN ALA ASP GLN THR PRO GLU ASP
SEQRES   7 A  209  LEU ASP MET GLU ASP ASN ASP ILE ILE GLU ALA HIS ARG
SEQRES   8 A  209  GLU GLN ILE GLY GLY SER THR VAL VAL THR THR GLU SER
SEQRES   9 A  209  GLY LEU LYS TYR GLU ASP LEU THR GLU GLY SER GLY ALA
SEQRES  10 A  209  GLU ALA ARG ALA GLY GLN THR VAL SER VAL HIS TYR THR
SEQRES  11 A  209  GLY TRP LEU THR ASP GLY GLN LYS PHE ASP SER SER LYS
SEQRES  12 A  209  ASP ARG ASN ASP PRO PHE ALA PHE VAL LEU GLY GLY GLY
SEQRES  13 A  209  MET VAL ILE LYS GLY TRP ASP GLU GLY VAL GLN GLY MET
SEQRES  14 A  209  LYS VAL GLY GLY VAL ARG ARG LEU THR ILE PRO PRO GLN
SEQRES  15 A  209  LEU GLY TYR GLY ALA ARG GLY ALA GLY GLY VAL ILE PRO
SEQRES  16 A  209  PRO ASN ALA THR LEU VAL PHE GLU VAL GLU LEU LEU ASP
SEQRES  17 A  209  VAL
SEQRES   1 B  209  MET GLY HIS HIS HIS HIS HIS HIS SER GLY GLU VAL LYS
SEQRES   2 B  209  PRO GLU VAL LYS PRO GLU THR HIS ILE ASN LEU LYS VAL
SEQRES   3 B  209  SER ASP GLY SER SER GLU ILE PHE PHE LYS ILE LYS LYS
SEQRES   4 B  209  THR THR PRO LEU ARG ARG LEU MET GLU ALA PHE ALA LYS
SEQRES   5 B  209  ARG GLN GLY LYS GLU MET ASP SER LEU ARG PHE LEU TYR
SEQRES   6 B  209  ASP GLY ILE ARG ILE GLN ALA ASP GLN THR PRO GLU ASP
SEQRES   7 B  209  LEU ASP MET GLU ASP ASN ASP ILE ILE GLU ALA HIS ARG
SEQRES   8 B  209  GLU GLN ILE GLY GLY SER THR VAL VAL THR THR GLU SER
SEQRES   9 B  209  GLY LEU LYS TYR GLU ASP LEU THR GLU GLY SER GLY ALA
SEQRES  10 B  209  GLU ALA ARG ALA GLY GLN THR VAL SER VAL HIS TYR THR
SEQRES  11 B  209  GLY TRP LEU THR ASP GLY GLN LYS PHE ASP SER SER LYS
SEQRES  12 B  209  ASP ARG ASN ASP PRO PHE ALA PHE VAL LEU GLY GLY GLY
SEQRES  13 B  209  MET VAL ILE LYS GLY TRP ASP GLU GLY VAL GLN GLY MET
SEQRES  14 B  209  LYS VAL GLY GLY VAL ARG ARG LEU THR ILE PRO PRO GLN
SEQRES  15 B  209  LEU GLY TYR GLY ALA ARG GLY ALA GLY GLY VAL ILE PRO
SEQRES  16 B  209  PRO ASN ALA THR LEU VAL PHE GLU VAL GLU LEU LEU ASP
SEQRES  17 B  209  VAL
SEQRES   1 D  209  MET GLY HIS HIS HIS HIS HIS HIS SER GLY GLU VAL LYS
SEQRES   2 D  209  PRO GLU VAL LYS PRO GLU THR HIS ILE ASN LEU LYS VAL
SEQRES   3 D  209  SER ASP GLY SER SER GLU ILE PHE PHE LYS ILE LYS LYS
SEQRES   4 D  209  THR THR PRO LEU ARG ARG LEU MET GLU ALA PHE ALA LYS
SEQRES   5 D  209  ARG GLN GLY LYS GLU MET ASP SER LEU ARG PHE LEU TYR
SEQRES   6 D  209  ASP GLY ILE ARG ILE GLN ALA ASP GLN THR PRO GLU ASP
SEQRES   7 D  209  LEU ASP MET GLU ASP ASN ASP ILE ILE GLU ALA HIS ARG
SEQRES   8 D  209  GLU GLN ILE GLY GLY SER THR VAL VAL THR THR GLU SER
SEQRES   9 D  209  GLY LEU LYS TYR GLU ASP LEU THR GLU GLY SER GLY ALA
SEQRES  10 D  209  GLU ALA ARG ALA GLY GLN THR VAL SER VAL HIS TYR THR
SEQRES  11 D  209  GLY TRP LEU THR ASP GLY GLN LYS PHE ASP SER SER LYS
SEQRES  12 D  209  ASP ARG ASN ASP PRO PHE ALA PHE VAL LEU GLY GLY GLY
SEQRES  13 D  209  MET VAL ILE LYS GLY TRP ASP GLU GLY VAL GLN GLY MET
SEQRES  14 D  209  LYS VAL GLY GLY VAL ARG ARG LEU THR ILE PRO PRO GLN
SEQRES  15 D  209  LEU GLY TYR GLY ALA ARG GLY ALA GLY GLY VAL ILE PRO
SEQRES  16 D  209  PRO ASN ALA THR LEU VAL PHE GLU VAL GLU LEU LEU ASP
SEQRES  17 D  209  VAL
HET     CA  C 201       1
HET    861  C 202      34
HET     CA  A 201       1
HET    PEG  A 202       7
HET    861  A 203      34
HET    861  B 201      34
HET    861  D 201      34
HETNAM      CA CALCIUM ION
HETNAM     861 3-(3,4,5-TRIMETHOXYPHENYL)PROPYL (2S)-1-
HETNAM   2 861  (BENZYLSULFONYL)PIPERIDINE-2-CARBOXYLATE
HETNAM     PEG DI(HYDROXYETHYL)ETHER
FORMUL   5   CA    2(CA 2+)
FORMUL   6  861    4(C25 H33 N O7 S)
FORMUL   8  PEG    C4 H10 O3
FORMUL  12  HOH   *424(H2 O)
HELIX    1   1 LEU C  -53  GLN C  -42  1                                  12
HELIX    2   2 GLU C  -39  ASP C  -37  5                                   3
HELIX    3   3 LYS C   47  ASN C   50  5                                   4
HELIX    4   4 ILE C   63  VAL C   70  1                                   8
HELIX    5   5 PRO C   84  GLY C   88  5                                   5
HELIX    6   6 LEU A  -53  GLN A  -42  1                                  12
HELIX    7   7 GLU A  -39  ASP A  -37  5                                   3
HELIX    8   8 LYS A   47  ASN A   50  5                                   4
HELIX    9   9 ILE A   63  VAL A   70  1                                   8
HELIX   10  10 PRO A   84  GLY A   88  5                                   5
HELIX   11  11 LEU B  -53  GLN B  -42  1                                  12
HELIX   12  12 GLU B  -39  LEU B  -35  5                                   5
HELIX   13  13 LYS B   47  ASN B   50  5                                   4
HELIX   14  14 ILE B   63  VAL B   70  1                                   8
HELIX   15  15 PRO B   84  GLY B   88  5                                   5
HELIX   16  16 LEU D  -53  GLN D  -42  1                                  12
HELIX   17  17 LYS D   47  ASN D   50  5                                   4
HELIX   18  18 ILE D   63  VAL D   70  1                                   8
HELIX   19  19 PRO D   84  GLY D   88  5                                   5
SHEET    1   A 5 GLU C -64  LYS C -58  0
SHEET    2   A 5 HIS C -75  SER C -69 -1  N  VAL C -70   O  ILE C -63
SHEET    3   A 5 ASP C -11  ARG C  -5  1  O  ILE C  -9   N  LYS C -71
SHEET    4   A 5 LEU C -35  TYR C -31 -1  N  LEU C -32   O  GLU C  -8
SHEET    5   A 5 ILE C -28  ARG C -27 -1  O  ILE C -28   N  TYR C -31
SHEET    1   B 6 VAL C   3  THR C   5  0
SHEET    2   B 6 LYS C  11  THR C  16 -1  O  TYR C  12   N  VAL C   4
SHEET    3   B 6 VAL C  78  ILE C  83 -1  O  ARG C  80   N  GLU C  13
SHEET    4   B 6 LEU C 104  ASP C 112 -1  O  LEU C 104   N  ILE C  83
SHEET    5   B 6 THR C  28  LEU C  37 -1  N  TRP C  36   O  VAL C 105
SHEET    6   B 6 LYS C  42  SER C  45 -1  O  ASP C  44   N  GLY C  35
SHEET    1   C 6 VAL C   3  THR C   5  0
SHEET    2   C 6 LYS C  11  THR C  16 -1  O  TYR C  12   N  VAL C   4
SHEET    3   C 6 VAL C  78  ILE C  83 -1  O  ARG C  80   N  GLU C  13
SHEET    4   C 6 LEU C 104  ASP C 112 -1  O  LEU C 104   N  ILE C  83
SHEET    5   C 6 THR C  28  LEU C  37 -1  N  TRP C  36   O  VAL C 105
SHEET    6   C 6 PHE C  53  VAL C  56 -1  O  PHE C  53   N  VAL C  31
SHEET    1   D 5 GLU A -64  LYS A -58  0
SHEET    2   D 5 HIS A -75  SER A -69 -1  N  VAL A -70   O  ILE A -63
SHEET    3   D 5 ASP A -11  ARG A  -5  1  O  ILE A  -9   N  LYS A -71
SHEET    4   D 5 LEU A -35  TYR A -31 -1  N  LEU A -32   O  GLU A  -8
SHEET    5   D 5 ILE A -28  ARG A -27 -1  O  ILE A -28   N  TYR A -31
SHEET    1   E 6 VAL A   3  THR A   5  0
SHEET    2   E 6 LYS A  11  THR A  16 -1  O  TYR A  12   N  VAL A   4
SHEET    3   E 6 VAL A  78  ILE A  83 -1  O  THR A  82   N  LYS A  11
SHEET    4   E 6 LEU A 104  ASP A 112 -1  O  LEU A 104   N  ILE A  83
SHEET    5   E 6 THR A  28  LEU A  37 -1  N  HIS A  32   O  GLU A 109
SHEET    6   E 6 LYS A  42  SER A  45 -1  O  ASP A  44   N  GLY A  35
SHEET    1   F 6 VAL A   3  THR A   5  0
SHEET    2   F 6 LYS A  11  THR A  16 -1  O  TYR A  12   N  VAL A   4
SHEET    3   F 6 VAL A  78  ILE A  83 -1  O  THR A  82   N  LYS A  11
SHEET    4   F 6 LEU A 104  ASP A 112 -1  O  LEU A 104   N  ILE A  83
SHEET    5   F 6 THR A  28  LEU A  37 -1  N  HIS A  32   O  GLU A 109
SHEET    6   F 6 PHE A  53  VAL A  56 -1  O  PHE A  53   N  VAL A  31
SHEET    1   G 5 GLU B -64  LYS B -58  0
SHEET    2   G 5 HIS B -75  SER B -69 -1  N  VAL B -70   O  ILE B -63
SHEET    3   G 5 ASP B -11  HIS B  -6  1  O  ILE B  -9   N  LYS B -71
SHEET    4   G 5 ARG B -34  TYR B -31 -1  N  LEU B -32   O  GLU B  -8
SHEET    5   G 5 ILE B -28  ARG B -27 -1  O  ILE B -28   N  TYR B -31
SHEET    1   H 6 VAL B   3  THR B   5  0
SHEET    2   H 6 LYS B  11  THR B  16 -1  O  TYR B  12   N  VAL B   4
SHEET    3   H 6 VAL B  78  ILE B  83 -1  O  ARG B  80   N  GLU B  13
SHEET    4   H 6 LEU B 104  ASP B 112 -1  O  LEU B 104   N  ILE B  83
SHEET    5   H 6 THR B  28  LEU B  37 -1  N  TRP B  36   O  VAL B 105
SHEET    6   H 6 LYS B  42  SER B  45 -1  O  ASP B  44   N  GLY B  35
SHEET    1   I 6 VAL B   3  THR B   5  0
SHEET    2   I 6 LYS B  11  THR B  16 -1  O  TYR B  12   N  VAL B   4
SHEET    3   I 6 VAL B  78  ILE B  83 -1  O  ARG B  80   N  GLU B  13
SHEET    4   I 6 LEU B 104  ASP B 112 -1  O  LEU B 104   N  ILE B  83
SHEET    5   I 6 THR B  28  LEU B  37 -1  N  TRP B  36   O  VAL B 105
SHEET    6   I 6 PHE B  53  VAL B  56 -1  O  PHE B  53   N  VAL B  31
SHEET    1   J 5 ILE D -63  LYS D -58  0
SHEET    2   J 5 HIS D -75  SER D -69 -1  N  VAL D -70   O  ILE D -63
SHEET    3   J 5 ASP D -11  HIS D  -6  1  O  ILE D  -9   N  LYS D -71
SHEET    4   J 5 ARG D -34  TYR D -31 -1  N  LEU D -32   O  GLU D  -8
SHEET    5   J 5 ILE D -28  ARG D -27 -1  O  ILE D -28   N  TYR D -31
SHEET    1   K 6 VAL D   3  THR D   5  0
SHEET    2   K 6 LYS D  11  THR D  16 -1  O  TYR D  12   N  VAL D   4
SHEET    3   K 6 VAL D  78  ILE D  83 -1  O  ARG D  80   N  GLU D  13
SHEET    4   K 6 LEU D 104  ASP D 112 -1  O  LEU D 104   N  ILE D  83
SHEET    5   K 6 THR D  28  LEU D  37 -1  N  HIS D  32   O  GLU D 109
SHEET    6   K 6 LYS D  42  SER D  45 -1  O  ASP D  44   N  GLY D  35
SHEET    1   L 6 VAL D   3  THR D   5  0
SHEET    2   L 6 LYS D  11  THR D  16 -1  O  TYR D  12   N  VAL D   4
SHEET    3   L 6 VAL D  78  ILE D  83 -1  O  ARG D  80   N  GLU D  13
SHEET    4   L 6 LEU D 104  ASP D 112 -1  O  LEU D 104   N  ILE D  83
SHEET    5   L 6 THR D  28  LEU D  37 -1  N  HIS D  32   O  GLU D 109
SHEET    6   L 6 PHE D  53  VAL D  56 -1  O  PHE D  53   N  VAL D  31
LINK         OD1 ASP C  51                CA    CA C 201     1555   1555  2.15
LINK         OD1 ASP A  51                CA    CA A 201     1555   1555  2.15
LINK         O   PRO C  52                CA    CA C 201     1555   1555  2.29
LINK         O   PRO A  52                CA    CA A 201     1555   1555  2.31
LINK        CA    CA C 201                 O   HOH C 337     1555   1555  2.31
LINK        CA    CA A 201                 O   HOH A 323     1555   1555  2.38
LINK        CA    CA A 201                 O   HOH A 303     1555   1555  2.40
LINK        CA    CA C 201                 O   HOH C 307     1555   1555  2.47
SITE     1 AC1  6 ASP B  51  PRO B  52  ASP C  51  PRO C  52
SITE     2 AC1  6 HOH C 307  HOH C 337
SITE     1 AC2 12 TYR C  33  PHE C  43  ASP C  44  GLY C  60
SITE     2 AC2 12 MET C  61  VAL C  62  ILE C  63  TRP C  66
SITE     3 AC2 12 GLY C  88  TYR C  89  VAL C  97  PHE C 106
SITE     1 AC3  6 ASP A  51  PRO A  52  HOH A 303  HOH A 323
SITE     2 AC3  6 ASP D  51  PRO D  52
SITE     1 AC4  4 ARG A  92  GLY A  95  GLU C   7  861 D 201
SITE     1 AC5 16 TYR A  33  PHE A  43  ASP A  44  PHE A  53
SITE     2 AC5 16 VAL A  62  ILE A  63  TRP A  66  TYR A  89
SITE     3 AC5 16 VAL A  97  ILE A  98  PHE A 106  HOH A 357
SITE     4 AC5 16 HOH A 433  TYR D  33  ASP D  44  PHE D  53
SITE     1 AC6 16 TYR B  33  PHE B  43  ASP B  44  PHE B  53
SITE     2 AC6 16 MET B  61  VAL B  62  ILE B  63  TRP B  66
SITE     3 AC6 16 TYR B  89  VAL B  97  ILE B  98  PHE B 106
SITE     4 AC6 16 TYR C  33  PHE C  53  HOH C 371  HOH C 426
SITE     1 AC7 14 PEG A 202  TYR D  33  PHE D  43  ASP D  44
SITE     2 AC7 14 PHE D  53  GLY D  60  MET D  61  VAL D  62
SITE     3 AC7 14 ILE D  63  TRP D  66  GLY D  88  TYR D  89
SITE     4 AC7 14 ILE D  98  PHE D 106
CRYST1   34.440   76.150   76.350  95.07  90.13  92.65 P 1           4
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      0.029036  0.001344  0.000186        0.00000
SCALE2      0.000000  0.013146  0.001170        0.00000
SCALE3      0.000000  0.000000  0.013149        0.00000
      
PROCHECK
Go to PROCHECK summary
 References