HEADER ENDOCYTOSIS 27-JUN-00 1E42
TITLE BETA2-ADAPTIN APPENDAGE DOMAIN, FROM CLATHRIN ADAPTOR AP2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AP-2 COMPLEX SUBUNIT BETA;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: APPENDAGE DOMAIN, RESIDUES 701-937;
COMPND 5 SYNONYM: PLASMA MEMBRANE ADAPTOR HA2/AP2 ADAPTIN BETA SUBUNIT,
COMPND 6 CLATHRIN ASSEMBLY PROTEIN COMPLEX 2 BETA LARGE CHAIN, AP105B,
COMPND 7 BETA2-ADAPTIN, ADAPTER-RELATED PROTEIN COMPLEX 2 BETA SUBUNIT,
COMPND 8 ADAPTOR PROTEIN COMPLEX AP-2 SUBUNIT BETA;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS ENDOCYTOSIS, ADAPTOR
EXPDTA X-RAY DIFFRACTION
AUTHOR D.J.OWEN,P.R.EVANS,H.T.MCMAHON
REVDAT 3 24-AUG-11 1E42 1 COMPND REMARK DBREF SEQADV
REVDAT 3 2 HETSYN FORMUL VERSN
REVDAT 2 24-FEB-09 1E42 1 VERSN
REVDAT 1 21-AUG-00 1E42 0
JRNL AUTH D.J.OWEN,Y.VALLIS,B.M.F.PEARSE,H.T.MCMAHON,
JRNL AUTH 2 P.R.EVANS
JRNL TITL THE STRUCTURE AND FUNCTION OF THE BETA2-ADAPTIN
JRNL TITL 2 APPENDAGE DOMAIN
JRNL REF EMBO J. V. 19 4216 2000
JRNL REFN ISSN 0261-4189
JRNL PMID 10944104
JRNL DOI 10.1093/EMBOJ/19.16.4216
REMARK 2
REMARK 2 RESOLUTION. 1.7 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 67.42
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 67980
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) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.057
REMARK 3 FREE R VALUE TEST SET COUNT : 3621
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 REFLECTION IN BIN (WORKING SET) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE SET COUNT : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3696
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 37
REMARK 3 SOLVENT ATOMS : 822
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 33.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.90000
REMARK 3 B22 (A**2) : -2.40000
REMARK 3 B33 (A**2) : 1.30000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.80000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.179
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.164
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.116
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.538
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : NULL
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL
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): 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 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED 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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : NULL
REMARK 3 ION PROBE RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RESIDUES A980 AND B980 WERE MODELLED
REMARK 3 AS GLYCEROL, BUT IDENTIFICATION IS NOT CERTAIN. RESIDUE B970
REMARK 3 WAS MODELLED AS A 50% NI ION, SINCE IT IS BOUND TO A
REMARK 3 HISTIDINE, BUT IT MAY BE ANOTHER MG ION
REMARK 4
REMARK 4 1E42 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-JUN-00.
REMARK 100 THE PDBE ID CODE IS EBI-5094.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-SEP-98
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.80
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX9.6
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.88
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 71562
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 19.960
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 4.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 6.850
REMARK 200 R MERGE (I) : 0.15700
REMARK 200 R SYM (I) : 0.15700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.79
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.6
REMARK 200 DATA REDUNDANCY IN SHELL : 4.80
REMARK 200 R MERGE FOR SHELL (I) : 0.75000
REMARK 200 R SYM FOR SHELL (I) : 0.75000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.480
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.9
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS:
REMARK 280 WELL SOLUTION: 1.6 - 2.0M MGCL2, 0.1M BICINE PH 8.7 - 9.0,
REMARK 280 15% GLYCEROL, 1MM DTT. PROTEIN: 40MG/ML, 5MM HEPES, 50MM NACL,
REMARK 280 4MM DTT, 1:1 MIXTURE
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 48.52000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 62.29500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 48.52000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 62.29500
REMARK 290 SMTRY3 4 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 300
REMARK 300 DETAILS:THE BETA-ADAPTIN PROTEIN IS PART OF THE
REMARK 300 ASSEMBLY PROTEINCOMPLEX 2, (AP-2), THAT IS A
REMARK 300 HETEROTETRAMER COMPOSED OF TWO LARGE CHAINS (ALPHA
REMARK 300 AND BETA), A MEDIUM CHAIN (AP50)AND A SMALL
REMARK 300 CHAIN (AP17).
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 MET A 680
REMARK 465 GLY A 681
REMARK 465 SER A 682
REMARK 465 SER A 683
REMARK 465 HIS A 684
REMARK 465 HIS A 685
REMARK 465 HIS A 686
REMARK 465 HIS A 687
REMARK 465 HIS A 688
REMARK 465 HIS A 689
REMARK 465 SER A 690
REMARK 465 SER A 691
REMARK 465 GLY A 692
REMARK 465 LEU A 693
REMARK 465 VAL A 694
REMARK 465 PRO A 695
REMARK 465 ARG A 696
REMARK 465 GLY A 697
REMARK 465 SER A 698
REMARK 465 HIS A 699
REMARK 465 MET A 700
REMARK 465 GLY A 701
REMARK 465 MET A 702
REMARK 465 ALA A 703
REMARK 465 PRO A 704
REMARK 465 MET B 680
REMARK 465 GLY B 681
REMARK 465 SER B 682
REMARK 465 SER B 683
REMARK 465 HIS B 684
REMARK 465 HIS B 685
REMARK 465 HIS B 686
REMARK 465 HIS B 687
REMARK 465 HIS B 688
REMARK 465 HIS B 689
REMARK 465 SER B 690
REMARK 465 SER B 691
REMARK 465 GLY B 692
REMARK 465 LEU B 693
REMARK 465 VAL B 694
REMARK 465 PRO B 695
REMARK 465 ARG B 696
REMARK 465 GLY B 697
REMARK 465 SER B 698
REMARK 465 HIS B 699
REMARK 465 MET B 700
REMARK 465 GLY B 701
REMARK 465 MET B 702
REMARK 465 ALA B 703
REMARK 465 PRO B 704
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 732 CZ NH1 NH2
REMARK 470 GLN A 733 CG CD OE1 NE2
REMARK 470 HIS A 773 ND1 CE1 NE2
REMARK 470 GLU A 828 CD OE1 OE2
REMARK 470 GLU A 847 OE1
REMARK 470 GLN B 733 OE1 NE2
REMARK 470 GLU B 828 CD OE1 OE2
REMARK 470 GLN B 906 OE1
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 2122 O HOH A 2217 1.95
REMARK 500 OE1 GLU B 724 O HOH B 2026 1.95
REMARK 500 O HOH A 2222 O HOH A 2223 1.98
REMARK 500 O HOH A 2251 O HOH A 2255 1.99
REMARK 500 O HOH B 2142 O HOH B 2146 1.99
REMARK 500 O HOH A 2402 O HOH A 2403 1.99
REMARK 500 O HOH B 2385 O HOH B 2386 2.02
REMARK 500 O HOH A 2233 O HOH A 2369 2.02
REMARK 500 O HOH B 2028 O HOH B 2054 2.04
REMARK 500 O GLU B 856 O HOH B 2340 2.04
REMARK 500 OE1 GLN B 748 O HOH B 2092 2.05
REMARK 500 OD1 ASP B 843 O HOH B 2324 2.05
REMARK 500 O HOH B 2120 O HOH B 2187 2.06
REMARK 500 OXT ASN B 937 O HOH B 2418 2.07
REMARK 500 NH1 ARG B 732 O HOH B 2041 2.07
REMARK 500 O HOH A 2323 O HOH A 2349 2.08
REMARK 500 OD2 ASP A 862 O HOH A 2324 2.08
REMARK 500 O HOH A 2290 O HOH A 2291 2.08
REMARK 500 O HOH B 2197 O HOH B 2314 2.09
REMARK 500 O HOH B 2288 O HOH B 2419 2.09
REMARK 500 O HOH B 2183 O HOH B 2298 2.10
REMARK 500 O HOH B 2041 O HOH B 2059 2.10
REMARK 500 OE2 GLU A 798 O HOH A 2216 2.10
REMARK 500 O HOH A 2066 O HOH B 2105 2.10
REMARK 500 O HOH B 2370 O HOH B 2372 2.11
REMARK 500 O HOH A 2134 O HOH B 2134 2.11
REMARK 500 OE1 GLU A 856 O HOH A 2316 2.11
REMARK 500 OD2 ASP A 862 O HOH A 2327 2.11
REMARK 500 OD1 ASP A 843 O HOH A 2295 2.13
REMARK 500 O HOH A 2309 O HOH A 2363 2.13
REMARK 500 O HOH A 2045 O HOH A 2051 2.14
REMARK 500 O ASN A 909 O HOH A 2377 2.16
REMARK 500 O HOH B 2204 O HOH B 2328 2.17
REMARK 500 O HOH B 2120 O HOH B 2289 2.17
REMARK 500 O HOH A 2065 O HOH A 2103 2.17
REMARK 500 OH TYR A 707 O HOH A 2004 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 2064 O HOH B 2138 2555 2.13
REMARK 500 O HOH A 2139 O HOH B 2402 2555 2.13
REMARK 500 O HOH A 2139 O HOH B 2404 2555 2.12
REMARK 500 O HOH A 2140 O HOH B 2404 2555 2.19
REMARK 500 O HOH A 2205 O HOH A 2247 4546 2.07
REMARK 500 O HOH A 2324 O HOH B 2324 3546 2.03
REMARK 500 O HOH A 2327 O HOH B 2324 3546 2.02
REMARK 500 O HOH B 2141 O HOH B 2228 2555 1.95
REMARK 500 O HOH B 2342 O HOH B 2342 2455 2.10
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 TRP B 898 CB TRP B 898 CG -0.108
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 ASP A 752 CB - CG - OD2 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ASP A 783 CB - CG - OD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ASP A 862 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 LEU A 891 CA - CB - CG ANGL. DEV. = 14.3 DEGREES
REMARK 500 ASP B 752 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 LEU B 891 CA - CB - CG ANGL. DEV. = 14.2 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 ASN A 779 -8.35 78.32
REMARK 500 ASN B 779 -6.92 78.39
REMARK 500 ASN B 809 -159.93 -140.94
REMARK 500 GLU B 856 62.10 62.41
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 MG A 960 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 872 OD1
REMARK 620 2 HOH A2340 O 87.7
REMARK 620 3 HOH A2198 O 173.6 97.0
REMARK 620 4 HOH A2332 O 92.6 90.4 91.8
REMARK 620 5 HOH A2337 O 90.9 178.5 84.4 89.8
REMARK 620 6 HOH A2338 O 86.2 89.4 89.4 178.8 90.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 960 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B2351 O
REMARK 620 2 ASN B 872 OD1 90.8
REMARK 620 3 HOH B2357 O 94.0 86.0
REMARK 620 4 HOH B2358 O 177.5 88.9 88.4
REMARK 620 5 HOH B2225 O 87.7 172.7 87.0 92.9
REMARK 620 6 HOH B2361 O 89.5 92.8 176.2 88.0 94.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 961 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 849 OE2
REMARK 620 2 HOH B2330 O 82.4
REMARK 620 3 HOH B2389 O 89.3 88.6
REMARK 620 4 HOH B2331 O 95.6 92.5 175.1
REMARK 620 5 HOH B2253 O 172.0 90.9 86.2 89.0
REMARK 620 6 HOH B2332 O 98.5 179.0 91.9 87.0 88.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 962 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B2199 O
REMARK 620 2 HOH B2315 O 86.7
REMARK 620 3 HOH B2317 O 89.1 95.0
REMARK 620 4 LYS B 842 O 171.5 92.7 82.6
REMARK 620 5 HOH B2325 O 90.1 176.8 84.6 90.4
REMARK 620 6 HOH B2316 O 92.0 87.2 177.6 96.4 93.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI B 970 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 735 NE2
REMARK 620 2 HOH A2148 O 88.4
REMARK 620 3 HOH B2043 O 93.0 89.0
REMARK 620 4 HOH B2049 O 91.4 179.8 91.1
REMARK 620 5 HOH A2096 O 90.4 87.3 175.0 92.6
REMARK 620 6 HOH A2097 O 176.4 88.8 89.3 91.4 87.2
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 971
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 972
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 971
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 972
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 960
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 960
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 961
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 962
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI B 970
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTD A 950
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTD B 950
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 980
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 980
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 CLONING HEADER MGSSHHHHHHSSGLVPRGSHM THEN RESIDUE 701-937
DBREF 1E42 A 701 937 UNP P63010 AP2B1_HUMAN 701 937
DBREF 1E42 B 701 937 UNP P63010 AP2B1_HUMAN 701 937
SEQADV 1E42 MET A 680 UNP P63010 EXPRESSION TAG
SEQADV 1E42 GLY A 681 UNP P63010 EXPRESSION TAG
SEQADV 1E42 SER A 682 UNP P63010 EXPRESSION TAG
SEQADV 1E42 SER A 683 UNP P63010 EXPRESSION TAG
SEQADV 1E42 HIS A 684 UNP P63010 EXPRESSION TAG
SEQADV 1E42 HIS A 685 UNP P63010 EXPRESSION TAG
SEQADV 1E42 HIS A 686 UNP P63010 EXPRESSION TAG
SEQADV 1E42 HIS A 687 UNP P63010 EXPRESSION TAG
SEQADV 1E42 HIS A 688 UNP P63010 EXPRESSION TAG
SEQADV 1E42 HIS A 689 UNP P63010 EXPRESSION TAG
SEQADV 1E42 SER A 690 UNP P63010 EXPRESSION TAG
SEQADV 1E42 SER A 691 UNP P63010 EXPRESSION TAG
SEQADV 1E42 GLY A 692 UNP P63010 EXPRESSION TAG
SEQADV 1E42 LEU A 693 UNP P63010 EXPRESSION TAG
SEQADV 1E42 VAL A 694 UNP P63010 EXPRESSION TAG
SEQADV 1E42 PRO A 695 UNP P63010 EXPRESSION TAG
SEQADV 1E42 ARG A 696 UNP P63010 EXPRESSION TAG
SEQADV 1E42 GLY A 697 UNP P63010 EXPRESSION TAG
SEQADV 1E42 SER A 698 UNP P63010 EXPRESSION TAG
SEQADV 1E42 HIS A 699 UNP P63010 EXPRESSION TAG
SEQADV 1E42 MET A 700 UNP P63010 EXPRESSION TAG
SEQADV 1E42 MET B 680 UNP P63010 EXPRESSION TAG
SEQADV 1E42 GLY B 681 UNP P63010 EXPRESSION TAG
SEQADV 1E42 SER B 682 UNP P63010 EXPRESSION TAG
SEQADV 1E42 SER B 683 UNP P63010 EXPRESSION TAG
SEQADV 1E42 HIS B 684 UNP P63010 EXPRESSION TAG
SEQADV 1E42 HIS B 685 UNP P63010 EXPRESSION TAG
SEQADV 1E42 HIS B 686 UNP P63010 EXPRESSION TAG
SEQADV 1E42 HIS B 687 UNP P63010 EXPRESSION TAG
SEQADV 1E42 HIS B 688 UNP P63010 EXPRESSION TAG
SEQADV 1E42 HIS B 689 UNP P63010 EXPRESSION TAG
SEQADV 1E42 SER B 690 UNP P63010 EXPRESSION TAG
SEQADV 1E42 SER B 691 UNP P63010 EXPRESSION TAG
SEQADV 1E42 GLY B 692 UNP P63010 EXPRESSION TAG
SEQADV 1E42 LEU B 693 UNP P63010 EXPRESSION TAG
SEQADV 1E42 VAL B 694 UNP P63010 EXPRESSION TAG
SEQADV 1E42 PRO B 695 UNP P63010 EXPRESSION TAG
SEQADV 1E42 ARG B 696 UNP P63010 EXPRESSION TAG
SEQADV 1E42 GLY B 697 UNP P63010 EXPRESSION TAG
SEQADV 1E42 SER B 698 UNP P63010 EXPRESSION TAG
SEQADV 1E42 HIS B 699 UNP P63010 EXPRESSION TAG
SEQADV 1E42 MET B 700 UNP P63010 EXPRESSION TAG
SEQRES 1 A 258 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 258 LEU VAL PRO ARG GLY SER HIS MET GLY MET ALA PRO GLY
SEQRES 3 A 258 GLY TYR VAL ALA PRO LYS ALA VAL TRP LEU PRO ALA VAL
SEQRES 4 A 258 LYS ALA LYS GLY LEU GLU ILE SER GLY THR PHE THR HIS
SEQRES 5 A 258 ARG GLN GLY HIS ILE TYR MET GLU MET ASN PHE THR ASN
SEQRES 6 A 258 LYS ALA LEU GLN HIS MET THR ASP PHE ALA ILE GLN PHE
SEQRES 7 A 258 ASN LYS ASN SER PHE GLY VAL ILE PRO SER THR PRO LEU
SEQRES 8 A 258 ALA ILE HIS THR PRO LEU MET PRO ASN GLN SER ILE ASP
SEQRES 9 A 258 VAL SER LEU PRO LEU ASN THR LEU GLY PRO VAL MET LYS
SEQRES 10 A 258 MET GLU PRO LEU ASN ASN LEU GLN VAL ALA VAL LYS ASN
SEQRES 11 A 258 ASN ILE ASP VAL PHE TYR PHE SER CYS LEU ILE PRO LEU
SEQRES 12 A 258 ASN VAL LEU PHE VAL GLU ASP GLY LYS MET GLU ARG GLN
SEQRES 13 A 258 VAL PHE LEU ALA THR TRP LYS ASP ILE PRO ASN GLU ASN
SEQRES 14 A 258 GLU LEU GLN PHE GLN ILE LYS GLU CYS HIS LEU ASN ALA
SEQRES 15 A 258 ASP THR VAL SER SER LYS LEU GLN ASN ASN ASN VAL TYR
SEQRES 16 A 258 THR ILE ALA LYS ARG ASN VAL GLU GLY GLN ASP MET LEU
SEQRES 17 A 258 TYR GLN SER LEU LYS LEU THR ASN GLY ILE TRP ILE LEU
SEQRES 18 A 258 ALA GLU LEU ARG ILE GLN PRO GLY ASN PRO ASN TYR THR
SEQRES 19 A 258 LEU SER LEU LYS CYS ARG ALA PRO GLU VAL SER GLN TYR
SEQRES 20 A 258 ILE TYR GLN VAL TYR ASP SER ILE LEU LYS ASN
SEQRES 1 B 258 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 258 LEU VAL PRO ARG GLY SER HIS MET GLY MET ALA PRO GLY
SEQRES 3 B 258 GLY TYR VAL ALA PRO LYS ALA VAL TRP LEU PRO ALA VAL
SEQRES 4 B 258 LYS ALA LYS GLY LEU GLU ILE SER GLY THR PHE THR HIS
SEQRES 5 B 258 ARG GLN GLY HIS ILE TYR MET GLU MET ASN PHE THR ASN
SEQRES 6 B 258 LYS ALA LEU GLN HIS MET THR ASP PHE ALA ILE GLN PHE
SEQRES 7 B 258 ASN LYS ASN SER PHE GLY VAL ILE PRO SER THR PRO LEU
SEQRES 8 B 258 ALA ILE HIS THR PRO LEU MET PRO ASN GLN SER ILE ASP
SEQRES 9 B 258 VAL SER LEU PRO LEU ASN THR LEU GLY PRO VAL MET LYS
SEQRES 10 B 258 MET GLU PRO LEU ASN ASN LEU GLN VAL ALA VAL LYS ASN
SEQRES 11 B 258 ASN ILE ASP VAL PHE TYR PHE SER CYS LEU ILE PRO LEU
SEQRES 12 B 258 ASN VAL LEU PHE VAL GLU ASP GLY LYS MET GLU ARG GLN
SEQRES 13 B 258 VAL PHE LEU ALA THR TRP LYS ASP ILE PRO ASN GLU ASN
SEQRES 14 B 258 GLU LEU GLN PHE GLN ILE LYS GLU CYS HIS LEU ASN ALA
SEQRES 15 B 258 ASP THR VAL SER SER LYS LEU GLN ASN ASN ASN VAL TYR
SEQRES 16 B 258 THR ILE ALA LYS ARG ASN VAL GLU GLY GLN ASP MET LEU
SEQRES 17 B 258 TYR GLN SER LEU LYS LEU THR ASN GLY ILE TRP ILE LEU
SEQRES 18 B 258 ALA GLU LEU ARG ILE GLN PRO GLY ASN PRO ASN TYR THR
SEQRES 19 B 258 LEU SER LEU LYS CYS ARG ALA PRO GLU VAL SER GLN TYR
SEQRES 20 B 258 ILE TYR GLN VAL TYR ASP SER ILE LEU LYS ASN
HET CL A 971 1
HET CL A 972 1
HET CL B 971 1
HET CL B 972 1
HET MG A 960 1
HET MG B 960 1
HET MG B 961 1
HET MG B 962 1
HET NI B 970 1
HET DTD A 950 8
HET DTD B 950 8
HET GOL A 980 6
HET GOL B 980 6
HETNAM CL CHLORIDE ION
HETNAM MG MAGNESIUM ION
HETNAM NI NICKEL (II) ION
HETNAM DTD DITHIANE DIOL
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 CL 4(CL 1-)
FORMUL 4 MG 4(MG 2+)
FORMUL 5 NI NI 2+
FORMUL 6 DTD 2(C4 H8 O2 S2)
FORMUL 7 GOL 2(C3 H8 O3)
FORMUL 8 HOH *822(H2 O)
HELIX 1 1 PRO A 716 ALA A 720 5 5
HELIX 2 2 PRO A 821 LEU A 825 5 5
HELIX 3 3 GLU A 833 ILE A 844 1 12
HELIX 4 4 PRO A 845 GLU A 849 5 5
HELIX 5 5 ASN A 860 ASN A 870 1 11
HELIX 6 6 ALA A 920 GLU A 922 5 3
HELIX 7 7 VAL A 923 LYS A 936 1 14
HELIX 8 8 PRO B 716 ALA B 720 5 5
HELIX 9 9 PRO B 821 LEU B 825 5 5
HELIX 10 10 GLU B 833 ILE B 844 1 12
HELIX 11 11 PRO B 845 GLU B 849 5 5
HELIX 12 12 ASN B 860 ASN B 870 1 11
HELIX 13 13 ALA B 920 GLU B 922 5 3
HELIX 14 14 VAL B 923 LYS B 936 1 14
SHEET 1 A 4 SER A 781 LEU A 788 0
SHEET 2 A 4 HIS A 735 ASN A 744 -1 N PHE A 742 O ILE A 782
SHEET 3 A 4 LEU A 723 ARG A 732 -1 N ARG A 732 O HIS A 735
SHEET 4 A 4 ALA A 712 LEU A 715 -1 N LEU A 715 O ILE A 725
SHEET 1 B 3 ALA A 754 PHE A 757 0
SHEET 2 B 3 ASN A 802 LYS A 808 -1 N LYS A 808 O ALA A 754
SHEET 3 B 3 VAL A 813 LEU A 819 -1 N CYS A 818 O LEU A 803
SHEET 1 C 5 LEU A 850 ILE A 854 0
SHEET 2 C 5 TYR A 912 CYS A 918 -1 N LEU A 916 O LEU A 850
SHEET 3 C 5 TRP A 898 ILE A 905 -1 N ARG A 904 O THR A 913
SHEET 4 C 5 GLN A 884 LYS A 892 -1 N LEU A 891 O ILE A 899
SHEET 5 C 5 TYR A 874 VAL A 881 -1 N VAL A 881 O GLN A 884
SHEET 1 D 4 SER B 781 LEU B 788 0
SHEET 2 D 4 HIS B 735 ASN B 744 -1 N PHE B 742 O ILE B 782
SHEET 3 D 4 LEU B 723 ARG B 732 -1 N ARG B 732 O HIS B 735
SHEET 4 D 4 ALA B 712 LEU B 715 -1 N LEU B 715 O ILE B 725
SHEET 1 E 3 ALA B 754 PHE B 757 0
SHEET 2 E 3 ASN B 802 LYS B 808 -1 N LYS B 808 O ALA B 754
SHEET 3 E 3 VAL B 813 LEU B 819 -1 N CYS B 818 O LEU B 803
SHEET 1 F 5 LEU B 850 ILE B 854 0
SHEET 2 F 5 TYR B 912 CYS B 918 -1 N LEU B 916 O LEU B 850
SHEET 3 F 5 TRP B 898 ILE B 905 -1 N ARG B 904 O THR B 913
SHEET 4 F 5 GLN B 884 LYS B 892 -1 N LEU B 891 O ILE B 899
SHEET 5 F 5 TYR B 874 VAL B 881 -1 N VAL B 881 O GLN B 884
LINK MG MG A 960 OD1 ASN A 872 1555 1555 2.06
LINK MG MG A 960 O HOH A2340 1555 1555 2.09
LINK MG MG A 960 O HOH A2198 1555 1555 2.07
LINK MG MG A 960 O HOH A2332 1555 1555 2.08
LINK MG MG A 960 O HOH A2337 1555 1555 2.07
LINK MG MG A 960 O HOH A2338 1555 1555 2.07
LINK MG MG B 960 O HOH B2351 1555 1555 2.09
LINK MG MG B 960 OD1 ASN B 872 1555 1555 2.07
LINK MG MG B 960 O HOH B2357 1555 1555 2.06
LINK MG MG B 960 O HOH B2358 1555 1555 2.08
LINK MG MG B 960 O HOH B2225 1555 1555 2.07
LINK MG MG B 960 O HOH B2361 1555 1555 2.08
LINK MG MG B 961 OE2 GLU B 849 1555 1555 2.15
LINK MG MG B 961 O HOH B2330 1555 1555 2.08
LINK MG MG B 961 O HOH B2389 1555 1555 2.04
LINK MG MG B 961 O HOH B2331 1555 1555 2.08
LINK MG MG B 961 O HOH B2253 1555 1555 2.08
LINK MG MG B 961 O HOH B2332 1555 1555 2.07
LINK MG MG B 962 O HOH B2315 1555 1555 2.08
LINK MG MG B 962 O HOH B2317 1555 1555 2.07
LINK MG MG B 962 O LYS B 842 1555 1555 2.08
LINK MG MG B 962 O HOH B2325 1555 1555 2.06
LINK MG MG B 962 O HOH B2316 1555 1555 2.08
LINK MG MG B 962 O HOH B2199 1555 1555 2.07
LINK NI NI B 970 O HOH A2148 1555 1555 2.08
LINK NI NI B 970 O HOH B2043 1555 1555 2.10
LINK NI NI B 970 O HOH B2049 1555 1555 2.10
LINK NI NI B 970 O HOH A2096 1555 1555 2.10
LINK NI NI B 970 O HOH A2097 1555 1555 2.10
LINK NI NI B 970 NE2 HIS B 735 1555 1555 2.17
CISPEP 1 GLU A 798 PRO A 799 0 -1.34
CISPEP 2 GLU B 798 PRO B 799 0 -3.44
SITE 1 AC1 5 ALA A 754 ILE A 755 PRO A 769 LEU A 770
SITE 2 AC1 5 HOH A2060
SITE 1 AC2 3 PRO A 793 VAL A 794 GLN B 756
SITE 1 AC3 4 ALA B 754 ILE B 755 PRO B 769 LEU B 770
SITE 1 AC4 3 GLN A 756 PRO B 793 VAL B 794
SITE 1 AC5 6 ASN A 872 HOH A2198 HOH A2332 HOH A2337
SITE 2 AC5 6 HOH A2338 HOH A2340
SITE 1 AC6 6 ASN B 872 HOH B2225 HOH B2351 HOH B2357
SITE 2 AC6 6 HOH B2358 HOH B2361
SITE 1 AC7 6 GLU B 849 HOH B2253 HOH B2330 HOH B2331
SITE 2 AC7 6 HOH B2332 HOH B2389
SITE 1 AC8 6 LYS B 842 HOH B2199 HOH B2315 HOH B2316
SITE 2 AC8 6 HOH B2317 HOH B2325
SITE 1 AC9 6 HOH A2096 HOH A2097 HOH A2148 HIS B 735
SITE 2 AC9 6 HOH B2043 HOH B2049
SITE 1 BC1 8 ALA A 746 LEU A 747 GLN A 748 ARG A 834
SITE 2 BC1 8 ARG A 879 TYR A 888 HOH A2067 HOH A2402
SITE 1 BC2 9 ALA B 746 LEU B 747 GLN B 748 ARG B 834
SITE 2 BC2 9 ALA B 877 ARG B 879 TYR B 888 HOH B2092
SITE 3 BC2 9 HOH B2419
SITE 1 BC3 7 SER A 761 PHE A 762 ASN A 895 ILE A 897
SITE 2 BC3 7 GLU A 922 VAL A 923 HOH A2119
SITE 1 BC4 5 SER B 761 ASN B 895 ILE B 897 GLU B 922
SITE 2 BC4 5 VAL B 923
CRYST1 97.040 124.590 67.640 90.00 124.18 90.00 C 1 2 1 8
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 0.010305 0.000000 0.006998 0.00000
SCALE2 0.000000 0.008026 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017871 0.00000
MTRIX1 1 -0.379985 0.020033 -0.924776 4.13700 1
MTRIX2 1 -0.011062 -0.999792 -0.017113 50.05200 1
MTRIX3 1 -0.924927 0.003727 0.380127 -5.46700 1
(ATOM LINES ARE NOT SHOWN.)
END
