HEADER TRANSFERASE/TRANSFERASE INHIBITOR 07-JUL-14 4QTD
TITLE STRUCTURE OF HUMAN JNK1 IN COMPLEX WITH SCH772984 AND THE AMPPNP-
TITLE 2 HYDROLYSED TRIPHOSPHATE REVEALING THE SECOND TYPE-I BINDING MODE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 8;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KINASE DOMAIN (1-363);
COMPND 5 SYNONYM: MAP KINASE 8, MAPK 8, JNK-46, STRESS-ACTIVATED PROTEIN
COMPND 6 KINASE 1C, SAPK1C, STRESS-ACTIVATED PROTEIN KINASE JNK1, C-JUN N-
COMPND 7 TERMINAL KINASE 1;
COMPND 8 EC: 2.7.11.24;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: JNK1, MAPK8, PRKM8, SAPK1, SAPK1C;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21-R3-PRARE2;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4
KEYWDS STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC,
KEYWDS 2 TRANSFERASE, KINASE, MAPK, SIGNALLING, INHIBITOR, ALLOSTERIC,
KEYWDS 3 STRUCTURAL GENOMICS CONSORTIUM (SGC), TRANSFERASE-TRANSFERASE
KEYWDS 4 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.CHAIKUAD,T.KEATES,F.VON DELFT,C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA,
AUTHOR 2 S.KNAPP,STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 3 20-SEP-23 4QTD 1 REMARK SEQADV LINK
REVDAT 2 24-SEP-14 4QTD 1 JRNL
REVDAT 1 23-JUL-14 4QTD 0
JRNL AUTH A.CHAIKUAD,E.M C TACCONI,J.ZIMMER,Y.LIANG,N.S.GRAY,
JRNL AUTH 2 M.TARSOUNAS,S.KNAPP
JRNL TITL A UNIQUE INHIBITOR BINDING SITE IN ERK1/2 IS ASSOCIATED WITH
JRNL TITL 2 SLOW BINDING KINETICS.
JRNL REF NAT.CHEM.BIOL. V. 10 853 2014
JRNL REFN ISSN 1552-4450
JRNL PMID 25195011
JRNL DOI 10.1038/NCHEMBIO.1629
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0069
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 59.68
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 60781
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) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.192
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3187
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) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4330
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.77
REMARK 3 BIN R VALUE (WORKING SET) : 0.2520
REMARK 3 BIN FREE R VALUE SET COUNT : 260
REMARK 3 BIN FREE R VALUE : 0.2940
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2871
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 161
REMARK 3 SOLVENT ATOMS : 367
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.47
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.48000
REMARK 3 B22 (A**2) : -0.14000
REMARK 3 B33 (A**2) : -0.34000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.069
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.071
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.049
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.639
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.970
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.959
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3227 ; 0.016 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3151 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4350 ; 1.613 ; 1.987
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7290 ; 0.802 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 399 ; 6.085 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 146 ;36.269 ;24.658
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 579 ;13.564 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;18.880 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 467 ; 0.104 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3701 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 708 ; 0.001 ; 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): 1464 ; 1.414 ; 1.400
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1463 ; 1.415 ; 1.398
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1839 ; 2.242 ; 2.091
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1839 ; 2.243 ; 2.091
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1763 ; 2.483 ; 1.796
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1763 ; 2.481 ; 1.796
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2489 ; 3.548 ; 2.519
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 3926 ; 6.992 ;13.277
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 3927 ; 6.991 ;13.283
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 : 5
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 6 A 55
REMARK 3 ORIGIN FOR THE GROUP (A): 22.6608 8.6994 45.0051
REMARK 3 T TENSOR
REMARK 3 T11: 0.1018 T22: 0.0457
REMARK 3 T33: 0.0084 T12: 0.0079
REMARK 3 T13: 0.0090 T23: 0.0186
REMARK 3 L TENSOR
REMARK 3 L11: 1.3345 L22: 0.9989
REMARK 3 L33: 2.1474 L12: 0.4019
REMARK 3 L13: -0.0973 L23: 0.1002
REMARK 3 S TENSOR
REMARK 3 S11: -0.0485 S12: -0.0095 S13: 0.0158
REMARK 3 S21: 0.1000 S22: -0.0392 S23: -0.0133
REMARK 3 S31: 0.1067 S32: 0.2073 S33: 0.0877
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 56 A 173
REMARK 3 ORIGIN FOR THE GROUP (A): 14.9068 13.7012 30.3932
REMARK 3 T TENSOR
REMARK 3 T11: 0.0784 T22: 0.0340
REMARK 3 T33: 0.0258 T12: -0.0177
REMARK 3 T13: -0.0018 T23: 0.0016
REMARK 3 L TENSOR
REMARK 3 L11: 0.2559 L22: 0.1716
REMARK 3 L33: 1.2228 L12: -0.0148
REMARK 3 L13: 0.5032 L23: 0.1591
REMARK 3 S TENSOR
REMARK 3 S11: -0.0032 S12: -0.0121 S13: 0.0148
REMARK 3 S21: 0.0541 S22: -0.0327 S23: -0.0043
REMARK 3 S31: 0.0192 S32: -0.0470 S33: 0.0359
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 174 A 185
REMARK 3 ORIGIN FOR THE GROUP (A): 24.1301 29.0029 28.8507
REMARK 3 T TENSOR
REMARK 3 T11: 0.0883 T22: 0.1062
REMARK 3 T33: 0.1292 T12: -0.0377
REMARK 3 T13: -0.0306 T23: 0.0689
REMARK 3 L TENSOR
REMARK 3 L11: 6.6400 L22: 3.9410
REMARK 3 L33: 1.2986 L12: -2.5627
REMARK 3 L13: 0.2168 L23: 1.8685
REMARK 3 S TENSOR
REMARK 3 S11: -0.1488 S12: -0.3748 S13: -0.7098
REMARK 3 S21: -0.2147 S22: 0.1352 S23: 0.3365
REMARK 3 S31: -0.1874 S32: -0.0090 S33: 0.0136
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 186 A 338
REMARK 3 ORIGIN FOR THE GROUP (A): 16.0580 16.2893 8.5489
REMARK 3 T TENSOR
REMARK 3 T11: 0.0538 T22: 0.0334
REMARK 3 T33: 0.0337 T12: -0.0030
REMARK 3 T13: 0.0018 T23: -0.0061
REMARK 3 L TENSOR
REMARK 3 L11: 0.1943 L22: 0.7796
REMARK 3 L33: 0.8099 L12: 0.3391
REMARK 3 L13: 0.1386 L23: -0.0684
REMARK 3 S TENSOR
REMARK 3 S11: 0.0105 S12: 0.0146 S13: 0.0014
REMARK 3 S21: 0.0036 S22: 0.0071 S23: 0.0031
REMARK 3 S31: -0.0651 S32: 0.0306 S33: -0.0176
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 339 A 363
REMARK 3 ORIGIN FOR THE GROUP (A): 10.0997 29.5618 40.6222
REMARK 3 T TENSOR
REMARK 3 T11: 0.1666 T22: 0.1182
REMARK 3 T33: 0.0853 T12: 0.0519
REMARK 3 T13: -0.0130 T23: -0.0772
REMARK 3 L TENSOR
REMARK 3 L11: 4.5950 L22: 4.4353
REMARK 3 L33: 1.1848 L12: -3.7637
REMARK 3 L13: 2.0639 L23: -1.1023
REMARK 3 S TENSOR
REMARK 3 S11: -0.3253 S12: -0.3474 S13: 0.2830
REMARK 3 S21: 0.4170 S22: 0.0942 S23: 0.0119
REMARK 3 S31: -0.0938 S32: -0.2423 S33: 0.2311
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4QTD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JUL-14.
REMARK 100 THE DEPOSITION ID IS D_1000086488.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-APR-14
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.8-7.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97625
REMARK 200 MONOCHROMATOR : SI (111) DOUBLE CRYSTAL
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : KIRKPATRICK BAEZ BIMORPH MIRROR
REMARK 200 PAIR
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63969
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 25.750
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 4.90
REMARK 200 R MERGE FOR SHELL (I) : 0.49700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2YDI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12-15% PEG3350 AND 0.1 M HEPES PH 6.8
REMARK 280 -7.8, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 25.47500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 54.08500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.77500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 54.08500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.47500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.77500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 SER A 0
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 ARG A 3
REMARK 465 SER A 4
REMARK 465 LYS A 5
REMARK 465 ALA A 176
REMARK 465 GLY A 177
REMARK 465 THR A 178
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 6 CG CD NE CZ NH1 NH2
REMARK 470 SER A 179 OG
REMARK 470 ASP A 362 CG OD1 OD2
REMARK 470 LEU A 363 CG CD1 CD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 516 O HOH A 788 2.10
REMARK 500 OD2 ASP A 169 O HOH A 778 2.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 126 CD GLU A 126 OE1 0.086
REMARK 500 GLU A 126 CD GLU A 126 OE2 0.080
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 263 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 263 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 GLN A 102 -52.06 -130.18
REMARK 500 ARG A 150 -12.26 72.51
REMARK 500 ALA A 173 -132.30 53.16
REMARK 500 PRO A 264 150.98 -47.44
REMARK 500 ALA A 282 35.63 -158.20
REMARK 500 ASP A 362 69.04 66.16
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 ANP A 425
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 MG A 426 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 156 OD1
REMARK 620 2 38Z A 424 O 103.5
REMARK 620 3 ANP A 425 O1A 95.7 155.8
REMARK 620 4 ANP A 425 O1B 166.7 82.5 82.0
REMARK 620 5 ANP A 425 O3G 85.0 102.8 93.3 82.0
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 413
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 414
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 415
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 416
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 417
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 418
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 419
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 420
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 421
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 422
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE A 423
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 38Z A 424
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP A 425
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 426
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4QTA RELATED DB: PDB
REMARK 900 RELATED ID: 4QTB RELATED DB: PDB
REMARK 900 RELATED ID: 4QTC RELATED DB: PDB
REMARK 900 RELATED ID: 4QTE RELATED DB: PDB
DBREF 4QTD A 1 363 UNP P45983 MK08_HUMAN 1 363
SEQADV 4QTD SER A 0 UNP P45983 EXPRESSION TAG
SEQRES 1 A 364 SER MET SER ARG SER LYS ARG ASP ASN ASN PHE TYR SER
SEQRES 2 A 364 VAL GLU ILE GLY ASP SER THR PHE THR VAL LEU LYS ARG
SEQRES 3 A 364 TYR GLN ASN LEU LYS PRO ILE GLY SER GLY ALA GLN GLY
SEQRES 4 A 364 ILE VAL CYS ALA ALA TYR ASP ALA ILE LEU GLU ARG ASN
SEQRES 5 A 364 VAL ALA ILE LYS LYS LEU SER ARG PRO PHE GLN ASN GLN
SEQRES 6 A 364 THR HIS ALA LYS ARG ALA TYR ARG GLU LEU VAL LEU MET
SEQRES 7 A 364 LYS CYS VAL ASN HIS LYS ASN ILE ILE GLY LEU LEU ASN
SEQRES 8 A 364 VAL PHE THR PRO GLN LYS SER LEU GLU GLU PHE GLN ASP
SEQRES 9 A 364 VAL TYR ILE VAL MET GLU LEU MET ASP ALA ASN LEU CYS
SEQRES 10 A 364 GLN VAL ILE GLN MET GLU LEU ASP HIS GLU ARG MET SER
SEQRES 11 A 364 TYR LEU LEU TYR GLN MET LEU CYS GLY ILE LYS HIS LEU
SEQRES 12 A 364 HIS SER ALA GLY ILE ILE HIS ARG ASP LEU LYS PRO SER
SEQRES 13 A 364 ASN ILE VAL VAL LYS SER ASP CYS THR LEU LYS ILE LEU
SEQRES 14 A 364 ASP PHE GLY LEU ALA ARG THR ALA GLY THR SER PHE MET
SEQRES 15 A 364 MET THR PRO TYR VAL VAL THR ARG TYR TYR ARG ALA PRO
SEQRES 16 A 364 GLU VAL ILE LEU GLY MET GLY TYR LYS GLU ASN VAL ASP
SEQRES 17 A 364 LEU TRP SER VAL GLY CYS ILE MET GLY GLU MET VAL CYS
SEQRES 18 A 364 HIS LYS ILE LEU PHE PRO GLY ARG ASP TYR ILE ASP GLN
SEQRES 19 A 364 TRP ASN LYS VAL ILE GLU GLN LEU GLY THR PRO CYS PRO
SEQRES 20 A 364 GLU PHE MET LYS LYS LEU GLN PRO THR VAL ARG THR TYR
SEQRES 21 A 364 VAL GLU ASN ARG PRO LYS TYR ALA GLY TYR SER PHE GLU
SEQRES 22 A 364 LYS LEU PHE PRO ASP VAL LEU PHE PRO ALA ASP SER GLU
SEQRES 23 A 364 HIS ASN LYS LEU LYS ALA SER GLN ALA ARG ASP LEU LEU
SEQRES 24 A 364 SER LYS MET LEU VAL ILE ASP ALA SER LYS ARG ILE SER
SEQRES 25 A 364 VAL ASP GLU ALA LEU GLN HIS PRO TYR ILE ASN VAL TRP
SEQRES 26 A 364 TYR ASP PRO SER GLU ALA GLU ALA PRO PRO PRO LYS ILE
SEQRES 27 A 364 PRO ASP LYS GLN LEU ASP GLU ARG GLU HIS THR ILE GLU
SEQRES 28 A 364 GLU TRP LYS GLU LEU ILE TYR LYS GLU VAL MET ASP LEU
HET EDO A 401 4
HET EDO A 402 4
HET EDO A 403 4
HET EDO A 404 4
HET EDO A 405 4
HET EDO A 406 4
HET EDO A 407 4
HET EDO A 408 8
HET EDO A 409 8
HET EDO A 410 4
HET EDO A 411 4
HET EDO A 412 4
HET EDO A 413 4
HET EDO A 414 4
HET EDO A 415 4
HET EDO A 416 4
HET EDO A 417 4
HET EDO A 418 4
HET EDO A 419 4
HET EDO A 420 4
HET EDO A 421 4
HET EDO A 422 4
HET EPE A 423 15
HET 38Z A 424 44
HET ANP A 425 13
HET MG A 426 1
HETNAM EDO 1,2-ETHANEDIOL
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETNAM 38Z (3R)-1-(2-OXO-2-{4-[4-(PYRIMIDIN-2-YL)PHENYL]PIPERAZIN-
HETNAM 2 38Z 1-YL}ETHYL)-N-[3-(PYRIDIN-4-YL)-2H-INDAZOL-5-
HETNAM 3 38Z YL]PYRROLIDINE-3-CARBOXAMIDE
HETNAM ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
HETNAM MG MAGNESIUM ION
HETSYN EDO ETHYLENE GLYCOL
HETSYN EPE HEPES
FORMUL 2 EDO 22(C2 H6 O2)
FORMUL 24 EPE C8 H18 N2 O4 S
FORMUL 25 38Z C33 H33 N9 O2
FORMUL 26 ANP C10 H17 N6 O12 P3
FORMUL 27 MG MG 2+
FORMUL 28 HOH *367(H2 O)
HELIX 1 1 PRO A 60 GLN A 62 5 3
HELIX 2 2 ASN A 63 VAL A 80 1 18
HELIX 3 3 LEU A 115 ILE A 119 1 5
HELIX 4 4 ASP A 124 ALA A 145 1 22
HELIX 5 5 LYS A 153 SER A 155 5 3
HELIX 6 6 ALA A 193 LEU A 198 1 6
HELIX 7 7 ASN A 205 HIS A 221 1 17
HELIX 8 8 ASP A 229 GLY A 242 1 14
HELIX 9 9 CYS A 245 LYS A 250 1 6
HELIX 10 10 GLN A 253 ARG A 263 1 11
HELIX 11 11 SER A 270 PHE A 275 1 6
HELIX 12 12 PRO A 276 PHE A 280 5 5
HELIX 13 13 SER A 284 LEU A 302 1 19
HELIX 14 14 ASP A 305 ARG A 309 5 5
HELIX 15 15 SER A 311 GLN A 317 1 7
HELIX 16 16 ILE A 321 TYR A 325 5 5
HELIX 17 17 ASP A 326 GLU A 331 1 6
HELIX 18 18 THR A 348 ASP A 362 1 15
SHEET 1 A 2 PHE A 10 ILE A 15 0
SHEET 2 A 2 SER A 18 LEU A 23 -1 O SER A 18 N ILE A 15
SHEET 1 B 5 TYR A 26 GLY A 35 0
SHEET 2 B 5 GLY A 38 ASP A 45 -1 O VAL A 40 N GLY A 33
SHEET 3 B 5 ARG A 50 SER A 58 -1 O ILE A 54 N CYS A 41
SHEET 4 B 5 ASP A 103 GLU A 109 -1 O VAL A 104 N LEU A 57
SHEET 5 B 5 LEU A 88 PHE A 92 -1 N LEU A 89 O VAL A 107
SHEET 1 C 3 ALA A 113 ASN A 114 0
SHEET 2 C 3 ILE A 157 VAL A 159 -1 O VAL A 159 N ALA A 113
SHEET 3 C 3 LEU A 165 ILE A 167 -1 O LYS A 166 N VAL A 158
LINK OD1AASN A 156 MG MG A 426 1555 1555 2.26
LINK O 38Z A 424 MG MG A 426 1555 1555 2.21
LINK O1A ANP A 425 MG MG A 426 1555 1555 1.93
LINK O1B ANP A 425 MG MG A 426 1555 1555 1.97
LINK O3G ANP A 425 MG MG A 426 1555 1555 1.98
SITE 1 AC1 6 GLN A 120 GLU A 217 HIS A 221 LYS A 222
SITE 2 AC1 6 ILE A 223 HOH A 687
SITE 1 AC2 4 CYS A 220 GLN A 240 LEU A 274 HOH A 648
SITE 1 AC3 9 PRO A 244 CYS A 245 PHE A 248 VAL A 303
SITE 2 AC3 9 ILE A 304 ASP A 305 HOH A 539 HOH A 565
SITE 3 AC3 9 HOH A 728
SITE 1 AC4 1 GLN A 317
SITE 1 AC5 4 GLY A 201 TYR A 202 HOH A 581 HOH A 737
SITE 1 AC6 6 VAL A 80 ASN A 81 HIS A 141 PRO A 333
SITE 2 AC6 6 PRO A 335 HOH A 708
SITE 1 AC7 3 HIS A 82 LYS A 83 SER A 328
SITE 1 AC8 6 ARG A 59 GLN A 62 GLU A 122 PRO A 281
SITE 2 AC8 6 EDO A 409 HOH A 749
SITE 1 AC9 10 ARG A 59 GLU A 122 LEU A 123 VAL A 278
SITE 2 AC9 10 LEU A 279 PHE A 280 PRO A 281 EDO A 408
SITE 3 AC9 10 HOH A 502 HOH A 609
SITE 1 BC1 3 TYR A 269 SER A 307 HOH A 816
SITE 1 BC2 2 SER A 292 HOH A 601
SITE 1 BC3 7 ASN A 28 ALA A 42 ALA A 43 TYR A 44
SITE 2 BC3 7 ASN A 51 ILE A 231 HOH A 593
SITE 1 BC4 3 ARG A 50 ASN A 51 ASP A 229
SITE 1 BC5 4 LEU A 88 LEU A 89 ASN A 90 HOH A 662
SITE 1 BC6 6 HIS A 125 GLU A 126 SER A 129 LYS A 290
SITE 2 BC6 6 TYR A 320 HOH A 750
SITE 1 BC7 1 TRP A 324
SITE 1 BC8 5 ASP A 326 GLU A 329 LYS A 340 GLN A 341
SITE 2 BC8 5 HOH A 517
SITE 1 BC9 1 TYR A 130
SITE 1 CC1 7 LYS A 203 ASN A 205 ALA A 306 EPE A 423
SITE 2 CC1 7 HOH A 668 HOH A 814 HOH A 815
SITE 1 CC2 4 LEU A 241 ALA A 267 TYR A 269 SER A 270
SITE 1 CC3 1 GLN A 253
SITE 1 CC4 6 GLU A 272 PRO A 276 ASP A 277 ARG A 295
SITE 2 CC4 6 HOH A 533 HOH A 634
SITE 1 CC5 17 LYS A 203 GLU A 204 ASN A 205 GLU A 239
SITE 2 CC5 17 TYR A 266 GLY A 268 TYR A 269 ARG A 309
SITE 3 CC5 17 SER A 311 GLU A 314 EDO A 419 HOH A 507
SITE 4 CC5 17 HOH A 554 HOH A 671 HOH A 741 HOH A 814
SITE 5 CC5 17 HOH A 815
SITE 1 CC6 20 VAL A 40 ALA A 53 GLU A 109 MET A 111
SITE 2 CC6 20 ASP A 112 ALA A 113 ASN A 114 CYS A 116
SITE 3 CC6 20 GLN A 117 GLN A 120 SER A 155 ASN A 156
SITE 4 CC6 20 LEU A 168 ANP A 425 MG A 426 HOH A 544
SITE 5 CC6 20 HOH A 597 HOH A 775 HOH A 817 HOH A 857
SITE 1 CC7 14 GLY A 35 ALA A 36 GLN A 37 LYS A 153
SITE 2 CC7 14 SER A 155 ASN A 156 THR A 188 38Z A 424
SITE 3 CC7 14 MG A 426 HOH A 607 HOH A 818 HOH A 819
SITE 4 CC7 14 HOH A 821 HOH A 867
SITE 1 CC8 3 ASN A 156 38Z A 424 ANP A 425
CRYST1 50.950 71.550 108.170 90.00 90.00 90.00 P 21 21 21 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 0.019627 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013976 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009245 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
