HEADER APOPTOSIS 27-MAY-13 4BPK
TITLE BCL-XL BOUND TO ALPHA BETA PUMA BH3 PEPTIDE 5
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BCL-2-LIKE PROTEIN 1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 1-26,83-209;
COMPND 5 SYNONYM: BCL2-L-1, APOPTOSIS REGULATOR BCL-X, BCL-XL;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: BCL-XL WITHOUT C-TERMINAL DOMAIN OR LOOP BETWEEN ALPHA
COMPND 8 1 AND ALPHA 2 HELICES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: ALPHA BETA BH3-PEPTIDE;
COMPND 11 CHAIN: C, D;
COMPND 12 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_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX6P3;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606
KEYWDS APOPTOSIS
EXPDTA X-RAY DIFFRACTION
AUTHOR B.J.SMITH,E.F.LEE,J.W.CHECCO,S.H.GELLMAN,W.D.FAIRLIE
REVDAT 7 20-DEC-23 4BPK 1 REMARK
REVDAT 6 15-NOV-23 4BPK 1 REMARK LINK ATOM
REVDAT 5 10-JUL-19 4BPK 1 REMARK
REVDAT 4 24-APR-19 4BPK 1 REMARK SEQRES
REVDAT 3 20-JUN-18 4BPK 1 LINK ATOM
REVDAT 2 10-MAY-17 4BPK 1 REMARK
REVDAT 1 09-APR-14 4BPK 0
JRNL AUTH B.J.SMITH,E.F.LEE,J.W.CHECCO,M.EVANGELISTA,S.H.GELLMAN,
JRNL AUTH 2 W.D.FAIRLIE
JRNL TITL STRUCTURE-GUIDED RATIONAL DESIGN OF ALPHA/BETA-PEPTIDE
JRNL TITL 2 FOLDAMERS WITH HIGH AFFINITY FOR BCL-2 FAMILY PROSURVIVAL
JRNL TITL 3 PROTEINS.
JRNL REF CHEMBIOCHEM V. 14 1564 2013
JRNL REFN ISSN 1439-4227
JRNL PMID 23929624
JRNL DOI 10.1002/CBIC.201300351
REMARK 2
REMARK 2 RESOLUTION. 1.76 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.2_1309)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.76
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.07
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 38364
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.221
REMARK 3 R VALUE (WORKING SET) : 0.219
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3620
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 36.0741 - 5.1984 0.94 2528 131 0.2372 0.2477
REMARK 3 2 5.1984 - 4.1280 1.00 2661 142 0.1776 0.1582
REMARK 3 3 4.1280 - 3.6068 1.00 2633 137 0.1707 0.2442
REMARK 3 4 3.6068 - 3.2772 1.00 2696 146 0.2056 0.2227
REMARK 3 5 3.2772 - 3.0425 1.00 2688 137 0.2187 0.2817
REMARK 3 6 3.0425 - 2.8632 1.00 2640 141 0.2083 0.2793
REMARK 3 7 2.8632 - 2.7198 1.00 2680 145 0.2175 0.2713
REMARK 3 8 2.7198 - 2.6015 1.00 2673 144 0.2156 0.2352
REMARK 3 9 2.6015 - 2.5014 1.00 2681 143 0.2232 0.2692
REMARK 3 10 2.5014 - 2.4151 1.00 2652 140 0.2137 0.2450
REMARK 3 11 2.4151 - 2.3396 1.00 2711 144 0.2176 0.2764
REMARK 3 12 2.3396 - 2.2727 1.00 2684 138 0.2237 0.2364
REMARK 3 13 2.2727 - 2.2129 1.00 2646 142 0.2355 0.2903
REMARK 3 14 2.2129 - 2.1589 1.00 2657 136 0.2286 0.2705
REMARK 3 15 2.1589 - 2.1098 1.00 2666 136 0.2503 0.2801
REMARK 3 16 2.1098 - 2.0649 1.00 2696 138 0.2473 0.2484
REMARK 3 17 2.0649 - 2.0236 1.00 2701 148 0.2519 0.3258
REMARK 3 18 2.0236 - 1.9854 1.00 2652 137 0.2611 0.3066
REMARK 3 19 1.9854 - 1.9500 1.00 2666 139 0.2737 0.3296
REMARK 3 20 1.9500 - 1.9169 1.00 2665 142 0.2834 0.3671
REMARK 3 21 1.9169 - 1.8860 1.00 2711 143 0.2667 0.2527
REMARK 3 22 1.8860 - 1.8570 1.00 2646 139 0.2858 0.2823
REMARK 3 23 1.8570 - 1.8297 1.00 2651 142 0.2897 0.3698
REMARK 3 24 1.8297 - 1.8039 0.99 2618 136 0.3116 0.3482
REMARK 3 25 1.8039 - 1.7795 0.98 2668 142 0.3363 0.3245
REMARK 3 26 1.7795 - 1.7564 0.85 2272 112 0.3523 0.3741
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.260
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.920
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.010 2933
REMARK 3 ANGLE : 1.058 3939
REMARK 3 CHIRALITY : 0.064 399
REMARK 3 PLANARITY : 0.004 520
REMARK 3 DIHEDRAL : 16.030 1085
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 18.3088 -27.8496 -12.7689
REMARK 3 T TENSOR
REMARK 3 T11: 0.1376 T22: 0.3573
REMARK 3 T33: 0.1263 T12: 0.0291
REMARK 3 T13: -0.0422 T23: -0.1274
REMARK 3 L TENSOR
REMARK 3 L11: 4.1447 L22: 9.5458
REMARK 3 L33: 1.1506 L12: -4.4369
REMARK 3 L13: 0.8859 L23: -2.0407
REMARK 3 S TENSOR
REMARK 3 S11: -0.2501 S12: -0.4170 S13: 0.4348
REMARK 3 S21: 0.4352 S22: 0.3343 S23: -0.4398
REMARK 3 S31: -0.1077 S32: -0.1191 S33: -0.0167
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4BPK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-MAY-13.
REMARK 100 THE DEPOSITION ID IS D_1290056945.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-AUG-12
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 : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9537
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 198352
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.760
REMARK 200 RESOLUTION RANGE LOW (A) : 3.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.7400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.76
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.82
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.4
REMARK 200 DATA REDUNDANCY IN SHELL : 9.35
REMARK 200 R MERGE FOR SHELL (I) : 0.71000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.390
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 2P1L
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.79
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES, PH7.5 1M SODIUM ACETATE
REMARK 280 50MM CADMIUM SULPHATE
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 32.58750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.28950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.06650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 40.28950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.58750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.06650
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -121.5 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A -3
REMARK 465 PRO A -2
REMARK 465 LEU A -1
REMARK 465 GLY A 0
REMARK 465 GLY A 196
REMARK 465 ASN A 197
REMARK 465 ASN A 198
REMARK 465 ALA A 199
REMARK 465 ALA A 200
REMARK 465 ALA A 201
REMARK 465 GLU A 202
REMARK 465 SER A 203
REMARK 465 ARG A 204
REMARK 465 LYS A 205
REMARK 465 GLY A 206
REMARK 465 GLN A 207
REMARK 465 GLU A 208
REMARK 465 ARG A 209
REMARK 465 GLY B -3
REMARK 465 PRO B -2
REMARK 465 LEU B -1
REMARK 465 GLY B 0
REMARK 465 MET B 1
REMARK 465 GLY B 196
REMARK 465 ASN B 197
REMARK 465 ASN B 198
REMARK 465 ALA B 199
REMARK 465 ALA B 200
REMARK 465 ALA B 201
REMARK 465 GLU B 202
REMARK 465 SER B 203
REMARK 465 ARG B 204
REMARK 465 LYS B 205
REMARK 465 GLY B 206
REMARK 465 GLN B 207
REMARK 465 GLU B 208
REMARK 465 ARG B 209
REMARK 465 ACE C -1
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLN A 3 CG CD OE1 NE2
REMARK 480 GLN A 121 OE1 NE2
REMARK 480 ARG B 102 CG CD NE
REMARK 480 GLN B 121 CD OE1 NE2
REMARK 480 GLU B 153 CG CD OE1 OE2
REMARK 480 LYS B 157 CB CG CD CE NZ
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 OF1 B3E D 4 O HOH D 2001 2.11
REMARK 500 OD1 ASN A 175 ND2 ASN B 5 2.12
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 B3Q C 8 C - N - CA ANGL. DEV. = -18.7 DEGREES
REMARK 500 B3Q C 8 C - N - CA ANGL. DEV. = -15.8 DEGREES
REMARK 500 B3D C 15 C - N - CA ANGL. DEV. = -21.0 DEGREES
REMARK 500 ACE D -1 O - C - N ANGL. DEV. = -16.5 DEGREES
REMARK 500 B3E D 4 C - N - CA ANGL. DEV. = -15.1 DEGREES
REMARK 500 B3D D 15 C - N - CA ANGL. DEV. = -20.7 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 HIS A 177 -0.13 -140.05
REMARK 500 HR7 C 11 -69.79 -24.62
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 B3E C 4 ILE C 5 148.56
REMARK 500 B3Q C 8 AHP C 9 145.47
REMARK 500 B3Q C 8 AHP C 9 147.25
REMARK 500 B3E D 4 ILE D 5 145.94
REMARK 500 B3Q D 8 AHP D 9 149.37
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 B3E C 4 -17.20
REMARK 500 B3Q C 8 -16.68
REMARK 500 B3Q C 8 -15.86
REMARK 500 B3A C 18 -18.53
REMARK 500 B3E D 4 -15.91
REMARK 500 B3Q D 8 -16.16
REMARK 500 B3A D 18 -19.75
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH C2002 DISTANCE = 6.16 ANGSTROMS
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 CD A1197 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 92 OE2
REMARK 620 2 HOH A2023 O 96.1
REMARK 620 3 HOH A2042 O 81.4 173.3
REMARK 620 4 HOH A2043 O 99.7 73.6 100.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A1196 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 129 OE1
REMARK 620 2 GLU A 129 OE2 52.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A1196 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 129 OE2
REMARK 620 2 GLU A 158 OE2 44.9
REMARK 620 3 HOH A2059 O 93.0 48.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A1199 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 153 OE1
REMARK 620 2 GLU A 153 OE2 55.3
REMARK 620 3 HOH A2051 O 89.9 80.8
REMARK 620 4 HOH A2064 O 89.5 117.7 156.2
REMARK 620 5 HOH A2065 O 78.6 133.1 92.3 64.3
REMARK 620 6 HOH A2066 O 155.1 103.0 98.8 91.6 123.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A1201 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 179 OE2
REMARK 620 2 HOH A2068 O 107.4
REMARK 620 3 HOH A2069 O 63.8 165.2
REMARK 620 4 GLU B 124 OE1 114.0 132.2 51.5
REMARK 620 5 GLU B 124 OE2 116.6 129.6 54.2 2.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD B1197 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 186 O
REMARK 620 2 ASP B 176 OD1 115.9
REMARK 620 3 ASP B 176 OD2 118.9 3.3
REMARK 620 4 HOH B2058 O 116.8 3.8 5.5
REMARK 620 5 HOH B2073 O 118.5 6.2 7.1 2.6
REMARK 620 6 HOH B2074 O 117.5 2.5 3.7 1.8 3.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD B1199 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 92 OE2
REMARK 620 2 HOH B2012 O 84.0
REMARK 620 3 HOH B2026 O 75.1 71.5
REMARK 620 4 HOH B2075 O 158.6 114.7 100.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD B1201 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 153 OE1
REMARK 620 2 ASP B 156 OD2 82.7
REMARK 620 3 HOH B2053 O 121.2 117.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD B1198 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 177 NE2
REMARK 620 2 HOH B2059 O 96.6
REMARK 620 3 HOH B2060 O 106.4 83.1
REMARK 620 4 HOH B2063 O 70.5 161.4 87.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD B1196 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY B 186 O
REMARK 620 2 ASP B 189 OD1 70.3
REMARK 620 3 ASP B 189 OD2 80.4 54.9
REMARK 620 N 1 2
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 1196
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 1197
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 1198
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1196
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1197
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1198
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1199
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 1199
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 1200
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1200
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 1202
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 1203
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 1204
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1205
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1202
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4BPI RELATED DB: PDB
REMARK 900 MCL-1 BOUND TO ALPHA BETA PUMA BH3 PEPTIDE 2
REMARK 900 RELATED ID: 4BPJ RELATED DB: PDB
REMARK 900 MCL-1 BOUND TO ALPHA BETA PUMA BH3 PEPTIDE 3
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 DELETION MUTANT CONTAINING RESIDUES 1-40 AND 81-209
REMARK 999 DELETION REMOVES 41-80 AND 210-233
DBREF 4BPK A 1 26 UNP Q07817 B2CL1_HUMAN 1 26
DBREF 4BPK A 83 209 UNP Q07817 B2CL1_HUMAN 83 209
DBREF 4BPK B 1 26 UNP Q07817 B2CL1_HUMAN 1 26
DBREF 4BPK B 83 209 UNP Q07817 B2CL1_HUMAN 83 209
DBREF 4BPK C -1 21 PDB 4BPK 4BPK -1 21
DBREF 4BPK D -1 21 PDB 4BPK 4BPK -1 21
SEQADV 4BPK GLY A -3 UNP Q07817 EXPRESSION TAG
SEQADV 4BPK PRO A -2 UNP Q07817 EXPRESSION TAG
SEQADV 4BPK LEU A -1 UNP Q07817 EXPRESSION TAG
SEQADV 4BPK GLY A 0 UNP Q07817 EXPRESSION TAG
SEQADV 4BPK GLY B -3 UNP Q07817 EXPRESSION TAG
SEQADV 4BPK PRO B -2 UNP Q07817 EXPRESSION TAG
SEQADV 4BPK LEU B -1 UNP Q07817 EXPRESSION TAG
SEQADV 4BPK GLY B 0 UNP Q07817 EXPRESSION TAG
SEQRES 1 A 157 GLY PRO LEU GLY MET SER GLN SER ASN ARG GLU LEU VAL
SEQRES 2 A 157 VAL ASP PHE LEU SER TYR LYS LEU SER GLN LYS GLY TYR
SEQRES 3 A 157 SER TRP SER GLN MET ALA ALA VAL LYS GLN ALA LEU ARG
SEQRES 4 A 157 GLU ALA GLY ASP GLU PHE GLU LEU ARG TYR ARG ARG ALA
SEQRES 5 A 157 PHE SER ASP LEU THR SER GLN LEU HIS ILE THR PRO GLY
SEQRES 6 A 157 THR ALA TYR GLN SER PHE GLU GLN VAL VAL ASN GLU LEU
SEQRES 7 A 157 PHE ARG ASP GLY VAL ASN TRP GLY ARG ILE VAL ALA PHE
SEQRES 8 A 157 PHE SER PHE GLY GLY ALA LEU CYS VAL GLU SER VAL ASP
SEQRES 9 A 157 LYS GLU MET GLN VAL LEU VAL SER ARG ILE ALA ALA TRP
SEQRES 10 A 157 MET ALA THR TYR LEU ASN ASP HIS LEU GLU PRO TRP ILE
SEQRES 11 A 157 GLN GLU ASN GLY GLY TRP ASP THR PHE VAL GLU LEU TYR
SEQRES 12 A 157 GLY ASN ASN ALA ALA ALA GLU SER ARG LYS GLY GLN GLU
SEQRES 13 A 157 ARG
SEQRES 1 B 157 GLY PRO LEU GLY MET SER GLN SER ASN ARG GLU LEU VAL
SEQRES 2 B 157 VAL ASP PHE LEU SER TYR LYS LEU SER GLN LYS GLY TYR
SEQRES 3 B 157 SER TRP SER GLN MET ALA ALA VAL LYS GLN ALA LEU ARG
SEQRES 4 B 157 GLU ALA GLY ASP GLU PHE GLU LEU ARG TYR ARG ARG ALA
SEQRES 5 B 157 PHE SER ASP LEU THR SER GLN LEU HIS ILE THR PRO GLY
SEQRES 6 B 157 THR ALA TYR GLN SER PHE GLU GLN VAL VAL ASN GLU LEU
SEQRES 7 B 157 PHE ARG ASP GLY VAL ASN TRP GLY ARG ILE VAL ALA PHE
SEQRES 8 B 157 PHE SER PHE GLY GLY ALA LEU CYS VAL GLU SER VAL ASP
SEQRES 9 B 157 LYS GLU MET GLN VAL LEU VAL SER ARG ILE ALA ALA TRP
SEQRES 10 B 157 MET ALA THR TYR LEU ASN ASP HIS LEU GLU PRO TRP ILE
SEQRES 11 B 157 GLN GLU ASN GLY GLY TRP ASP THR PHE VAL GLU LEU TYR
SEQRES 12 B 157 GLY ASN ASN ALA ALA ALA GLU SER ARG LYS GLY GLN GLU
SEQRES 13 B 157 ARG
SEQRES 1 C 22 ACE HT7 ALA ARG B3E ILE GLY ALA B3Q AHP ARG HR7 MET
SEQRES 2 C 22 ALA ASP B3D LEU ASN B3A GLN TYR NH2
SEQRES 1 D 22 ACE HT7 ALA ARG B3E ILE GLY ALA B3Q AHP ARG HR7 MET
SEQRES 2 D 22 ALA ASP B3D LEU ASN B3A GLN TYR NH2
MODRES 4BPK HT7 C 1 TRP
MODRES 4BPK B3E C 4 GLU (3S)-3-AMINOHEXANEDIOIC ACID
MODRES 4BPK AHP C 9 ALA 2-AMINO-HEPTANOIC ACID
MODRES 4BPK HR7 C 11 ARG
MODRES 4BPK B3D C 15 ASP 3-AMINOPENTANEDIOIC ACID
MODRES 4BPK B3A C 18 ALA (3S)-3-AMINOBUTANOIC ACID
MODRES 4BPK HT7 D 1 TRP
MODRES 4BPK B3E D 4 GLU (3S)-3-AMINOHEXANEDIOIC ACID
MODRES 4BPK AHP D 9 ALA 2-AMINO-HEPTANOIC ACID
MODRES 4BPK HR7 D 11 ARG
MODRES 4BPK B3D D 15 ASP 3-AMINOPENTANEDIOIC ACID
MODRES 4BPK B3A D 18 ALA (3S)-3-AMINOBUTANOIC ACID
HET HT7 C 1 15
HET B3E C 4 10
HET B3Q C 8 17
HET AHP C 9 9
HET HR7 C 11 12
HET B3D C 15 8
HET B3A C 18 6
HET NH2 C 21 1
HET ACE D -1 3
HET HT7 D 1 15
HET B3E D 4 10
HET B3Q D 8 10
HET AHP D 9 9
HET HR7 D 11 12
HET B3D D 15 8
HET B3A D 18 6
HET NH2 D 21 1
HET CD A1196 2
HET CD A1197 1
HET CD A1198 1
HET CD A1199 1
HET CD A1200 2
HET CD A1201 1
HET EDO A1202 4
HET CD B1196 1
HET CD B1197 1
HET CD B1198 1
HET CD B1199 1
HET CD B1200 2
HET CD B1201 1
HET CD B1202 1
HET CD B1203 1
HET CD B1204 2
HET EDO B1205 4
HETNAM HT7 (3S)-3-AMINO-4-(1H-INDOL-3-YL)BUTANOIC ACID
HETNAM B3E (3S)-3-AMINOHEXANEDIOIC ACID
HETNAM B3Q (3S)-3,6-DIAMINO-6-OXOHEXANOIC ACID
HETNAM AHP 2-AMINO-HEPTANOIC ACID
HETNAM HR7 (3S)-3-AMINO-6-[(DIAMINOMETHYLIDENE)AMINO]HEXANOIC ACID
HETNAM B3D 3-AMINOPENTANEDIOIC ACID
HETNAM B3A (3S)-3-AMINOBUTANOIC ACID
HETNAM NH2 AMINO GROUP
HETNAM ACE ACETYL GROUP
HETNAM CD CADMIUM ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN HT7 BETA-HOMOTRYPTOPHAN
HETSYN B3Q (S)-BETA-3-HOMOGLUTAMINE
HETSYN HR7 BETA-HOMOARGININE
HETSYN B3D BETA-HOMOASPARTATE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 HT7 2(C12 H14 N2 O2)
FORMUL 3 B3E 2(C6 H11 N O4)
FORMUL 3 B3Q 2(C6 H12 N2 O3)
FORMUL 3 AHP 2(C7 H15 N O2)
FORMUL 3 HR7 2(C7 H16 N4 O2)
FORMUL 3 B3D 2(C5 H9 N O4)
FORMUL 3 B3A 2(C4 H9 N O2)
FORMUL 3 NH2 2(H2 N)
FORMUL 4 ACE C2 H4 O
FORMUL 5 CD 15(CD 2+)
FORMUL 11 EDO 2(C2 H6 O2)
FORMUL 22 HOH *151(H2 O)
HELIX 1 1 MET A 1 LYS A 20 1 20
HELIX 2 2 SER A 25 TYR A 101 1 21
HELIX 3 3 TYR A 101 SER A 110 1 10
HELIX 4 4 THR A 118 PHE A 131 1 14
HELIX 5 5 ASN A 136 LYS A 157 1 22
HELIX 6 6 VAL A 161 LEU A 178 1 18
HELIX 7 7 LEU A 178 ASN A 185 1 8
HELIX 8 8 GLY A 187 TYR A 195 1 9
HELIX 9 9 SER B 2 LYS B 20 1 19
HELIX 10 10 SER B 25 TYR B 101 1 21
HELIX 11 11 TYR B 101 SER B 110 1 10
HELIX 12 12 THR B 118 PHE B 131 1 14
HELIX 13 13 ASN B 136 LYS B 157 1 22
HELIX 14 14 VAL B 161 LEU B 178 1 18
HELIX 15 15 LEU B 178 ASN B 185 1 8
HELIX 16 16 GLY B 186 TYR B 195 1 10
HELIX 17 17 HT7 C 1 ARG C 10 1 10
HELIX 18 18 MET C 12 ASN C 17 1 6
HELIX 19 19 HT7 D 1 ARG D 10 1 10
HELIX 20 20 MET D 12 ASN D 17 1 6
LINK C HT7 C 1 N ALA C 2 1555 1555 1.33
LINK C ARG C 3 N B3E C 4 1555 1555 1.33
LINK C B3E C 4 N ILE C 5 1555 1555 1.33
LINK C ALA C 7 N B3Q C 8 1555 1555 1.33
LINK C B3Q C 8 N AHP C 9 1555 1555 1.34
LINK C AHP C 9 N ARG C 10 1555 1555 1.33
LINK C ARG C 10 N HR7 C 11 1555 1555 1.33
LINK C HR7 C 11 N MET C 12 1555 1555 1.34
LINK C ASP C 14 N B3D C 15 1555 1555 1.33
LINK C B3D C 15 N LEU C 16 1555 1555 1.33
LINK C ASN C 17 N B3A C 18 1555 1555 1.33
LINK C B3A C 18 N GLN C 19 1555 1555 1.33
LINK C TYR C 20 N NH2 C 21 1555 1555 1.33
LINK C ACE D -1 N HT7 D 1 1555 1555 1.33
LINK C HT7 D 1 N ALA D 2 1555 1555 1.33
LINK C ARG D 3 N B3E D 4 1555 1555 1.33
LINK C B3E D 4 N ILE D 5 1555 1555 1.33
LINK C ALA D 7 N B3Q D 8 1555 1555 1.33
LINK C B3Q D 8 N AHP D 9 1555 1555 1.34
LINK C AHP D 9 N ARG D 10 1555 1555 1.33
LINK C ARG D 10 N HR7 D 11 1555 1555 1.33
LINK C HR7 D 11 N MET D 12 1555 1555 1.33
LINK C ASP D 14 N B3D D 15 1555 1555 1.33
LINK C B3D D 15 N LEU D 16 1555 1555 1.34
LINK C ASN D 17 N B3A D 18 1555 1555 1.33
LINK C B3A D 18 N GLN D 19 1555 1555 1.33
LINK C TYR D 20 N NH2 D 21 1555 1555 1.33
LINK OE2 GLU A 92 CD CD A1197 1555 1555 2.36
LINK OE1 GLU A 129 CD B CD A1196 1555 1555 2.54
LINK OE2 GLU A 129 CD A CD A1196 1555 1555 2.41
LINK OE2 GLU A 129 CD B CD A1196 1555 1555 2.39
LINK OE1 GLU A 153 CD CD A1199 1555 1555 2.32
LINK OE2 GLU A 153 CD CD A1199 1555 1555 2.40
LINK OE2 GLU A 158 CD A CD A1196 1555 3544 2.44
LINK OE2 GLU A 179 CD CD A1201 1555 1555 2.37
LINK O GLY A 186 CD CD B1197 1555 3654 2.33
LINK CD A CD A1196 O HOH A2059 1555 1555 2.52
LINK CD CD A1197 O HOH A2023 1555 1555 2.45
LINK CD CD A1197 O HOH A2042 1555 1555 2.34
LINK CD CD A1197 O HOH A2043 1555 1555 2.39
LINK CD CD A1199 O HOH A2051 1555 1555 2.39
LINK CD CD A1199 O HOH A2064 1555 1555 2.40
LINK CD CD A1199 O HOH A2065 1555 1555 2.39
LINK CD CD A1199 O HOH A2066 1555 1555 2.59
LINK CD CD A1201 O HOH A2068 1555 1555 2.25
LINK CD CD A1201 O HOH A2069 1555 1555 2.24
LINK CD CD A1201 OE1 GLU B 124 3644 1555 2.47
LINK CD CD A1201 OE2 GLU B 124 3644 1555 2.40
LINK OE2 GLU B 92 CD CD B1199 1555 1555 2.31
LINK OE2 GLU B 129 CD B CD B1200 1555 1555 2.65
LINK OE1 GLU B 153 CD CD B1201 1555 1555 2.40
LINK OD2 ASP B 156 CD CD B1201 1555 1555 2.53
LINK OD1 ASP B 176 CD CD B1197 1555 1555 2.55
LINK OD2 ASP B 176 CD CD B1197 1555 1555 2.55
LINK NE2 HIS B 177 CD CD B1198 1555 1555 2.37
LINK O GLY B 186 CD CD B1196 1555 1555 2.58
LINK OD1 ASP B 189 CD CD B1196 1555 1555 2.38
LINK OD2 ASP B 189 CD CD B1196 1555 1555 2.39
LINK CD CD B1197 O HOH B2058 1555 1555 2.33
LINK CD CD B1197 O HOH B2073 1555 1555 2.33
LINK CD CD B1197 O HOH B2074 1555 1555 2.44
LINK CD CD B1198 O HOH B2059 1555 1555 2.37
LINK CD CD B1198 O HOH B2060 1555 1555 2.48
LINK CD CD B1198 O HOH B2063 1555 1555 2.48
LINK CD CD B1199 O HOH B2012 1555 1555 2.38
LINK CD CD B1199 O HOH B2026 1555 1555 2.38
LINK CD CD B1199 O HOH B2075 1555 1555 2.69
LINK CD A CD B1200 OF2 B3E D 4 1555 1555 2.68
LINK CD CD B1201 O HOH B2053 1555 1555 2.40
LINK CD A CD B1204 O HOH B2076 1555 1555 2.46
LINK CD B CD B1204 O HOH B2076 1555 1555 2.46
SITE 1 AC1 3 GLY B 186 ASP B 189 HOH B2069
SITE 1 AC2 6 GLY A 186 ASP A 189 ASP B 176 HOH B2058
SITE 2 AC2 6 HOH B2073 HOH B2074
SITE 1 AC3 4 HIS B 177 HOH B2059 HOH B2060 HOH B2063
SITE 1 AC4 3 GLU A 129 GLU A 158 HOH A2059
SITE 1 AC5 4 GLU A 92 HOH A2023 HOH A2042 HOH A2043
SITE 1 AC6 1 HIS A 113
SITE 1 AC7 5 GLU A 153 HOH A2051 HOH A2064 HOH A2065
SITE 2 AC7 5 HOH A2066
SITE 1 AC8 5 GLN B 88 GLU B 92 HOH B2012 HOH B2026
SITE 2 AC8 5 HOH B2075
SITE 1 AC9 3 GLU B 129 ARG D 3 B3E D 4
SITE 1 BC1 3 ASP B 156 HOH B2052 HOH B2053
SITE 1 BC2 1 HIS A 177
SITE 1 BC3 2 HIS B 113 B3D C 15
SITE 1 BC4 2 HIS B 113 B3D C 15
SITE 1 BC5 2 GLU B 158 HOH B2076
SITE 1 BC6 4 GLU A 179 HOH A2068 HOH A2069 GLU B 124
SITE 1 BC7 4 ASN B 136 HOH B2047 HOH B2077 HOH B2078
SITE 1 BC8 4 GLN A 88 ARG A 91 ASP B 11 ARG B 91
CRYST1 65.175 72.133 80.579 90.00 90.00 90.00 P 21 21 21 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 0.015343 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013863 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012410 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
