HEADER PROTEIN TRANSPORT 25-JUN-02 1M2V
TITLE CRYSTAL STRUCTURE OF THE YEAST SEC23/24 HETERODIMER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN TRANSPORT PROTEIN SEC23;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SEC23; SEC23P; CYTOPLASMIC GTPASE-ACTIVATING PROTEIN; SEC23
COMPND 5 COPII-COAT PROTEIN;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: PROTEIN TRANSPORT PROTEIN SEC24;
COMPND 9 CHAIN: B;
COMPND 10 SYNONYM: SEC24; SEC24P; SEC24 PROTEIN; ABNORMAL NUCLEAR MORPHOLOGY 1
COMPND 11 SEC24 COPII-COAT PROTEIN;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: SEC23;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 10 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 11 ORGANISM_TAXID: 4932;
SOURCE 12 GENE: SAR1;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ZINC-FINGER, BETA BARREL, VWA DOMAIN, GELSOLIN DOMAIN, PROTEIN
KEYWDS 2 TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR X.BI,R.A.CORPINA,J.GOLDBERG
REVDAT 3 14-FEB-24 1M2V 1 REMARK LINK
REVDAT 2 24-FEB-09 1M2V 1 VERSN
REVDAT 1 20-SEP-02 1M2V 0
JRNL AUTH X.BI,R.A.CORPINA,J.GOLDBERG
JRNL TITL STRUCTURE OF THE SEC23/24-SAR1 PRE-BUDDING COMPLEX OF THE
JRNL TITL 2 COPII VESICLE COAT
JRNL REF NATURE V. 419 271 2002
JRNL REFN ISSN 0028-0836
JRNL PMID 12239560
JRNL DOI 10.1038/NATURE01040
REMARK 2
REMARK 2 RESOLUTION. 2.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.96
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 91.2
REMARK 3 NUMBER OF REFLECTIONS : 49495
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 SET) : 0.210
REMARK 3 FREE R VALUE : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2388
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.92
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 67.50
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5694
REMARK 3 BIN R VALUE (WORKING SET) : 0.3320
REMARK 3 BIN FREE R VALUE : 0.3970
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.40
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 326
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.022
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11506
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 69
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 37.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.87000
REMARK 3 B22 (A**2) : 7.31000
REMARK 3 B33 (A**2) : -13.19000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.41
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.62
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.950
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.400 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.470 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.890 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.030 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.37
REMARK 3 BSOL : 38.23
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : &_1_PARAMETER_INFILE_4
REMARK 3 PARAMETER FILE 5 : &_1_PARAMETER_INFILE_5
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : &_1_TOPOLOGY_INFILE_4
REMARK 3 TOPOLOGY FILE 5 : &_1_TOPOLOGY_INFILE_5
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1M2V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JUL-02.
REMARK 100 THE DEPOSITION ID IS D_1000016528.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-FEB-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X25
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.050
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : CCP4 (TRUNCATE)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49463
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.750
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.2
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.92
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: SEC23 FROM PDB ENTRY 1M2O
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0 M AMMONIUM FORMATE, 18 MM
REMARK 280 DITHIOTHREITOL, 10 % (W/V) XYLITOL, 0.1 M HEPES PH 7.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP AT 273K
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 45.15450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 90.10000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 63.18550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 90.10000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 45.15450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 63.18550
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 1
REMARK 465 GLY A 199
REMARK 465 GLN A 200
REMARK 465 LYS A 201
REMARK 465 PRO A 202
REMARK 465 THR A 203
REMARK 465 GLY A 204
REMARK 465 PRO A 205
REMARK 465 GLY A 206
REMARK 465 GLY A 207
REMARK 465 ALA A 208
REMARK 465 ALA A 209
REMARK 465 SER A 210
REMARK 465 HIS A 211
REMARK 465 LEU A 212
REMARK 465 PRO A 213
REMARK 465 ASN A 214
REMARK 465 ALA A 215
REMARK 465 MET A 216
REMARK 465 ASN A 217
REMARK 465 LYS A 218
REMARK 465 VAL A 219
REMARK 465 THR A 220
REMARK 465 ALA A 466
REMARK 465 ALA A 467
REMARK 465 ASN A 468
REMARK 465 SER A 469
REMARK 465 ASN A 470
REMARK 465 PRO A 471
REMARK 465 MET A 472
REMARK 465 MET A 473
REMARK 465 SER A 474
REMARK 465 ALA A 475
REMARK 465 PRO A 476
REMARK 465 GLY A 477
REMARK 465 SER A 478
REMARK 465 ALA A 479
REMARK 465 ASP A 480
REMARK 465 ASP A 543
REMARK 465 ASP A 544
REMARK 465 GLY A 545
REMARK 465 ALA A 546
REMARK 465 ASN A 729
REMARK 465 PRO A 730
REMARK 465 SER A 731
REMARK 465 ASP A 732
REMARK 465 ASN A 733
REMARK 465 TYR A 734
REMARK 465 GLN A 735
REMARK 465 ASP A 736
REMARK 465 MET A 737
REMARK 465 ALA A 738
REMARK 465 ARG A 739
REMARK 465 GLY A 740
REMARK 465 GLY A 741
REMARK 465 SER A 742
REMARK 465 THR A 743
REMARK 465 ILE A 744
REMARK 465 VAL A 745
REMARK 465 LEU A 746
REMARK 465 THR A 747
REMARK 465 ASP A 748
REMARK 465 ASP A 749
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 HIS B 3
REMARK 465 HIS B 4
REMARK 465 LYS B 5
REMARK 465 LYS B 6
REMARK 465 ARG B 7
REMARK 465 VAL B 8
REMARK 465 TYR B 9
REMARK 465 PRO B 10
REMARK 465 GLN B 11
REMARK 465 ALA B 12
REMARK 465 GLN B 13
REMARK 465 LEU B 14
REMARK 465 GLN B 15
REMARK 465 TYR B 16
REMARK 465 GLY B 17
REMARK 465 GLN B 18
REMARK 465 ASN B 19
REMARK 465 ALA B 20
REMARK 465 THR B 21
REMARK 465 PRO B 22
REMARK 465 LEU B 23
REMARK 465 GLN B 24
REMARK 465 GLN B 25
REMARK 465 PRO B 26
REMARK 465 ALA B 27
REMARK 465 GLN B 28
REMARK 465 PHE B 29
REMARK 465 MET B 30
REMARK 465 PRO B 31
REMARK 465 PRO B 32
REMARK 465 GLN B 33
REMARK 465 ASP B 34
REMARK 465 PRO B 35
REMARK 465 ALA B 36
REMARK 465 ALA B 37
REMARK 465 ALA B 38
REMARK 465 GLY B 39
REMARK 465 MET B 40
REMARK 465 SER B 41
REMARK 465 TYR B 42
REMARK 465 GLY B 43
REMARK 465 GLN B 44
REMARK 465 MET B 45
REMARK 465 GLY B 46
REMARK 465 MET B 47
REMARK 465 PRO B 48
REMARK 465 PRO B 49
REMARK 465 GLN B 50
REMARK 465 GLY B 51
REMARK 465 ALA B 52
REMARK 465 VAL B 53
REMARK 465 PRO B 54
REMARK 465 SER B 55
REMARK 465 MET B 56
REMARK 465 GLY B 57
REMARK 465 GLN B 58
REMARK 465 GLN B 59
REMARK 465 GLN B 60
REMARK 465 ASP B 74
REMARK 465 GLN B 75
REMARK 465 ALA B 76
REMARK 465 THR B 77
REMARK 465 THR B 78
REMARK 465 SER B 79
REMARK 465 MET B 80
REMARK 465 ASN B 81
REMARK 465 ASP B 82
REMARK 465 MET B 83
REMARK 465 HIS B 84
REMARK 465 LEU B 85
REMARK 465 HIS B 86
REMARK 465 ASN B 87
REMARK 465 VAL B 88
REMARK 465 PRO B 89
REMARK 465 LEU B 90
REMARK 465 VAL B 91
REMARK 465 ASP B 92
REMARK 465 PRO B 93
REMARK 465 ASN B 94
REMARK 465 ALA B 95
REMARK 465 TYR B 96
REMARK 465 MET B 97
REMARK 465 GLN B 98
REMARK 465 PRO B 99
REMARK 465 GLN B 100
REMARK 465 VAL B 101
REMARK 465 PRO B 102
REMARK 465 VAL B 103
REMARK 465 GLN B 104
REMARK 465 MET B 105
REMARK 465 GLY B 106
REMARK 465 THR B 107
REMARK 465 PRO B 108
REMARK 465 LEU B 109
REMARK 465 GLN B 110
REMARK 465 GLN B 111
REMARK 465 GLN B 112
REMARK 465 GLN B 113
REMARK 465 GLN B 114
REMARK 465 PRO B 115
REMARK 465 MET B 116
REMARK 465 ALA B 117
REMARK 465 ALA B 118
REMARK 465 PRO B 119
REMARK 465 ALA B 120
REMARK 465 TYR B 121
REMARK 465 GLY B 122
REMARK 465 GLN B 123
REMARK 465 PRO B 124
REMARK 465 SER B 125
REMARK 465 ALA B 126
REMARK 465 ALA B 127
REMARK 465 MET B 128
REMARK 465 GLY B 129
REMARK 465 GLN B 130
REMARK 465 ASN B 131
REMARK 465 MET B 132
REMARK 465 SER B 363
REMARK 465 GLU B 364
REMARK 465 ASN B 365
REMARK 465 ASN B 366
REMARK 465 GLU B 367
REMARK 465 GLU B 368
REMARK 465 SER B 369
REMARK 465 ALA B 370
REMARK 465 ASP B 371
REMARK 465 SER B 463
REMARK 465 GLY B 464
REMARK 465 VAL B 465
REMARK 465 VAL B 466
REMARK 465 VAL B 770
REMARK 465 GLN B 771
REMARK 465 THR B 772
REMARK 465 GLU B 773
REMARK 465 ASP B 774
REMARK 465 GLY B 775
REMARK 465 GLU B 776
REMARK 465 ALA B 777
REMARK 465 THR B 778
REMARK 465 ASP B 823
REMARK 465 VAL B 824
REMARK 465 PHE B 825
REMARK 465 GLY B 826
REMARK 465 THR B 827
REMARK 465 GLN B 828
REMARK 465 ASP B 829
REMARK 465 ILE B 830
REMARK 465 PHE B 831
REMARK 465 ASP B 832
REMARK 465 ILE B 833
REMARK 465 PRO B 834
REMARK 465 ILE B 835
REMARK 465 GLY B 836
REMARK 465 LYS B 837
REMARK 465 GLN B 838
REMARK 465 GLU B 839
REMARK 465 ILE B 840
REMARK 465 PRO B 841
REMARK 465 VAL B 842
REMARK 465 VAL B 843
REMARK 465 GLU B 844
REMARK 465 ASN B 845
REMARK 465 SER B 846
REMARK 465 GLU B 847
REMARK 465 GLY B 876
REMARK 465 ALA B 877
REMARK 465 SER B 878
REMARK 465 LEU B 879
REMARK 465 SER B 880
REMARK 465 GLU B 881
REMARK 465 PRO B 882
REMARK 465 VAL B 883
REMARK 465 ASN B 884
REMARK 465 HIS B 885
REMARK 465 ALA B 886
REMARK 465 SER B 887
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 481 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 875 CG CD NE CZ NH1 NH2
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 TYR B 296 NH1 ARG B 624 2.19
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 GLY A 677 N - CA - C ANGL. DEV. = 17.3 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 VAL A 30 -69.78 64.22
REMARK 500 CYS A 61 -72.22 -108.63
REMARK 500 SER A 76 75.12 39.62
REMARK 500 ILE A 82 -73.76 -58.83
REMARK 500 THR A 94 28.26 -71.31
REMARK 500 ASN A 95 46.06 -146.53
REMARK 500 ASN A 100 61.00 -113.20
REMARK 500 THR A 114 -164.01 -72.74
REMARK 500 ASN A 115 -170.54 -36.11
REMARK 500 VAL A 118 46.72 -108.93
REMARK 500 VAL A 120 146.34 -7.67
REMARK 500 THR A 131 43.85 -87.43
REMARK 500 CYS A 179 134.32 -175.15
REMARK 500 ASN A 225 12.44 -68.97
REMARK 500 GLN A 233 48.76 -75.21
REMARK 500 VAL A 234 -7.11 -176.84
REMARK 500 PRO A 253 164.43 -47.28
REMARK 500 ALA A 254 -90.82 -11.19
REMARK 500 ALA A 261 51.76 -92.06
REMARK 500 ARG A 309 162.59 -48.56
REMARK 500 SER A 316 34.03 -92.50
REMARK 500 ASP A 317 31.93 39.16
REMARK 500 SER A 409 179.77 -51.95
REMARK 500 ASP A 411 40.85 -100.14
REMARK 500 GLN A 572 1.52 -58.99
REMARK 500 ALA A 577 152.59 -48.06
REMARK 500 VAL A 598 49.20 -79.19
REMARK 500 PHE A 599 -78.16 -65.78
REMARK 500 LEU A 643 54.25 -62.17
REMARK 500 SER A 647 6.41 -69.78
REMARK 500 PHE A 659 -44.34 79.89
REMARK 500 LYS A 675 -11.71 -44.73
REMARK 500 ALA A 676 91.42 -174.02
REMARK 500 TYR A 678 -62.61 -11.91
REMARK 500 PRO A 682 -51.81 -27.67
REMARK 500 TYR A 684 43.05 -90.14
REMARK 500 ASP A 704 -10.48 95.08
REMARK 500 ALA A 721 -18.83 -49.98
REMARK 500 SER A 726 10.41 -66.77
REMARK 500 SER A 751 155.93 -41.19
REMARK 500 PRO B 134 44.09 -67.79
REMARK 500 GLU B 146 23.48 -71.69
REMARK 500 LEU B 147 -165.83 -47.89
REMARK 500 PRO B 148 53.12 26.52
REMARK 500 PRO B 149 121.72 -25.35
REMARK 500 ILE B 151 -19.93 71.28
REMARK 500 VAL B 162 93.85 -65.91
REMARK 500 ARG B 208 79.72 -151.14
REMARK 500 ASP B 215 15.46 -67.99
REMARK 500 ASP B 218 47.45 35.12
REMARK 500
REMARK 500 THIS ENTRY HAS 92 RAMACHANDRAN OUTLIERS.
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 ZN A 800 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 56 SG
REMARK 620 2 CYS A 61 SG 107.8
REMARK 620 3 CYS A 80 SG 101.2 118.4
REMARK 620 4 CYS A 83 SG 100.9 97.0 129.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 950 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 231 SG
REMARK 620 2 CYS B 234 SG 106.8
REMARK 620 3 CYS B 253 SG 104.5 87.0
REMARK 620 4 CYS B 256 SG 103.8 127.9 124.3
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 ZN A 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 950
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1M2O RELATED DB: PDB
REMARK 900 COMPLEX OF YEAST SEC23 AND SAR1 G-PROTEIN
DBREF 1M2V A 1 768 UNP P15303 SEC23_YEAST 1 768
DBREF 1M2V B 1 926 UNP P40482 SEC24_YEAST 1 926
SEQRES 1 A 768 MET ASP PHE GLU THR ASN GLU ASP ILE ASN GLY VAL ARG
SEQRES 2 A 768 PHE THR TRP ASN VAL PHE PRO SER THR ARG SER ASP ALA
SEQRES 3 A 768 ASN SER ASN VAL VAL PRO VAL GLY CYS LEU TYR THR PRO
SEQRES 4 A 768 LEU LYS GLU TYR ASP GLU LEU ASN VAL ALA PRO TYR ASN
SEQRES 5 A 768 PRO VAL VAL CYS SER GLY PRO HIS CYS LYS SER ILE LEU
SEQRES 6 A 768 ASN PRO TYR CYS VAL ILE ASP PRO ARG ASN SER SER TRP
SEQRES 7 A 768 SER CYS PRO ILE CYS ASN SER ARG ASN HIS LEU PRO PRO
SEQRES 8 A 768 GLN TYR THR ASN LEU SER GLN GLU ASN MET PRO LEU GLU
SEQRES 9 A 768 LEU GLN SER THR THR ILE GLU TYR ILE THR ASN LYS PRO
SEQRES 10 A 768 VAL THR VAL PRO PRO ILE PHE PHE PHE VAL VAL ASP LEU
SEQRES 11 A 768 THR SER GLU THR GLU ASN LEU ASP SER LEU LYS GLU SER
SEQRES 12 A 768 ILE ILE THR SER LEU SER LEU LEU PRO PRO ASN ALA LEU
SEQRES 13 A 768 ILE GLY LEU ILE THR TYR GLY ASN VAL VAL GLN LEU HIS
SEQRES 14 A 768 ASP LEU SER SER GLU THR ILE ASP ARG CYS ASN VAL PHE
SEQRES 15 A 768 ARG GLY ASP ARG GLU TYR GLN LEU GLU ALA LEU THR GLU
SEQRES 16 A 768 MET LEU THR GLY GLN LYS PRO THR GLY PRO GLY GLY ALA
SEQRES 17 A 768 ALA SER HIS LEU PRO ASN ALA MET ASN LYS VAL THR PRO
SEQRES 18 A 768 PHE SER LEU ASN ARG PHE PHE LEU PRO LEU GLU GLN VAL
SEQRES 19 A 768 GLU PHE LYS LEU ASN GLN LEU LEU GLU ASN LEU SER PRO
SEQRES 20 A 768 ASP GLN TRP SER VAL PRO ALA GLY HIS ARG PRO LEU ARG
SEQRES 21 A 768 ALA THR GLY SER ALA LEU ASN ILE ALA SER LEU LEU LEU
SEQRES 22 A 768 GLN GLY CYS TYR LYS ASN ILE PRO ALA ARG ILE ILE LEU
SEQRES 23 A 768 PHE ALA SER GLY PRO GLY THR VAL ALA PRO GLY LEU ILE
SEQRES 24 A 768 VAL ASN SER GLU LEU LYS ASP PRO LEU ARG SER HIS HIS
SEQRES 25 A 768 ASP ILE ASP SER ASP HIS ALA GLN HIS TYR LYS LYS ALA
SEQRES 26 A 768 CYS LYS PHE TYR ASN GLN ILE ALA GLN ARG VAL ALA ALA
SEQRES 27 A 768 ASN GLY HIS THR VAL ASP ILE PHE ALA GLY CYS TYR ASP
SEQRES 28 A 768 GLN ILE GLY MET SER GLU MET LYS GLN LEU THR ASP SER
SEQRES 29 A 768 THR GLY GLY VAL LEU LEU LEU THR ASP ALA PHE SER THR
SEQRES 30 A 768 ALA ILE PHE LYS GLN SER TYR LEU ARG LEU PHE ALA LYS
SEQRES 31 A 768 ASP GLU GLU GLY TYR LEU LYS MET ALA PHE ASN GLY ASN
SEQRES 32 A 768 MET ALA VAL LYS THR SER LYS ASP LEU LYS VAL GLN GLY
SEQRES 33 A 768 LEU ILE GLY HIS ALA SER ALA VAL LYS LYS THR ASP ALA
SEQRES 34 A 768 ASN ASN ILE SER GLU SER GLU ILE GLY ILE GLY ALA THR
SEQRES 35 A 768 SER THR TRP LYS MET ALA SER LEU SER PRO TYR HIS SER
SEQRES 36 A 768 TYR ALA ILE PHE PHE GLU ILE ALA ASN THR ALA ALA ASN
SEQRES 37 A 768 SER ASN PRO MET MET SER ALA PRO GLY SER ALA ASP ARG
SEQRES 38 A 768 PRO HIS LEU ALA TYR THR GLN PHE ILE THR THR TYR GLN
SEQRES 39 A 768 HIS SER SER GLY THR ASN ARG ILE ARG VAL THR THR VAL
SEQRES 40 A 768 ALA ASN GLN LEU LEU PRO PHE GLY THR PRO ALA ILE ALA
SEQRES 41 A 768 ALA SER PHE ASP GLN GLU ALA ALA ALA VAL LEU MET ALA
SEQRES 42 A 768 ARG ILE ALA VAL HIS LYS ALA GLU THR ASP ASP GLY ALA
SEQRES 43 A 768 ASP VAL ILE ARG TRP LEU ASP ARG THR LEU ILE LYS LEU
SEQRES 44 A 768 CYS GLN LYS TYR ALA ASP TYR ASN LYS ASP ASP PRO GLN
SEQRES 45 A 768 SER PHE ARG LEU ALA PRO ASN PHE SER LEU TYR PRO GLN
SEQRES 46 A 768 PHE THR TYR TYR LEU ARG ARG SER GLN PHE LEU SER VAL
SEQRES 47 A 768 PHE ASN ASN SER PRO ASP GLU THR ALA PHE TYR ARG HIS
SEQRES 48 A 768 ILE PHE THR ARG GLU ASP THR THR ASN SER LEU ILE MET
SEQRES 49 A 768 ILE GLN PRO THR LEU THR SER PHE SER MET GLU ASP ASP
SEQRES 50 A 768 PRO GLN PRO VAL LEU LEU ASP SER ILE SER VAL LYS PRO
SEQRES 51 A 768 ASN THR ILE LEU LEU LEU ASP THR PHE PHE PHE ILE LEU
SEQRES 52 A 768 ILE TYR HIS GLY GLU GLN ILE ALA GLN TRP ARG LYS ALA
SEQRES 53 A 768 GLY TYR GLN ASP ASP PRO GLN TYR ALA ASP PHE LYS ALA
SEQRES 54 A 768 LEU LEU GLU GLU PRO LYS LEU GLU ALA ALA GLU LEU LEU
SEQRES 55 A 768 VAL ASP ARG PHE PRO LEU PRO ARG PHE ILE ASP THR GLU
SEQRES 56 A 768 ALA GLY GLY SER GLN ALA ARG PHE LEU LEU SER LYS LEU
SEQRES 57 A 768 ASN PRO SER ASP ASN TYR GLN ASP MET ALA ARG GLY GLY
SEQRES 58 A 768 SER THR ILE VAL LEU THR ASP ASP VAL SER LEU GLN ASN
SEQRES 59 A 768 PHE MET THR HIS LEU GLN GLN VAL ALA VAL SER GLY GLN
SEQRES 60 A 768 ALA
SEQRES 1 B 926 MET SER HIS HIS LYS LYS ARG VAL TYR PRO GLN ALA GLN
SEQRES 2 B 926 LEU GLN TYR GLY GLN ASN ALA THR PRO LEU GLN GLN PRO
SEQRES 3 B 926 ALA GLN PHE MET PRO PRO GLN ASP PRO ALA ALA ALA GLY
SEQRES 4 B 926 MET SER TYR GLY GLN MET GLY MET PRO PRO GLN GLY ALA
SEQRES 5 B 926 VAL PRO SER MET GLY GLN GLN GLN PHE LEU THR PRO ALA
SEQRES 6 B 926 GLN GLU GLN LEU HIS GLN GLN ILE ASP GLN ALA THR THR
SEQRES 7 B 926 SER MET ASN ASP MET HIS LEU HIS ASN VAL PRO LEU VAL
SEQRES 8 B 926 ASP PRO ASN ALA TYR MET GLN PRO GLN VAL PRO VAL GLN
SEQRES 9 B 926 MET GLY THR PRO LEU GLN GLN GLN GLN GLN PRO MET ALA
SEQRES 10 B 926 ALA PRO ALA TYR GLY GLN PRO SER ALA ALA MET GLY GLN
SEQRES 11 B 926 ASN MET ARG PRO MET ASN GLN LEU TYR PRO ILE ASP LEU
SEQRES 12 B 926 LEU THR GLU LEU PRO PRO PRO ILE THR ASP LEU THR LEU
SEQRES 13 B 926 PRO PRO PRO PRO LEU VAL ILE PRO PRO GLU ARG MET LEU
SEQRES 14 B 926 VAL PRO SER GLU LEU SER ASN ALA SER PRO ASP TYR ILE
SEQRES 15 B 926 ARG SER THR LEU ASN ALA VAL PRO LYS ASN SER SER LEU
SEQRES 16 B 926 LEU LYS LYS SER LYS LEU PRO PHE GLY LEU VAL ILE ARG
SEQRES 17 B 926 PRO TYR GLN HIS LEU TYR ASP ASP ILE ASP PRO PRO PRO
SEQRES 18 B 926 LEU ASN GLU ASP GLY LEU ILE VAL ARG CYS ARG ARG CYS
SEQRES 19 B 926 ARG SER TYR MET ASN PRO PHE VAL THR PHE ILE GLU GLN
SEQRES 20 B 926 GLY ARG ARG TRP ARG CYS ASN PHE CYS ARG LEU ALA ASN
SEQRES 21 B 926 ASP VAL PRO MET GLN MET ASP GLN SER ASP PRO ASN ASP
SEQRES 22 B 926 PRO LYS SER ARG TYR ASP ARG ASN GLU ILE LYS CYS ALA
SEQRES 23 B 926 VAL MET GLU TYR MET ALA PRO LYS GLU TYR THR LEU ARG
SEQRES 24 B 926 GLN PRO PRO PRO ALA THR TYR CYS PHE LEU ILE ASP VAL
SEQRES 25 B 926 SER GLN SER SER ILE LYS SER GLY LEU LEU ALA THR THR
SEQRES 26 B 926 ILE ASN THR LEU LEU GLN ASN LEU ASP SER ILE PRO ASN
SEQRES 27 B 926 HIS ASP GLU ARG THR ARG ILE SER ILE LEU CYS VAL ASP
SEQRES 28 B 926 ASN ALA ILE HIS TYR PHE LYS ILE PRO LEU ASP SER GLU
SEQRES 29 B 926 ASN ASN GLU GLU SER ALA ASP GLN ILE ASN MET MET ASP
SEQRES 30 B 926 ILE ALA ASP LEU GLU GLU PRO PHE LEU PRO ARG PRO ASN
SEQRES 31 B 926 SER MET VAL VAL SER LEU LYS ALA CYS ARG GLN ASN ILE
SEQRES 32 B 926 GLU THR LEU LEU THR LYS ILE PRO GLN ILE PHE GLN SER
SEQRES 33 B 926 ASN LEU ILE THR ASN PHE ALA LEU GLY PRO ALA LEU LYS
SEQRES 34 B 926 SER ALA TYR HIS LEU ILE GLY GLY VAL GLY GLY LYS ILE
SEQRES 35 B 926 ILE VAL VAL SER GLY THR LEU PRO ASN LEU GLY ILE GLY
SEQRES 36 B 926 LYS LEU GLN ARG ARG ASN GLU SER GLY VAL VAL ASN THR
SEQRES 37 B 926 SER LYS GLU THR ALA GLN LEU LEU SER CYS GLN ASP SER
SEQRES 38 B 926 PHE TYR LYS ASN PHE THR ILE ASP CYS SER LYS VAL GLN
SEQRES 39 B 926 ILE THR VAL ASP LEU PHE LEU ALA SER GLU ASP TYR MET
SEQRES 40 B 926 ASP VAL ALA SER LEU SER ASN LEU SER ARG PHE THR ALA
SEQRES 41 B 926 GLY GLN THR HIS PHE TYR PRO GLY PHE SER GLY LYS ASN
SEQRES 42 B 926 PRO ASN ASP ILE VAL LYS PHE SER THR GLU PHE ALA LYS
SEQRES 43 B 926 HIS ILE SER MET ASP PHE CYS MET GLU THR VAL MET ARG
SEQRES 44 B 926 ALA ARG GLY SER THR GLY LEU ARG MET SER ARG PHE TYR
SEQRES 45 B 926 GLY HIS PHE PHE ASN ARG SER SER ASP LEU CYS ALA PHE
SEQRES 46 B 926 SER THR MET PRO ARG ASP GLN SER TYR LEU PHE GLU VAL
SEQRES 47 B 926 ASN VAL ASP GLU SER ILE MET ALA ASP TYR CYS TYR VAL
SEQRES 48 B 926 GLN VAL ALA VAL LEU LEU SER LEU ASN ASN SER GLN ARG
SEQRES 49 B 926 ARG ILE ARG ILE ILE THR LEU ALA MET PRO THR THR GLU
SEQRES 50 B 926 SER LEU ALA GLU VAL TYR ALA SER ALA ASP GLN LEU ALA
SEQRES 51 B 926 ILE ALA SER PHE TYR ASN SER LYS ALA VAL GLU LYS ALA
SEQRES 52 B 926 LEU ASN SER SER LEU ASP ASP ALA ARG VAL LEU ILE ASN
SEQRES 53 B 926 LYS SER VAL GLN ASP ILE LEU ALA THR TYR LYS LYS GLU
SEQRES 54 B 926 ILE VAL VAL SER ASN THR ALA GLY GLY ALA PRO LEU ARG
SEQRES 55 B 926 LEU CYS ALA ASN LEU ARG MET PHE PRO LEU LEU MET HIS
SEQRES 56 B 926 SER LEU THR LYS HIS MET ALA PHE ARG SER GLY ILE VAL
SEQRES 57 B 926 PRO SER ASP HIS ARG ALA SER ALA LEU ASN ASN LEU GLU
SEQRES 58 B 926 SER LEU PRO LEU LYS TYR LEU ILE LYS ASN ILE TYR PRO
SEQRES 59 B 926 ASP VAL TYR SER LEU HIS ASP MET ALA ASP GLU ALA GLY
SEQRES 60 B 926 LEU PRO VAL GLN THR GLU ASP GLY GLU ALA THR GLY THR
SEQRES 61 B 926 ILE VAL LEU PRO GLN PRO ILE ASN ALA THR SER SER LEU
SEQRES 62 B 926 PHE GLU ARG TYR GLY LEU TYR LEU ILE ASP ASN GLY ASN
SEQRES 63 B 926 GLU LEU PHE LEU TRP MET GLY GLY ASP ALA VAL PRO ALA
SEQRES 64 B 926 LEU VAL PHE ASP VAL PHE GLY THR GLN ASP ILE PHE ASP
SEQRES 65 B 926 ILE PRO ILE GLY LYS GLN GLU ILE PRO VAL VAL GLU ASN
SEQRES 66 B 926 SER GLU PHE ASN GLN ARG VAL ARG ASN ILE ILE ASN GLN
SEQRES 67 B 926 LEU ARG ASN HIS ASP ASP VAL ILE THR TYR GLN SER LEU
SEQRES 68 B 926 TYR ILE VAL ARG GLY ALA SER LEU SER GLU PRO VAL ASN
SEQRES 69 B 926 HIS ALA SER ALA ARG GLU VAL ALA THR LEU ARG LEU TRP
SEQRES 70 B 926 ALA SER SER THR LEU VAL GLU ASP LYS ILE LEU ASN ASN
SEQRES 71 B 926 GLU SER TYR ARG GLU PHE LEU GLN ILE MET LYS ALA ARG
SEQRES 72 B 926 ILE SER LYS
HET ZN A 800 1
HET ZN B 950 1
HETNAM ZN ZINC ION
FORMUL 3 ZN 2(ZN 2+)
FORMUL 5 HOH *69(H2 O)
HELIX 1 1 ASP A 2 GLY A 11 1 10
HELIX 2 2 THR A 22 ASN A 29 1 8
HELIX 3 3 PRO A 90 THR A 94 5 5
HELIX 4 4 PRO A 102 GLN A 106 5 5
HELIX 5 5 GLU A 133 SER A 149 1 17
HELIX 6 6 GLN A 189 THR A 198 1 10
HELIX 7 7 SER A 223 PHE A 227 5 5
HELIX 8 8 VAL A 234 ASN A 244 1 11
HELIX 9 9 ALA A 261 LYS A 278 1 18
HELIX 10 10 SER A 310 SER A 316 1 7
HELIX 11 11 HIS A 321 GLY A 340 1 20
HELIX 12 12 GLY A 354 THR A 365 1 12
HELIX 13 13 THR A 377 LEU A 387 1 11
HELIX 14 14 THR A 516 SER A 522 1 7
HELIX 15 15 ASP A 524 THR A 542 1 19
HELIX 16 16 ASP A 547 ALA A 564 1 18
HELIX 17 17 LEU A 582 ARG A 591 1 10
HELIX 18 18 SER A 602 THR A 614 1 13
HELIX 19 19 ASP A 617 GLN A 626 1 10
HELIX 20 20 ASP A 644 VAL A 648 5 5
HELIX 21 21 GLY A 667 LYS A 675 1 9
HELIX 22 22 GLY A 677 GLN A 683 5 7
HELIX 23 23 TYR A 684 VAL A 703 1 20
HELIX 24 24 GLN A 720 SER A 726 1 7
HELIX 25 25 SER A 751 VAL A 764 1 14
HELIX 26 26 THR B 63 ILE B 73 1 11
HELIX 27 27 THR B 152 LEU B 156 5 5
HELIX 28 28 PRO B 164 MET B 168 5 5
HELIX 29 29 ASN B 192 LYS B 200 1 9
HELIX 30 30 PRO B 263 ASP B 267 5 5
HELIX 31 31 ASP B 273 ASP B 279 5 7
HELIX 32 32 ARG B 280 CYS B 285 1 6
HELIX 33 33 PRO B 293 THR B 297 5 5
HELIX 34 34 SER B 313 SER B 319 1 7
HELIX 35 35 GLY B 320 ASN B 332 1 13
HELIX 36 36 CYS B 399 PHE B 414 1 16
HELIX 37 37 ALA B 423 GLY B 436 1 14
HELIX 38 38 LYS B 470 LEU B 476 1 7
HELIX 39 39 SER B 481 GLN B 494 1 14
HELIX 40 40 ASP B 508 PHE B 518 1 11
HELIX 41 41 ASN B 533 MET B 550 1 18
HELIX 42 42 SER B 638 SER B 645 1 8
HELIX 43 43 ASP B 647 SER B 666 1 20
HELIX 44 44 LEU B 668 ILE B 690 1 23
HELIX 45 45 ASN B 706 ARG B 708 5 3
HELIX 46 46 MET B 709 LYS B 719 1 11
HELIX 47 47 PRO B 729 LEU B 743 1 15
HELIX 48 48 PRO B 744 TYR B 753 1 10
HELIX 49 49 PRO B 818 PHE B 822 5 5
HELIX 50 50 PHE B 848 LEU B 859 1 12
HELIX 51 51 ARG B 889 THR B 901 1 13
HELIX 52 52 SER B 912 SER B 925 1 14
SHEET 1 1 3 VAL A 33 TYR A 37 0
SHEET 2 1 3 TYR A 456 GLU A 461 -1 O TYR A 456 N TYR A 37
SHEET 3 1 3 LYS A 413 ILE A 418 -1 N LYS A 413 O GLU A 461
SHEET 1 4 8 THR A 109 ILE A 113 0
SHEET 2 4 8 ASN A 500 LEU A 512 -1 O ILE A 502 N TYR A 112
SHEET 3 4 8 PHE A 19 PRO A 20 1 O PHE A 19 N LEU A 512
SHEET 4 4 8 ASN A 500 LEU A 512 1 O GLN A 510 N PHE A 19
SHEET 5 4 8 LEU A 484 GLN A 494 -1 N ALA A 485 O ASN A 509
SHEET 6 4 8 ALA A 399 THR A 408 -1 O PHE A 400 N GLN A 494
SHEET 7 4 8 THR A 444 LEU A 450 -1 N TRP A 445 O MET A 404
SHEET 8 4 8 SER A 422 ALA A 423 -1 O SER A 422 N LYS A 446
SHEET 1 5 2 SER A 77 SER A 79 0
SHEET 2 5 2 ARG A 86 HIS A 88 -1 N ASN A 87 O TRP A 78
SHEET 1 1615 THR A 342 GLY A 348 0
SHEET 2 1615 ALA A 282 ALA A 288 1 O ALA A 282 N THR A 342
SHEET 3 1615 ILE A 123 ASP A 129 1 O ILE A 123 N ARG A 283
SHEET 4 1615 LEU A 156 TYR A 162 1 O LEU A 156 N PHE A 124
SHEET 5 1615 LEU A 229 PRO A 230 -1 O LEU A 229 N ILE A 157
SHEET 6 1615 LEU A 156 TYR A 162 -1 N ILE A 157 O LEU A 229
SHEET 7 1615 VAL A 165 ASP A 170 -1 N GLN A 167 O THR A 161
SHEET 8 1615 ARG A 178 ARG A 183 -1 O ARG A 178 N ASP A 170
SHEET 9 1615 ASN B 374 ILE B 378 1 O MET B 375 N CYS A 179
SHEET 10 1615 ILE B 354 LYS B 358 -1 O ILE B 354 N ILE B 378
SHEET 11 1615 ILE B 347 VAL B 350 -1 O CYS B 349 N HIS B 355
SHEET 12 1615 TYR B 306 ASP B 311 1 O PHE B 308 N LEU B 348
SHEET 13 1615 GLY B 440 SER B 446 1 O LYS B 441 N CYS B 307
SHEET 14 1615 ILE B 495 SER B 503 1 O THR B 496 N ILE B 442
SHEET 15 1615 THR B 523 PRO B 527 1 N HIS B 524 O LEU B 499
SHEET 1 24 1 ASP A 570 ARG A 575 0
SHEET 1 27 4 THR A 628 PHE A 632 0
SHEET 2 27 4 ILE A 653 ASP A 657 -1 O ILE A 653 N PHE A 632
SHEET 3 27 4 PHE A 661 HIS A 666 -1 O LEU A 663 N LEU A 656
SHEET 4 27 4 ARG A 710 GLU A 715 1 O ARG A 710 N ILE A 662
SHEET 1 31 1 ARG B 702 CYS B 704 0
SHEET 1 32 3 GLY B 204 ILE B 207 0
SHEET 2 32 3 TYR B 594 VAL B 600 -1 N TYR B 594 O ILE B 207
SHEET 3 32 3 LEU B 566 TYR B 572 -1 O ARG B 567 N ASN B 599
SHEET 1 35 7 VAL B 287 MET B 291 0
SHEET 2 35 7 GLN B 623 THR B 636 -1 O ILE B 626 N TYR B 290
SHEET 3 35 7 VAL B 189 PRO B 190 1 N VAL B 189 O PRO B 634
SHEET 4 35 7 GLN B 623 THR B 636 1 O PRO B 634 N VAL B 189
SHEET 5 35 7 TYR B 608 LEU B 619 -1 N CYS B 609 O MET B 633
SHEET 6 35 7 CYS B 553 GLY B 562 -1 N MET B 554 O SER B 618
SHEET 7 35 7 LEU B 582 MET B 588 -1 O CYS B 583 N MET B 558
SHEET 1 36 2 ARG B 250 ARG B 252 0
SHEET 2 36 2 ALA B 259 ASP B 261 -1 N ASN B 260 O TRP B 251
SHEET 1 41 1 VAL B 394 SER B 395 0
SHEET 1 56 3 LEU B 799 ASP B 803 0
SHEET 2 56 3 GLU B 807 MET B 812 -1 N PHE B 809 O ILE B 802
SHEET 3 56 3 SER B 870 VAL B 874 1 O SER B 870 N LEU B 808
LINK SG CYS A 56 ZN ZN A 800 1555 1555 2.51
LINK SG CYS A 61 ZN ZN A 800 1555 1555 2.35
LINK SG CYS A 80 ZN ZN A 800 1555 1555 2.43
LINK SG CYS A 83 ZN ZN A 800 1555 1555 2.48
LINK SG CYS B 231 ZN ZN B 950 1555 1555 2.39
LINK SG CYS B 234 ZN ZN B 950 1555 1555 2.39
LINK SG CYS B 253 ZN ZN B 950 1555 1555 2.35
LINK SG CYS B 256 ZN ZN B 950 1555 1555 2.38
CISPEP 1 ALA A 295 PRO A 296 0 -0.26
CISPEP 2 PHE A 706 PRO A 707 0 0.36
SITE 1 AC1 4 CYS A 56 CYS A 61 CYS A 80 CYS A 83
SITE 1 AC2 4 CYS B 231 CYS B 234 CYS B 253 CYS B 256
CRYST1 90.309 126.371 180.200 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 0.011073 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007913 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005549 0.00000
(ATOM LINES ARE NOT SHOWN.)
END